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Scientists Found a New Antibody That Neutralizes All COVID Variants
COVID-19 vaccines have been effective at keeping people from getting severely ill and dying from the virus, but they’ve required different boosters to try to keep on top of all of the coronavirus variants that have popped up. Now, researchers have discovered an antibody that neutralizes all known COVID-19 variants.
The antibody, called SP1-77, is the result of a collaborative effort from researchers at Boston Children’s Hospital and Duke University. Results from mouse studies they’ve conducted were recently published in the journal Science Immunology, and they look promising.
But what does it mean, exactly, to have an antibody that can neutralize all variants of COVID-19, and what kind of impact will this have on vaccines in the future? Here’s what you need to know.
What is SP1-77?
SP1-77 is an antibody developed by researchers that so far can neutralize all forms of SARS-CoV-2, the virus that causes COVID-19. It was created after researchers modified a mouse model that was originally made to search for broadly neutralizing antibodies to HIV, which also mutates.
The mice used in the study have built-in human immune systems that mimic the way our immune systems develop better antibodies when we’re exposed to a pathogen. The researchers inserted two human gene segments into the mice, which then created a range of antibodies that humans might make. The mice were then exposed to SARS-CoV-2’s spike protein (which is what the virus uses to latch onto your cells) and produced nine different families of antibodies that bound to the spike protein to try to neutralize it.
Those antibodies were then tested and one—SP1-77—was able to neutralize Alpha, Beta, Gamma, Delta, and all Omicron strains (including the current circulating ones) of COVID-19.
The antibody works in a slightly different way than many of the antibodies people make to vaccines. To infect you, SARS-CoV-2 has to first attach to ACE2 receptors in your cells. The current COVID-19 vaccines block this binding from happening by attaching to the spike protein’s receptor-binding domain (RBD) at certain spots, a press release from Boston Children’s Hospital explains.
The SP1-77 antibody also binds to the RBD, but doesn’t prevent the virus from binding to ACE2 receptors. What it does do is block the virus from fusing its outer membrane with the membrane of your cells, which is what needs to happen to make you sick.
“SP1-77 binds the spike protein at a site that so far has not been mutated in any variant, and it neutralizes these variants by a novel mechanism,” study co-author Tomas Kirchhausen, Ph.D., said in a statement. “These properties may contribute to its broad and potent activity.”
What does this mean for the future of COVID-19 vaccines and treatments?
It’s not clear right now. It’s important to note that this research was done in mice—not humans—although studies on the antibody are ongoing.
“This is very early-stage proof-of-concept work to illustrate that broadly neutralizing antibodies can be generated using a mouse model,” says Amesh A. Adalja, M.D., infectious disease expert and senior scholar at the Johns Hopkins Center for Health Security. “Such work, if replicated and expanded, could form the basis of new monoclonal antibody products as well as a vaccine.”
Experts say that a vaccine that could take out all variants of COVID-19 would definitely be welcome. “We’d love to have a vaccine that is active against all circulating variants, including those yet to come,” says Thomas Russo, M.D., professor and chief of infectious disease at the University at Buffalo in New York. “It’s the holy grail of vaccines.”
That could potentially mean that you would only need to get a COVID-19 shot or booster once a year or even less frequently, depending on how long protection from the vaccine lasted, Dr. Russo says.
The researchers have applied for a patent for the SP1-77 antibody and mouse model used to create it, and plan to create something that can be used by the general public if all goes well.
Korin Miller is a freelance writer specializing in general wellness, sexual health and relationships, and lifestyle trends, with work appearing in Men’s Health, Women’s Health, Self, Glamour, and more. She has a master’s degree from American University, lives by the beach, and hopes to own a teacup pig and taco truck one day.
Powerful New Antibody Neutralizes All Known COVID Variants
The antibody could greatly improve our ability to defend against future variants.
Future vaccine development may be inspired by the findings.
Therapeutic antibodies that were effective early in the pandemic have lost their efficacy as
In a study that was published in Science Immunology, Alt and Sai Luo, Ph.D., utilized a modified version of a humanized mouse model that his lab had previously used to look for broadly neutralizing antibodies to HIV, another virus that often mutates. Since the mice effectively have built-in human immune systems, the model closely resembles how the trial-and-error process our immune system uses to create increasingly effective antibodies.
The researchers initially introduced two human gene segments into the mice, causing their B cells to create a wide repertoire of humanized antibodies in a short period of time. They subsequently exposed the mice to the original Wuhan-Hu-1 strain of the virus’s SARS-CoV-2 spike protein, which is the main protein targeted by our antibodies and current vaccines. The modified mice developed nine lineages, or “families,” of humanized antibodies that bonded to the spike in response.
Together with a Duke University team led by Dr. Barton Haynes, Alt and Luo then assessed the efficacy of these antibodies. Antibodies from three of the nine lineages were effective in neutralizing the original Wuhan-Hu-1 virus. The SP1-77 antibody and other members of its lineage, in particular, demonstrated extremely wide activity, neutralizing Alpha, Beta, Gamma, Delta, and all prior and current Omicron strains.
A new approach to virus neutralization
What caused the SP1-77 antibody to be so broadly neutralizing? Structural studies by a collaborating team led by Bing Chen, Ph.D. and Jun Zhang, Ph.D. at Boston Children’s Hospital and the Haynes group at Duke, showed that SP1-77 works differently from current antibodies (either therapeutic antibodies or those we make in response to current vaccines).
Many of the existing antibodies work by attaching to the receptor-binding domain (RBD) of the spike in certain regions, preventing SARS-CoV-2 from binding to our cells’ ACE2 receptors, which is the initial step in infection. The SP1-77 antibody binds to the RBD as well, but in a completely different manner that does not prevent the virus from binding to ACE2 receptors.
Using a novel live-cell imaging platform described in a preprint, collaborators Alex Kreutzberger, Ph.D. and Tomas Kirchhausen, Ph.D., of Boston Children’s Hospital showed that SP1-77 prevents the virus from fusing its outer membrane with the membrane of the target cell. This thwarts the final necessary step that throws the door open to infection.
These features may inform the design of new SARS-CoV-2 vaccines. “SP1-77 binds the spike protein at a site that so far has not been mutated in any SARS-CoV-2 variant, broadly neutralizing current variants by a novel mechanism,” says Kirchhausen.
Reference: “An Antibody from Single Human VH-rearranging Mouse Neutralizes All SARS-CoV-2 Variants Through BA.5 by Inhibiting Membrane Fusion” by Sai Luo, Jun Zhang, Alex J.B. Kreutzberger, Amanda Eaton, Robert J. Edwards, Changbin Jing, Hai-Qiang Dai, Gregory D. Sempowski, Kenneth Cronin, Robert Parks, Adam Yongxin Ye, Katayoun Mansouri, Maggie Barr, Novalia Pishesha, Aimee Chapdelaine Williams, Lucas Vieira Francisco, Anand Saminathan, Hanqin Peng, Himanshu Batra, Lorenza Bellusci, Surender Khurana, S. Munir Alam, David C. Montefiori, Kevin O. Saunders, Ming Tian, Hidde Ploegh, Tom Kirchhausen, Bing Chen, Barton F. Haynes and Frederick W. Alt, 11 August 2022, Science Immunology.
DOI: 10.1126/sciimmunol.add5446
The study was funded by the Howard Hughes Medical Institute, the Bill & Melinda Gates Foundation, the NIH NIAID Consortia for HIV/AIDS Vaccine Development, the Massachusetts Consortium on Pathogen Readiness, Emergent Ventures, the Food and Drug Administration, the NIH Maximizing Investigators’ Research Award, NIH Grant AI163019, the Danish Technical University and SANA, IONIS, and a Harvard Virology Program NIH training grant.
Alt and Ming Tian, Ph.D., at Boston Children’s are authors of a patent application describing the mouse model. Luo, Haynes, and Alt are authors of patent applications describing the antibodies.
“Inescapable” COVID-19 Antibody Discovery – Neutralizes All Known SARS-CoV-2 Strains
An artistic rendering of antibodies surrounding a SARS-CoV-2 particle.
An antibody therapy that appears to neutralize all known
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Sunlight Neutralizes COVID-19 8 Times Faster Than Assumed
Researchers from UC Santa Barbara, Oregon State University, University of Manchester and ETH Zurich are calling for a closer look at sunlight’s ability to neutralize SARS-CoV-2 after finding that the most recent study on the matter was not up to par.
The team compared data from a July 2020 study that reported rapid sunlight inactivation of SARS-CoV-2 in a lab setting, with a theory of coronavirus inactivation by solar radiation that was published just a month earlier.
They noticed that the virus was inactivated as much as eight times faster in experiments than the most recent theoretical model predicted. “The theory assumes that inactivation works by having UV-B hit the RNA of the virus, damaging it,” UC Santa Barbara mechanical engineering professor and lead author Paolo Luzzatto-Fegiz said in a statement.
However, the research team felt that RNA inactivation by UV-B “might not be the whole story.” The scientists speculated that there could be another mechanism at play aside from RNA inactivation by UV-B rays such as UV-A, the less energetic component of sunlight.
“People think of UV-A as not having much of an effect, but it might be interacting with some of the molecules in the medium,” Luzzatto-Fezig explained. Those molecules in turn could be interacting with the virus, speeding up inactivation.
“So, scientists don’t yet know what’s going on,” Luzzatto-Fegiz said; “Our analysis points to the need for additional experiments to separately test the effects of specific light wavelengths and medium composition.”
If UV-A turns out to be capable of inactivating the coronavirus, this could prove very fruitful as there are now many types of inexpensive LED bulbs that are even stronger than natural sunlight. UV-A could also potentially be used to amplify the effect of air filtration systems at relatively low risk for human health.