BioQuakes

AP Biology class blog for discussing current research in Biology

Tag: antibody

Next-Gen Therapeutics!

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On January 8, 2024

In Student Post

Scientists at St. Jude Children’s Research Hospital have launched a massive mission to confront the escalating challenge of antibiotic resistance in Mycobacterium abscessus (Mab), a pathogen naturally resistant to antibiotics. The urgency of this is emphasized by the increasing threat of Mab infections in healthcare settings, mainly those with compromised lung function or weakened immune systems. In response to the need for innovative therapeutics, the researchers at St. Jude undertook a careful approach, which focused on redesigning the antibiotic spectinomycin to generate new versions capable of overcoming the primary driver of resistance, which is something called efflux (the process cells use to remove drugs). The findings of their work, published in Proceedings of the National Academy of Science, discovered the development of structurally distinct N-ethylene linked aminomethyl spectinomycins (eAmSPCs), outperforming standard spectinomycin by up to 64 times in power against Mycobacterium abscessus.

Antibody

Connecting to class, this work underscores the significance of antibodies (Unfortunate Ned), which are proteins produced by B cells in response to specific pathogens. The development of this variant against Mab links to the antibody-mediated immune response. Engineering more potent antibiotics against Mab shows a real-world application of understanding and manipulating the immune system’s humoral response, highlighting the importance of B cells in providing long-term protection against infections.

Humoral Response Drawing

Overall, the significance of this breakthrough is not only in the efficiency of eAmSPCs, but also in solving their course of action. By explaining how these compounds avoid efflux, the researchers have paved the way for a shift in antimicrobial therapy. The researchers discovered that eAmSPCs show compatibility with various classes of antibiotics used to treat Mab, while retaining their effectiveness against other mycobacterial strains. This adaptable characteristic leads eAmSPCs to be the potential future of therapeutics, offering hope for patients struggling with limited or nonexistent treatment options.

 

(Post Includes Edits Made Through Grammarly)

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?

Learn From the Greeks: The “Trojan Horse” Method to Cure Ebola

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On October 16, 2017

In Student Post

The study to find a cure for the dangerous virus Ebola has resulted in a promising new find: a new strategy has shown positive results.  This new technique involves the placement of antibodies into the cell with the Ebola virus and then it binds to the NPC1 protein before the virus can, essentially rendering it useless.

To understand exactly how these special rainbow unicorn antibodies work, it is essential if we know how the Ebola virus spreads.  The different strains of the Ebola virus (Sudan, Zaire, Tai Forest, Bundibugyo, and Reston) are genetically a little different but they do the same thing.  The virus enters the cell through glycoproteins and gets engulfed into a lysosome. Once inside a lysosome, the virus transforms into a new state where it can bind to a human protein called NPC1.  Once bound to this protein the virus can eject its information into the cytoplasm of the cell and spread.

The solution lies in the binding of the special antibody.  The antibody ZMapp can effectively destroy the Ebola virus, but it is only effective on the Zaire strain. The other strains of Ebola are a little genetically different that the ZMapp antibody does not detect the other strains. Thus, a different approach is required to fight the virus.  The virus can be stopped if an antibody is able to enter the cell with the virus and either bind to the NPC1 protein before the virus does or bind to the virus to disable its ability to bind to anything else.

When the Ebola virus is in a cell’s lysosome it structurally alters itself to enable it to bind with the NPC1, and an advantage that scientists have discovered is that between the different strains of Ebola virus, the transformed versions are very similar, thus an antibody can be made that can bind to all of the different strains.  The problem with this, however, is that antibodies cannot enter the cell the same way that viruses can.

Ebola Virus

The solution that the researchers came up with stems back to the Trojan Horse story from Ancient Greece. The researchers added an extra arm to the antibody, enabling it to latch onto the virus and hitch a ride with it into the lysosome.  Once in the lysosome with the virus, the virus alters and the antibody can then bind again and disable the virus.  This method can potentially be a cure for all of the strains of the Ebola virus, causing an end to a very dangerous virus.

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