BioQuakes

AP Biology class blog for discussing current research in Biology

Tag: Virus (Page 1 of 3)

Secretive Bacteria: A Revolutionary Discovery in Bacteria

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On April 7, 2025

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For decades, scientists believed that genetic code was like an open book. They believed that each gene is neatly stored in the chromosomes. However, a groundbreaking study from Columbia University has flipped this idea on its head. Researchers have discovered that bacteria can create free-floating, ephemeral genes, or genes that don’t permanently reside in the genome but still play important roles in survival. This raises important questions. Could similar floating genes exist in humans, hidden from our current understanding of genetics? If so, this discovery could change how we think about genetic information, evolution, and gene therapy.

Bacterias

The research, led by Samuel Sternberg and Stephen Tang, focused on an unusual bacterial defense system against viral infections. Instead of cutting up viral DNA, like the well-known CRISPR system, this new defense involved an enzyme called reverse transcriptase, which synthesizes DNA from an RNA template. 

Using a new experimental technique, the researchers found that this enzyme repeatedly copied a small loop of RNA, producing long, repetitive strands of DNA. At first, they thought it was a mistake, but after more digging, they realized that this mysterious DNA was actually a functioning, temporary gene that played a vital role in stopping viral infections. When bacteria were exposed to viruses, this free-floating DNA made a protective protein that prevented viral replication, acting as a defense shield.

This discovery challenges the traditional understanding of molecular biology, which states that genetic instructions flow in a plain sequence from DNA to RNA to protein. The existence of genes that function without being permanently stored in chromosomes could mean that our understanding of the human genome is incomplete. It raises the possibility that humans might also have hidden genetic instructions that only appear under certain conditions. If such genes exist, they could provide insight into diseases, immune responses, or even the evolution of complex life.

The study also has implications for gene therapy. CRISPR, a revolutionary gene-editing tool, has already transformed medicine by allowing scientists to cut DNA precisely. However, it has limitations because even though it can remove or disable genes, it cannot efficiently add new genetic material. The bacterial reverse transcriptase described in this study could help overcome this hurdle by allowing researchers to “write” new DNA sequences directly into the genome, leading to more advanced genetic treatments for diseases.

In AP Biology, we learned about gene expression and regulation, including how DNA is transcribed into RNA and then translated into proteins. This study challenges that structure by showing that genetic information isn’t always locked inside chromosomes. Gene regulation is complex and involves transcription factors, promoters, and enhancers, which determine when and how much of a gene is expressed. The discovery of floating genes suggests that gene expression might be even more involved, with certain genetic instructions appearing only when needed. This discovery also ties into endosymbiotic theory, which explains how some of our cellular structures, like mitochondria, originated from ancient bacterial ancestors. This theory proposes that early eukaryotic cells engulfed bacteria that eventually became permanent parts of the cell. The idea that bacteria have temporary genes that can be activated when needed suggests that early life forms may have exchanged more genetic material than we’ve previously thought. 

If free-floating genes exist in bacteria, could they exist in humans? What if our cells produce hidden genetic instructions in response to environmental triggers? Could these genes hold the key to curing genetic disorders?

What do you think? Could hidden genes in human cells play a role in health and disease? Drop your thoughts in the comments!



COVID-19 Pneumonia: A Lasting Impact on the Lungs

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On December 16, 2024

In Student Post

COVID-19 pneumonia occurs when the SARS-CoV-2 virus causes severe inflammation in the lungs, leading to symptoms like difficulty breathing, low oxygen levels, and persistent coughing. In serious cases, the infection damages the tiny air sacs (alveoli) in the lungs, making it harder for oxygen to pass into the bloodstream. This condition can require hospitalization and even mechanical ventilation to help patients breathe. While many patients recover fully, a significant number experience long-term effects or long term COVID-19 pneumonia, even years after infection. These effects are especially concerning for those who had severe pneumonia, as their lungs often suffer from fibrosis—scarring that makes it harder for the lungs to expand and contract properly.

Recent studies have shown that about half of patients who were hospitalized with COVID-19 pneumonia still have lung abnormalities like ground-glass opacities (hazy spots on CT scans) and areas of scarring more than a year after recovery. These changes can cause ongoing symptoms such as reduced lung function and trouble breathing, affecting daily life.

 

Fibrosis is the main cause for long-terSARS-CoV-2 without backgroundm lung damage, and it forms when the body’s immune response to COVID-19 pneumonia becomes excessive. When the immune system encounters severe inflammation, it attempts to repair the damage by producing fibrous connective tissue. However, an overactive immune response can result in too much fibrous connective tissue being deposited, which alters the lung’s structure. The stiffened lung tissue makes it difficult for oxygen to pass efficiently into the bloodstream, which can lead to shortness of breath and reduced exercise capacity.

Similarly, in AP Biology when inflammation as an immune response becomes excessive it can become harmful in the long term. Furthermore, oftentimes when the body overreacts to pathogens the body can be negatively affected. A fever as an immune response can also be harmful because as pathogens can die from the high heat, the enzymes in our body can also denature. This loss of structure leads to function loss, which has implications for our energy levels. For example, the denaturation of enzymes involved in cellular respiration  causes essential energy processes to slow. 

Understanding the long-term effects of COVID-19 pneumonia is critical as researchers work to develop treatments that target scarring and improve lung health. These advancements could offer relief to the many patients still grappling with the lingering impacts of this disease, giving them a better chance at full recovery. As a recent patient of pneumonia, I’ve understood its complexity and danger!

Needles No More: Testing A New Intranasal Vaccine for COVID-19

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On December 16, 2024

In Student Post

Have needles always freaked you out? Does going to the doctor for an influenza vaccine, “flu shot,” cause you to tense up or feel anxious? You are not alone, as needles have very frequently been the reason why so many individuals — myself included — are often reluctant to get the necessary vaccines to stay protected against a plethora of viruses. However, new research from Griffith University has led to the development of an intranasal vaccine for COVID-19, eliminating the need for a direct injection to get the vaccine for the deadly SARS-CoV-2 virus.

A person, wearing gloves and a surgical mask, handles a COVID-19 Vaccine vial and syringe

A person, wearing gloves, protective glasses, and a surgical mask, handling a COVID-19 vaccine vial and syringe.

For the past four years, Professor Suresh Mahalingam and his team have been conducting research on this vaccine. From his research, he confidently shares that this intranasal vaccine has been found to have no adverse side effects, short or long-term, and is “designed to be administered intranasally, thereby inducing potential mucosal immunity as well as systemic immunity with just a single dose.”

Along these lines, Science Direct highlights the significance of vaccines having both mucosal and systematic immunity, clearly defining each type of immunity as well:

Most human pathogens initiate infection through mucosal portals of entry—the respiratory, gastrointestinal, and genitourinary tracts. Therefore, inducing protective immune responses by administering vaccines directly at the mucosa would be an ideal approach. Mucosal immunity can prevent these infections. In contrast, systemic immunity clears infection only after successful invasion, by limiting replication and destroying the pathogens. Ideally, both mucosal and systemic immunity should be raised against targeted pathogens.

Mahalingam’s research has also shown the immense benefits of live-attenuated vaccines like this one, as “they induce potent and long-lived humoral and cellular immunity, often with just a single dose.” According to Pfizer, “Live-attenuated vaccines contain live pathogens from either a bacteria or a virus that have been ‘attenuated,’ or weakened.” This new intranasal vaccine, CDO-7N-1, has so far been able to provide broad immunity against all major variants of COVID-19, including having a neutralizing capacity for SARS-CoV-1.

While the mRNA COVID-19 vaccines created by Pfizer-BioNTech and Moderna only target spike (S) proteins for specific variants of COVID-19, CDO-7N-1 offers immunity to “all major SARS-CoV-2 proteins and is highly effective against all major variants to date.” This means that this intranasal vaccine can ensure protection against reinfection and virus transmission, preventing the vaccine from spreading further.

Schematic structure of SARS-CoV-2

Labeled structure diagram of SARS-CoV-2

In fact, CDO-7N-1 even remains stable at 4°C for up to seven months, allowing the vaccine to be more accessible to low- and middle-income countries without the necessary infrastructure to store the vaccines in a highly controlled environment.

Specifically, as we’ve learned recently in AP Biology, our bodies’ immune systems have adaptive immunity responses that protect us after exposure to pathogens such as COVID-19. These responses ultimately rely on two types of white blood cells called lymphocytes: T-lymphocytes (“T cells”) and B-lymphocytes (“B Cells”). T cells and B cells function as both a cell-mediated response and a humoral response, respectively, to target infected cells and the invading pathogen.

With an injected COVID-19 vaccine, as the vaccine enters your body and passes through the immune system, T cells and B cells are stimulated and remain in your body in preparation in case you become infected with COVID-19. This same process applies to the CDO-7N-1 vaccine and other nasal vaccines, as the same lymphocytes will remain in the body to fight off the pathogen when present.

Closeup of a doctor’s hands, vaccine, and receiving arm for injection

As of recently, CDO-7N-1 is still on route to complete several rounds of clinical trials before it is officially released for public use, yet Professor Mahalingam’s research has shown the vaccine’s promising results for helping to usher in a new generation of COVID-19 vaccines free of needle injections.

Perhaps in the upcoming months, we will no longer need to extend our arms for vaccines but instead be ready to inhale them!

Could Gene Editing be the Key to Perpetual Virus Resistance?

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On May 3, 2024

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Influenza viruses have spread rapidly despite the vaccines many of us, humans, get (I, for one, just had the flu despite being vaccinated). Vaccines help our bodies recognize certain pathogens and create baseline antibodies to help neutralize them, but, as I learned in AP Bio class, mutations randomly happen. Not only is this genetic variation the key to natural selection in nature, but also for viruses (though viruses also often use the recombination process). As host organisms work as the viruses’ environment that they are trying to survive and reproduce in, natural selection could choose the viruses with mutations that are not recognized by our immune system from the vaccine and potentially create a new virus strand our vaccine is ineffective against.

Potentially more effective and permanent than vaccines, scientists are now exploring gene editing. A step up from the human interference in artifical selection that we learned in AP Bio, where humans choose to breed organisms with specifc traits to create ideal offspring, gene editing changes the organisms themselves. Typically thought of with genetically modified organisms (GMO) referring to plants and plant-based foods, gene editing can also be done on animals.

Take, for example, genetically-modified chickens that protect against avian influenza infections that have run throughout poultry farms at devastating costs. Since the ANP32A gene in chickens codes for the protein that influenza viruses rely on to successfully hijack cells, scientists edited that gene with CRISPR molecular scissors. As the protein is absolutely essential to the virus hijacking chicken cells, no simple mutations should be enough to override the gene editing; thus, chickens should theoretically be permanently resistant to the virus.

CRISPR-Cas9 Editing of the Genome (26453307604).jpg

In multiple studies done, this permanent resistance was almost the case: every typical chicken got the flu when closely exposed to high levels of it (at least 1000 infectious particles), whereas genetically-modifed chickens very rarely got it. In the first study, ten out of ten typical chickens got it, while just one out of 10 edited chickens got it and also at a lower level. In another experiment with an astounding 1 million infectous particles in two separate incubators, all of the typical chickens got it in both incubators and none of the modified chicken got it in one of the incubators, but five out of ten got it in the other. As it turns out, viruses in the latter incubator adapted to use proteins very similar to the protein the edited gene eliminated. There are two proteins very similar to the eliminated protein in chickens, so, to create full flu resistance in chickens, those two genes would need to be edited as well, researchers confirmed. However, editing those genes may hurt chicken development.

Chickens are everywhere, vital to many people’s diet, and can pass the flu to pigs and even us. If we can make chickens resistant to the flu, it could do us and our world wonders — plus, who knows where we will go from there!? Thus, I believe researchers should focus on figuring out if they can edit those three genes in chickens without hurting their development and how to create resistance with this incredible gene-editing ability if not.

We need to make use of our incredible technologies to limit illnesses and improve society; do you have any thoughts on gene editing or possibly even how we can maximize its potential to practically accomplish this task?

“4′-FlU” – The Future of Flu Fighting!

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On February 27, 2024

In Student Post

This study conducted by researchers at Georgia State University’s Center for Translational Antiviral Research examined the effectiveness of a new potential antiviral drug, 4′-fluorouridine (4′-FlU), against influenza A viruses. Research had shown promise for 4′-FlU in combating different strains of influenza, including seasonal and pandemic viruses, in cell cultures and animal models.
The researchers investigated whether influenza viruses could develop resistance to 4′-FlU and the impact of such resistance on the virus’s ability to spread. They found that while some influenza strains developed resistance to the drug, these resistant variants were significantly weakened in animals, particularly in their ability to cause severe respiratory infections and transmit between hosts.

SARS-CoV-2 virion animation

In connection to our class, the concept of natural selection, which is a fundamental principle in evolutionary biology, is evident in the development of resistance to 4′-FlU by the influenza viruses. Through the process of random mutations shown by the drug, resistant variants of the virus emerge, highlighting the role of genetic variation in evolutionary processes. Secondly, the study underscores the importance of understanding molecular genetics, specifically the structure and function of DNA and RNA. The identification of specific genetic mutations in the influenza virus that create resistance to 4′-FlU demonstrates how changes in nucleotide sequences can lead to altered genetic characteristics, such as drug resistance. The study identified specific genetic mutations in the influenza virus that became resistance to 4′-FlU, but the researchers determined that these mutations were unlikely to have significant clinical implications. They also discovered that administering 4′-FlU at certain doses could effectively overcome moderate resistance and prevent lethal infection in mice.

Influenza Virus - 52461389748
The study shows the urgent need for new influenza therapeutics, given the limitations of current antiviral drugs, which often face challenges with viral resistance. The research provides valuable insights into the development and potential effectiveness of 4′-FlU as a treatment option for influenza, suggesting hope for improved battle against future influenza outbreaks or pandemics.

 

(Post includes edits suggested by Grammarly) 

From Individual to Environmental: COVID-19 Antigen Testing Expands

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On January 7, 2024

In Student Post

Until recently, testing for COVID-19 has focused on the individual rather than on the environment. However, newly introduced technology promises to expand the scope of COVID-19 detection. Researchers at Washington University in St. Louis have developed an apparatus to detect the presence of the covert virus in SARS-CoV-2 without backgroundenvironmental settings. Previous attempts at this technology have been limited by the volume of air tested. Without adequate air quantity, the sensitivity of the technology is negatively impacted. The current system, however, is capable of concentrating up to 1000 m³ of air per minute, compared to the two to eight cubic meters assessed in previous attempts. The result is a system that increases viral detection sensitivity while maintaining specificity.

The newly introduced apparatus functions by using centrifugal force to approximate viral particles to a liquid matrix adherent to the wall of the test chamber. Within the matrix are found nanobodies, bioengineered antibody fragments derived from llama antibodies. As we discussed in class, the human immune system is composed of humoral and self-mediated factors. Antibodies fall into the humoral category. While human antibodies consist of a light chain and a heavy chain, llama antibodies are composed of two heavy chains. By isolating heavy chain llama antibody fragments sensitized to the COVID-19 spike protein and then splicing multiple sensitized heavy chains together, researchers were able to amplify the viral signal, in a manner similar to PCR.

While the device has yet to be approved, cleared, or authorized by the FDA, it holds promise for meaningful real-world application. For example, prior to a large public event, indoor spaces could be screened for the presence of COVID-19. If the virus were detected, remediation could be performed and the environment retested prior to the public event. In doing so, countless potential COVID-19 infections could be avoided.

This novel technology diverges from current efforts at viral detection in that it does not rely on the existence of an infected individual but rather focuses on environmental detection thereby constituting primary prevention. In the future, the technology could be applied to prevention of other infectious diseases, both viral and bacterial. Further work is needed to explore the potential application of this method.

I urge readers to respond to the above and offer opinions.

The “Slow but Steady” Increase of yet Another COVID-19 Variant: What are the Implications?

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On January 7, 2024

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“Globally, there has been a slow but steady increase in the proportion of BA.2.86 reported, with its global prevalence at 8.9% in epidemiological week 44” (WHO)

Another variant? Since the beginning of the epidemic, we have seen a few strains of COVID-19 arise, notably the Omicron, Delta, and Alpha variants. You may ask, how do these mutations keep on materializing?

Like all viruses, SARS-CoV-2 — the virus responsible for COVID-19 — goes under, and will continue to go under, several mutations.

File:SARS-CoV-2 without background.pngAs a coronavirus, SARS-CoV-2 uses protein spikes (visualization on right) that fit into cellular receptors, in order to infiltrate our cells. Upon entry of the virus, the invaded cell begins to translate the viral RNA into viral proteins, which leads to the production of new viral genomes. According to Akiko Awasaki, PhD, this is where mutations often arise, stating that, “When viruses enter the host cells and replicate and make copies of their genomes, they inevitably introduce some errors into the code.” While these introduced errors may be inconsequential, they can also be of benefit to the virus, increasing contagiousness. These successful mutations may change how the virus behaves in the future, becoming the foundations of new evolutionary steps.

As we learned in AP Bio, the sequence of amino acids plays a heavy role in the primary structure of the spike protein. When the sequence is altered, hydrogen bonds will be corrupted or created, affecting the stability of the secondary structures like alpha helices and beta pleated sheets. This changes will in turn affect the tertiary structure, ultimately morphing the three-dimensional shape of the spike protein.

Given this knowledge of how SARS-CoV-2 invades cells, and how it may lead to evolution and mutation, what is the significance of this newest variant, and how can it be fought?

BA.2.86 was discovered over the summer with cases from Denmark, Israel, the United Kingdom, and the United States. Later on, it spread to various countries all over the globe, being discovered in wastewater in countries such as Spain and Thailand. As weeks passed, the new strain did not seem to pose a threat compared to its predecessors. However, months later, BA.2.86 on the rise. On November 11th, the CDC estimated that 3.0% of cases came from BA.2.86. November 28th’s estimate, 8.9%, is shockingly almost triple of the earlier estimate just two weeks prior. This is apparently garnering the strain some sort of reputation, now being labelled a “variant of interest” by the World Health Organization.

While the percentage may seem scary, the rise of the strain has not brought a disproportionate growth in infections or hospitalizations. Rather than posing new or threatening danger, it seems to be much better adept to escaping our bodies’ defense systems. The improved ability to slip past antibodies, compared to previous variants, likely comes from its large number of mutations, 30, on its spike protein. Antibodies, which serve to fight these invaders, may find difficulty recognizing and defeating the new strain.

Due to the strain only taking the notice of researchers recently, there are still many things to be uncovered. Some researchers have affirmed their support in newer vaccines against BA.2.86 and future variants. As always, it is best to wear masks when necessary, wash your hands, quarantine if you are experiencing symptoms, and receive the latest vaccine.

File:Janssen COVID-19 vaccine (2021) K.jpg

 

 

 

 

Cracking Down on Long COVID

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On December 15, 2023

In Student Post

In a study funded by the National Institutes of Health (NIH), nearly 10,000 Americans, including COVID-19 survivors, became the researcher’s focus, attempting to figure out the complexities of “Long COVID-19”. This condition leaves individuals fighting with lingering symptoms even after the virus has been vanquished, which presents various challenges, ranging from persistent fatigue to cognitive fog and prolonged dizziness. Nature Reviews Microbiology further examines the ongoing challenges in “long COVID” symptoms, emphasizing the necessity for consistent research efforts. This exploration acknowledges the need for continued studies to understand and address the complexities of the condition. It urges a proactive approach, encouraging the scientific community to stay observant and work together to enhance our understanding of long COVID. By prioritizing continuous research,  strategies for diagnosis and management can adapt to the evolving nature of this condition. As part of the NIH’s 1.15 billion dollar “recover initiative,” the study revealed vital insights, showing that the severity of “Long COVID” is higher in individuals infected before the emergence of the 2021 Omicron variant. SARS-CoV-2 illustration (17)

The research identified 12 key symptoms, establishing a comprehensive scoring system that not only aids in diagnosis but also classifies patients into distinct subgroups, hence refining our understanding of the condition. Health Affairs jumps into the global impact of long COVID, stressing the significance of collaborative international efforts in research and treatment. Furthermore, the study described the influence of vaccination status and the timing of infection, compared with unvaccinated individuals and those infected pre-2021, demonstrating a higher susceptibility to severe forms of long COVID-19.
In the context of our AP Biology class, this study aligns with our exploration of infectious diseases and the biological responses to pathogens. The study advances our scientific understanding of the complexities between our immune system and the evolving nature of viral threats. B and T memory cells are formed during vaccination when specific immune cells are activated in response to antigens present in the vaccine. These memory cells, produced by both B and T cells, retain a “memory” of the encountered antigens. Upon exposure to the same pathogen, these memory cells enable a quicker and more effective immune response, contributing to long-term protection through vaccines. Throughout the year, we have learned the biology behind vaccines, and this study reinforces our learning by demonstrating that vaccines play a crucial role in preventing individuals from experiencing ‘Long Covid’ symptoms. The reason behind this is the vaccine’s ability to prime the immune system, effectively fighting the virus and reducing the risk of prolonged symptoms. Decoding the mysteries of “long COVID” through collaborative initiatives like NIH’s “RECOVER” not only fuels my scientific curiosity but also emphasizes the real-world impact of scientific research on global health.

Symptoms of coronavirus disease 2019 4.0

(Post includes edits made through Grammarly)

Have you ever been caught with a viral disease and been misdiagnosed by your doctor? New CRISPR technology may eliminate this from happening.

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On April 30, 2023

In Student Post

So first, what even are viral diseases and how can they affect your health?  Well, some common viral diseases include HIV, herpesvirus, COVID-19, or even the common cold. Any disease classified under viral can enter your body through breathing air, touching something with viruses on it, intercourse, close contact, or getting bitten by a bug “such as a mosquito or tick”. Viruses typically infect one type of cell in your body and this is why the “common cold typically infects only cells in your nose, mouth, and throat”. 

In a study by PubMed Central (PMC) their goal was to identify the most common errors in diagnosing infectious diseases and their causes using physicians’ reports. In their concluding results, “the most common infectious diseases affected by diagnostic errors were upper respiratory tract infections (URTIs) (n = 69, 14.8%), tuberculosis (TB) (n = 66, 14.1%), pleuro-pulmonary infections (n = 54, 11.6%)”. This data was taken from a sample of 465 patient cases and the researchers concluded that, “a substantial proportion of errors in diagnosing infectious diseases moderately or seriously affect patients’ outcomes”. So when diagnosing viral infectious diseases, steps need to be taken to improve our testing process.

Researchers from the American Chemical Society are looking at using “glow in the dark” proteins to help diagnose viral diseases. Fireflies, anglerfish, and phytoplankton all create a glowing effect using bioluminescence, which is caused by a chemical reaction involving luciferase protein. This protein has been used in sensors for point-of-care testing, but lacks the high sensitivity needed for clinical diagnostic tests. Researchers wanted to combine CRISPR-related proteins with a bioluminescence technique to improve sensitivity. They developed a new technique called LUNAS, which uses recombinase polymerase amplification (RPA) to amplify RNA or DNA samples. Two CRISPR/Cas9 proteins bind to targeted nucleic acid sequences and form the complete luciferase protein, causing blue light to shine in the presence of a chemical substrate. This new technique successfully detected SARS-CoV-2 RNA in clinical samples within “20 minutes, even at low concentrations“. The researchers believe this technique could be used to detect many other viruses effectively and easily.

In relation to AP Biology, we have learned about the process of gene expression where RNA and proteins are produced due to a specific gene being activated. The regulation of gene expression conserves energy and allows organisms to turn on and off genes only when they are required. The CRISPR (Clustered Regularly Interspaced Short Palindromic Repeats) gene which are found in prokaryotes cut DNA phages and plasmids to prevent damage to the prokaryote itself. It is used as a rudimentary immune response system. The CRISPR can be associated with other proteins to create an associated complex which allows for the excision and insertion of genes along the length of the genome. Using this process, viral diseases can be identified when combined with the bioluminescence mentioned above.

Looking into the future, researchers are searching for ways to apply CRISPR proteins to detect a greater range of viral diseases so that all patients can get the proper care that they need.

Analyzing Viruses in One Step Using LUNAS

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On April 23, 2023

In Student Post

In this article from the American Chemical Society, Maarten Merkx and his colleagues research how to use and combine CRISPR-related proteins with a bioluminescence technique whose signal could be detected with a digital camera. This new technique can diagnose illnesses faster while being much more efficient and practical. Bioluminescence is a chemical reaction involving the luciferase protein that causes the luminescent, glow-in-the-dark effect. The luciferase protein has been incorporated into sensors that emit an easily observed light when they find their target, but they lack the incredibly high sensitivity required of a clinical diagnostic test.

Mareel - Bioluminescence in Norra Grundsund harbor 2

CRISPR, a gene-editing technique, has the ability to increase sensitivity, but it requires many steps and additional specialized equipment. With the new technique, called LUNAS (luminescent nucleic acid sensor), two CRISPR/Cas9 proteins specific for different neighboring parts of a viral genome each have a distinct fragment of luciferase attached to them. If a specific viral genome that the researchers were testing for was present, the two CRISPR/Cas9 proteins would bind to the targeted nucleic acid sequences and come close to each other, allowing the complete luciferase protein to form and shine blue light in the presence of a chemical substrate. RPA-LUNAS successfully detected SARS-CoV-2 RNA within 20 minutes, even at concentrations as low as 200 copies per microliter.

This is similar to the process of gene regulation that uses an inducible operon as we learned in class. An inducible operon is a type of negative regulation that turns on when it interacts with an inducer. It is usually off which means there is an active repressor that binds to the operator to block the RNA polymerase from transcribing the DNA. When there is the inducer, such as the virus, the inducer inactivates the repressor by binding to the allosteric site which allows the RNA polymerase, such as the CRISPR/Cas9 proteins, to transcribe and eventually produce the protein, such as the luciferase protein.

As we are recovering from the devastating COVID-19 Pandemic, how can new medical advancements and technology help us prepare for future outbreaks?

Is Monkeypox even around anymore?

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On March 16, 2023

In Student Post

According to the CDC, monkeypox is a virus that can cause many symptoms ranging from respiratory problems to rashes and scabs, as research studies have shown. While, according to the world health organization, the virus was first identified in 1970, and there have been multiple outbreaks since. The first outbreak to reach the US occurred in 2003, when a young girl was bitten by a prairie dog and exhibited symptoms days later. Typically, the virus has an incubation period of 3-17 days which a patient may not show symptoms. However, once the virus emerges, it may stay with a patient for up to four weeks. Often the virus enters the system through either the skin or the respiratory system. After this,  the virus binds the D8L protein to chondroitin sulfate, a cell surface receptor. Once the virus has bound to a cell, it can enter through either endocytosis or by fusing through the cell membrane. After this, the virus can infect the cell and spread to others.

When the virus had a recent outbreak this past May the CDC and WHO were quick to react. As the virus emerged soon after the COVID-19 pandemic, it could be said that both WHO and the CDC were “warmed up” for this monkeypox outbreak and the virus was quickly dispelled in the continental US. However, before it could be dealt with, 30 thousand people in the US were infected and across the world, just over 85 thousand cases were reported. Similarly, a study was done across the US, surveying hundreds of cases between April and June of 2022, and the study revealed that while monkeypox is very infectious, it doesn’t necessarily target those with immune system problems nor the elderly. However, 95% of people who contracted the virus did develop some sort of rash, meaning that was the most common symptom. While the mortality rate of monkeypox is relatively low, at around 3%, it is still a debilitating disease, affecting nearly a hundred thousand people across the world. As such, it is impressive how countries have come together to deal with this virus so quickly. But how?

While the first US outbreak was from animal to human, the 2022-23 outbreak has been somewhat trickier for eradication as the recent outbreak has spread from human to human. However, the monkeypox virus is quite similar to the smallpox virus, for which a vaccine exists. Luckily, this vaccine is up to 85% effective for those experiencing symptoms.Smallpox vaccine (cropped)

However, more measures had to be taken than simply a vaccine that is only 85% effective. The CDC and WHO implemented measures such as mask-wearing, vigorous hand washing, and awareness campaigns in areas heavily affected by monkeypox. With these protocols implemented across the world, monkeypox was tamped down quite quickly in relation to how quickly it spread. As such, monkeypox left the media just as soon as it emerged, and generally, people can sleep soundly at night without worry of waking up feverish, with large painful rashes and scabs.

 

Can Your Lungs Work Against COVID-19?

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On February 28, 2023

In Student Post

Within the last two to three years there has been an immense focus in the field of science, COVID-19. This pandemic has sparked a myriad of research opportunities as well as brought up questions we didn’t even know we needed answered.

With this, recent research at the University of Sydney shows that our lungs contain a protein that blocks the COVID-19 infection and works to create a protective barrier within our body. The way it works is that a protein receptor found in our lungs sticks to the virus, and then pulls it away from the targeted cells. The protein is known as the Leucine-Rich Repeat-Containing Protein 15 or in short, LRRC15. For context, leucine is an essential amino acid for protein synthesis as well as many other biological functions. The protein is a built-in receptor inside of our bodies that binds to the COVID-19 virus and doesn’t pass on the infection.

Lungs diagram detailed

Initially, the research was published on February 9, 2023, in the PLOS Biology Journal. Led by Professor Greg Neely and his team members, the findings serve to open a new sect of immunology and COVID research, specifically around the protein, LRRC15. Moreover, it creates a path to develop new drugs and treatments to prevent infections such as COVID-19. Greely states that ” This new receptor acts by binding to the virus and sequestering it which reduces infection,” essentially the receptor is able to attach to the virus and “squish” it before it moves to infection. He also pushes the idea that the new receptor can be used to “design broad-acting drugs that can block viral infection or even suppress lung fibrosis.” Continually Dr. Lipin Loo, one of Greely’s team members, mentions, “We think it acts a bit like Velcro, molecular Velcro, in that it sticks to the spike of the virus and then pulls it away from the target cell types,” here he outlines the stickiness of both the receptor and the virus as well as the receptor’s nature to latch onto the virus and “hold” it. In addition, Loo states, “When we stain the lungs of healthy tissue, we don’t see much of LRRC15, but then in COVID-19 lungs, we see much more of the protein,” here he fronts the idea that COVID-19 lungs are far richer in the LRRC15 protein than normal lungs, this may be due to a result of the protein’s ability to immobilize the virus.

To outline COVID-19 infects us by using a spike protein to attach to a specific receptor in our cells. It mainly uses the ACE2 receptor to enter human cells. Moreover, our lung cells have high levels of ACE2 receptors, which is why being infected can often cause severe problems in our lungs. Similar to ACE2, LRRC15 is a receptor for COVID. But, LRRC15 does not support infection, instead, it sticks to the virus and immobilizes it. This prevents other cells from becoming infected. LRRC15 attaches to the spike of the virus and pulls it away from certain target cell types. The LRRC15 protein is widely present throughout our body, it is in the: lungs, skin, tongue, fibroblasts, placenta, and lymph nodes. However, the researchers observe that the lungs “light up” with LRRC15 after infection. They think the new protein is a part of our body’s natural response to combatting the COVID-19 infection. It creates a barrier that separates the virus from our lung cells most susceptible to COVID-19 infection

SARS-COV-2

To connect to our AP Bio Class, we learned about adaptive immunity where we develop an acquired immunity after being exposed to pathogens, a specific response. I see some similarity here in that the LRRC15 protein is specific to immobilizing the COVID-19 infection. Additionally, in our Cell Signalling Chapter, we focused on signal transduction and its stages, reception, transduction, and response. Specifically in the reception stage, we focused on intracellular and transmembrane receptors. I think that LRRC15 would be transmembrane in order for it to efficiently bind to the COVID-19 Spike. With this, however, I would like to see more about the transduction component of the LRRC15 receptor. Lastly in our Enzyme Unit, we learned about how different factors can affect enzymatic activity; heat, pH, and even general surroundings. I wonder which factors work to hinder and work to stimulate the purpose of the LRRC15. I invite any and all comments with additional info relevant to the topics discussed.

Researchers Find Ways To Combat COVID-19

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On January 16, 2023

In Student Post

Ever since COVID-19 was discovered scientists had no idea how to stop this virus. After lots of research we were able to know that there were many different variants of  COVID-19. We understood that some variants were stronger than others according to research. There is an article that talks about how they can be able to stop all kinds of COVID-19 viruses and the different variants. In the article, Professor Seung Soo Oh had an idea on how to stop all kinds of variants in one go. He says that the virus can change its structure whenever. It will then bind to the angiotensin-converting enzyme receptor which is a receptor protein. His team developed a hybrid neutralizer that is able to bind to the virus which then cause the virus to not interact with the protein receptor. This neutralizer was able to be about 5 times more effective then what they first had when COVID-19 was discovered.

According to this article, Omicron which was found in November of 2021 in South Africa, is the most dangerous variant of COVID-19. It is a variant of COVID-19 and is one of the strongest variants. In December of 2019, sub-variants of Omicron began to appear. Some of the sub-variants include BA.5, BQ.1, and BQ.1.1. According to the article, the Omicron sub-variants were very effective and was more transmissible then the Delta variant. The neutralizer should be able to stop Omicron and the sub-variants.

According to another article, variants aren’t weakened by covid vaccines that were had a while ago. In order to help stop COVID-19, the article says that getting boosters will be more effective for any new variants that are discovered. This doesn’t mean they will 100% work. With this knowledge, the new neutralizer that was developed should be able to stop all these viruses from mutating and from entering the cell.

This relates to what we have learned in class this year because we have learned cell structure. When COVID enters the cell, it must bind to a receptor. Once it enters the cell the RNA or DNA would then reproduce. This is similar to what we have learned about how other things enter the cell such as glucose and amino acids. In receptor mediated endocytosis, the ligands must bind to the receptor and then enter the cell. This relates to what we have learned in class because we have learned how molecules are able to enter the cell and how receptors work.

 

SARS-CoV-2 without background

 

There Are More Viruses On Earth Than Stars In The Universe. Why do only some infect us?

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On January 16, 2023

In Student Post

Scientists have estimated that there are 10 nonillion (10 to the 31st power) viruses currently on our planet. They are everywhere. Many viruses are beneficial for their host, many inflict no harm, but why do so few viruses affect us and even fewer severely affect us? The short answer: “These pathogens are extraordinarily picky about the cells they infect, and only an infinitesimally small fraction of the viruses that surround us actually pose any threat to humans” says virologist Sara Sawyer.

Understanding how certain viruses affect humans is crucial for protecting and preventing future outbreaks. COVID-19, the most recent outbreak that experienced a “spillover event,” was initially spread through interactions with an animal that is a “non-human primate”. This is called zoonosis. Multiple outbreaks have been introduced this way, but not can be started this way. Pathogens can also enter through cuts, scrapes, mosquitoes, ticks, etc. Once a virus has entered, it needs to find a way to get inside the cells and replicate. To do this, it must first attach to the surface of a host cell and then inject its genetic material (RNA) into the cell. The virus’s genetic material then takes over the machinery of the host cell, using it to replicate itself and produce new viruses. Viruses with a lot of genetic flexibility, and particularly those that encode their genomes as RNA rather than DNA, are well-suited to crossing the species divide. The majority of pathogens that have infected the human population in recent decades have been RNA viruses, including Ebola, SARS, MERS, Zika, several influenza viruses, and SARS-CoV-2. The more lethal viruses were found to have been hiding in their hosts for longer periods of time before showing any symptoms. This would allow it to replicate and spread to new species.

 

Coronavirus. SARS-CoV-2

So the answer is; that a virus has to be incredibly sophisticated for it to cause harm to a human, pandemics are so rare because of precautionary measures such as vaccines, healthcare, and proper sanitation. The continuous study of viruses and their behavior is an important task for the human population and its future as current viruses are continuously mutating and developing with each given day.

 

Got a weird COVID-19 symptom? You’re not alone

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On December 8, 2022

In Student Post

COVID-19 is one of the most commonly known diseases of the decade, for most people today are familiar with its many symptoms, including chills, cough, difficulty breathing, etc. Rarely, SARS-CoV-2 will affect people in ways not expected by a respiratory virus; however, people are starting to see it cause odd symptoms. Peter Chin-Hong, an infectious diseases physician at the University of California, San Francisco said that people have developed patchy tongues, puffy digits, and hair loss as a result of SARS-CoV-2.  Chin-Hong still notes that these symptoms may be less dangerous because they are capable of going away on their own.

SARS-CoV-2 without background

Link to Image

It is not always confirmed that COVID tongue, COVID toe, COVID eye, or other strange symptoms are due to COVID-19, but the large scale of coronavirus infections means that SARS-CoV-2 has many chances to show the public how it affects people differently. The U.S. announced they already have had 98 million cases confirmed, and Chin-Hong informed Science New that “statistically speaking, you’re going to find people with more and more weird things.” 

In October, the  Journal of Medical Case Reports released a study done by Saira Chaughtai, an Internal medicine doctor, after a patient obtained unbelievable symptoms after ten days of testing positive for COVID-19. Their tongues swell up and eventually erupted in white-ringed lesions. Chaughtai told Science News “I was like, ‘Oh my god, COVID can do anything.'”

Chin-Hong has also seen patients with unusual tongues; however, they had that looked “as if they’d chewed a mouthful of tortilla chips.”  

Changhai was perplexed about how she was going to treat her patients with COVID tongue. She began by researching scientific literature while giving her patients various types of mouthwash to help in the meantime. She even went to such great lengths in teaming up with a sports medicine doctor who shined a low-level laser light on patients’ tongues, a photobiomodulation therapy normally used to treat muscle injury. Chaughtai thought laser light therapy could heal swollen tongues because it increases blood flow. It showed good results as her patient’s tongue lesions healed even though she still feels some sensitivity. 

Another abnormal effect of COVID-19 is COVID finger or toe which causes swelling in peoples’ fingers or toes. The symptoms also included toes or fingers turning a pink, red, or purplish color. It is know to be very painful. Michael Nirenberg of Friendly Foot Care has seen at least 40 people with this symptom who have been exposed to the coronavirus. He found that fingers or toes will normally heal within a couple of months. Nirenberg told his patient to apply nitroglycerin ointment which he thinks increases blood flow to their fingers or toes. 

“We can’t predict who’s going to get what,” Chin-Hong states, for he feels people should be aware that COVID-19 is capable of causing a wide variety of symptoms. He noted that strange symptoms occur mainly with unvaccinated people. “If this is a reason why some people might get vaccinated,” Chin-Hong says, “I think that would be great,” for these symptoms may seem less severe and harmful as symptoms involving the heart or lungs, but they still can be alarming to see. 

In AP Biology this year, we discussed how there are specific receptor proteins integrated into the plasma membrane. The binding between the receptor protein and a ligand, or signaling molecule, is highly specific. Recent studies found that SARS-CoV-2 enters the cell through a specific receptor protein called ACE2. SARS-CoV-2 spike binds to its receptor human ACE2 (hACE2) and an enzyme called proteases activates it. We also talked about enzymes in AP Biology; they are proteins that function and set off reactions or processes. It is important to understand how the unfamiliar virus enters into cells to learn more about its influence on the human body; this can help scientists discover more information on how and why these strange symptoms occur.

Is the recently discovered hidden cavity on the SARS-CoV-2 protein a target for drugs?

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On December 6, 2022

In Student Post

Many of us have been vaccinated against COVID-19 and have had the virus, leading us to become used to the virus being prevalent in our lives during the past few years. Even though a successful vaccine has been rolling out for a while now, new therapies have not yet been discovered for future strains. Finding new therapies for the virus remains a major priority in the field of science, even if many of us have been protected already. This issue remains a priority because new variants and strains have been continuing to emerge, and some resist present therapy mechanisms.

SARS-CoV-2

The most effective approach to attempting to combat the virus is addressing the proteins on the surface of therapeutic targets, known as spike proteins. The spike protein (S proteins) located on the surface of the virus leads to its spiky protrusions, and its mechanism to enter human cells. Like we learned in AP Biology class, the spike proteins of the virus latch to cells by matching with a specific receptor on a cell’s surface. The spike proteins of the virus have to latch on to the new cell to infect. Successful messenger RNA vaccines properly target this spike protein, which is the main goal when creating new therapies for viruses. 

                                             Spiky appearance of SARS CoV-2 virus

Luigi Gervasio, a chemistry and structural/molecular biology professor at University College London, and his team have been working towards addressing this issue. By partnering with the University of Barcelona’s research team, the two teams took the first steps to discover a possible mechanism for future drugs to detect and protect against the SARS CoV-2 Virus. Through thorough research and investigation, they uncovered a “hidden” cavity on the surface of a prominent infectious agent of the virus known as Nsp1. The team was able to make this discovery by testing small molecules that had the potential to bind to the Nsp1 cavity. The team identified one, 5 acetylaminoindane, which is essential for the development of new drugs against viruses. They concluded that this cavity permitted the calculation of the cavity’s atomically spatial arrangement, which will allow the development of these drugs.

The results of their breakthrough findings set the stage for developing new therapies that will be able to target the NSp1 protein against SARS-CoV-2 and present Nsp1 proteins in future coronavirus strains. Not only will this finding be impactful for targeting SARS-CoV-2 and future variants, but also new cavities on the surface of other proteins that have yet to be found by scientists. Finally, this research is monumental for both SARS-CoV-2 and virus treatment in years to come!  

 

Shhhhhhh! Some Viruses Can Sneak into Cells and Cause Cancer

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On October 27, 2022

In Student Post

Viruses! We all hate the colds we get in the fall that come with a cough, a runny nose, and a sore throat.  These bugs have gone around since nursery school, so we were taught that viruses were transmitted through touching door knobs, getting coughed on, and touching someone who is sick.  While these are how viruses are spread from person to person, the infection that occurs on a cellular level is much more complex.  

For starters, only a handful of viruses are known to actually cause illness in humans, but the ones that do have adapted to do it very efficiently, and some are even known to cause cancer.  Viruses that cause cancer include human papillomavirus, Kaposi Sarcoma-associated Herpesvirus, and Epstein-Barr virus.  The way that these viruses get into the cells is very unique compared to the common cold virus, and a team at the University of Michigan Medical School decided to take a closer look at just how they invade to try and get a better grasp on how to prevent cancers caused by viruses in humans.

The virus they researched is called SV40 and it causes tumors in monkeys.  The way that SV40 infects monkey cells is by burrowing itself through the cell membrane and then into its nucleus in order to duplicate itself.  SV40 is used as a tool to understand how the cancer causing viruses work because of the biological similarities that monkeys and humans have.  An earlier team studied how SV40 travels through the cell.  It goes from the surface, through the endosome, the ER, and then enters the cytosol.  

The most recent study illuminates the rest of the virus’ passage through the cell. The way SV40 gets into the nucleus is through the nuclear pore complex.  This is how many viruses enter the nucleus, but the SV40 is too large to enter through this pore.   The virus must disassemble in order to gain access to the nucleus. This process partially disassembles the virus into a smaller package made of two proteins and genetic material (DNA).  As we have learned in class, the DNA is the macromolecule that codes for how to build the proteins that build the virus.  When the DNA for the virus is connected with the two proteins, it uses both the nuclear pore complex and another complex called LINC.  LINC connects the two membranes of the nucleus together.  Many other viruses grab onto the little fingers sticking out of the nuclear pore complex (seen below), while SV40 seeks out LINC in order to get into the nucleus.  

202012 Nuclear pore complex

The difference in entrances between more common viruses and SV40 could be what makes SV40 cancer-causing.  The next step is to research how SV40 exploits LINC in order to expand upon how other diseases could enter the nucleus, and hopefully find a way to trigger the immune system in order to expel or digest the viruses before it is too late.  

Antitoxin Mechanism Saves Us From Virus Attacks!

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On February 25, 2022

In Student Post

Researchers in Lund have recently discovered an antitoxin mechanism that may be able to protect bacteria against virus attacks by neutralizing hundreds of toxins. Understanding this antitoxin mechanism, named the Panacea, could be the next step to the future success of phage therapy, a treatment for antibiotic resistant infections.

These toxin-antitoxin mechanisms are a kind of on-off switch in bacterial DNA genomes. They are found to attack bacteriophages to defend bacteria.This activation of toxins allows bacteria to “lockdown” and limit growth and spreading of a virus. In order for Phage therapy to be successful in the future, it is important to understand these mechanisms in great depth. The goal of Phage therapy is to use viruses to treat bacterial infections. A toxin dramatically inhibits bacterial growth and an adjacent gene encoding an antitoxin counteracts the toxic effect. Although toxin-antitoxin pairs have been associated with new toxins or antitoxins before, the ability of the Panacea is unprecedented.

Phage therapy

As research continues on toxin-antitoxin systems and phage therapy it is clear that what we know is just the tip of the iceberg. As bacteria increasingly become resistant to antibiotics, other approaches are needed to help eliminate infections. The next steps of this research is to continue deepening the understanding of the Panacea and finding toxin-antitoxin systems on a universal scale.

In AP biology class we learned about inhibitors. An inhibitor is something that slows down or prevents a particular reaction or process. A toxin inhibits bacteria from growing and reproducing so the antitoxin can act against the virus that has already spread.

Optimus Prime, Megatron, Proteins? The New Transformer Vaccine Candidate!

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On January 17, 2022

In Student Post

Amid the global outbreak of COVID-19, with no end in sight after nearly two years, the future wellbeing of humans is in danger. Coughs, fevers, and shortness of breath have lent way to millions of deaths across the globe. As thousands of researchers relentlessly work to find solutions to this virus, multiple vaccine candidates have emerged. Specifically, in the United States, millions of Americans have received doses of the Pfizer-BioNTech, Moderna, and Johnson & Johnson’s Janssen vaccines. However, scientists at Scripps Research recently recognized a new, self-assembling COVID-19 vaccine as a potentially more efficient and effective way to fight this worldwide battle.

 

Primarily, it is critical to understand how vaccines function as they help protect the immune system. The COVID-19 vaccines currently in effect are mRNA-based; in other words, the messenger RNA signals one’s body to produce a harmless viral protein that resembles the structure of a spike protein. The body, with the help of T-Helper cells, recognizes this structure as a foreign invader as B cells bind to and identify the antigen. The T-Helper cells will then signal these B cells to form B-Plasma cells and B-Memory cells. When getting the vaccine, the B-Memory cells are especially important as they prevent reinfection. This is a process known as adaptive immunity. Here, in the event of future infection with the spike-protein COVID-19, the memory cells would help carry out the same response more quickly and efficiently. Essentially, this process acts as the body’s training in case of any future infections.

 

While the Scripps Research COVID-19 vaccine would evoke a similar immune response to that described above, it differs from other candidates in how it assembles in the human body; this new vaccine would be comprised of proteins that are able to self-assemble. On their own, these nanoparticle proteins would transform into a sphere protein structure surrounded by smaller proteins, mimicking the coronavirus’s shape. Here, the self-assembled spike proteins are more sturdy and stable than in an mRNA-produced structure. Thus, it more accurately prepares the body for future infection with COVID-19. In fact, multiple tests found that mice who were given the experimental vaccine were able to fight off not only SARS-CoV-2 but also SARS-CoV1 along with the alpha, beta and gamma variants.

 

Nonetheless, influencing the public to get a newer vaccine instead of the well-trusted vaccines already in production requires proof of the candidate’s benefits. Primarily, as mentioned, early results find that this new candidate would perform well with many different strains of COVID-19. Additionally, researchers assert that this vaccine would be relatively simple to produce on a mass scale. Lastly, scientists found that this vaccine may well be more protective and long-lasting than current vaccine candidates. Although the process of vaccine approval is lengthy and often difficult, I am hopeful for the future of the Scripps Research vaccine if it is put into production. Moreover, I believe that such experimentation with self-assembling nanoparticle proteins transcends the current pandemic. The benefits of this field present a wide array of opportunities, and I look forward to seeing what its future may hold.

 

What do you think? Are these transformer-like self-assembling particles a gateway to the future of medicine or an unnecessary distraction from effective treatments already in circulation?

How are new COVID variants identified?

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On January 4, 2022

In Student Post

COVID variants are of high concern for scientists studying the disease. Some variants can be more infectious or cause more severe illness. Additionally, some variants can evade vaccines by having different surface proteins than the variant the vaccine was created for. This causes the antibodies produced from the vaccine to be less effective against other variants. In AP Biology class we discussed how the Delta Variant, first identified in December 2020, has a different spike protein structure than the original virus from which the vaccine was created from. This allows the variant to be more infectious, and make the vaccine less effective against it. But, what are COVID variants? And how are they discovered? Hand with surgical latex gloves holding Coronavirus and A Variant of Concern text

COVID variants are “versions” of the virus with a different genetic code than the original one discovered. However, not every mutation leads to a new variant. This is because the genetic code of the virus codes for proteins. Some mutations will not change the structure of the protein and thus not change the virus. So, COVID variants can be defined as versions of the virus with a significantly different genetic code than the original virus.

To detect new COVID variants, scientists sequence the genetic code of virus which appears in positive COVID tests. Scientists look at the similarity of the genetic sequences they find. Then, if many of the sequences they get look very similar to each other, but different to any other known virus, a variant has been discovered.

To sequence the RNA of the virus, scientists use what is called Next Generation Sequencing (NGS). To understand how NGS works, it is best to start with what is called Sanger Sequencing. Sanger Sequencing utilizes a modified PCR reaction called chain-termination PCR to generate DNA or RNA fragments of varying length. The ending nucleotide of each sequence is called a ddNTP, which contains a florescent die corresponding to the type of nucleotide. The addition of a ddNTP also terminates the copying of the particular sequence. The goal of this PCR reaction is to generate a fragment of every length from the start to the end of the sequence. The sequences can then be sorted by length using a specialized form of gel electrophoresis. The sequence is then read by using a laser to check the color of the fluorescent die at the end of each sequence. Based on the color and size, the nucleotide at that position of the genomic sequence can be found.

Sanger Sequencing Example

The difference with NGS is that many sequences can be done in parallel, allowing for very high throughput. In other words, with NGS many COVID tests can be sequenced in once.

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