New antibody neutralizes all known SARS-CoV-2 variants

3D printing of SARS-CoV-2 spike protein in front of 3D printing of SARS-CoV-2 viral particles. The spike protein (foreground) allows the virus to enter and infect human cells. In the virus model, the surface of the virus (blue) is covered with spike proteins (red) that allow the virus to enter and infect human cells. Credit: NIH

last week, California researcher showed how we are applying our COVID-19 wastewater study to the current monkeypox outbreak. This week, Boston researchers tapped into a humanized mouse model previously used to search for HIV antibodies in the ongoing battle against SARS-CoV-2.

Using a mouse model, the Boston Children’s Hospital team discovered antibodies that neutralize all known SARS-CoV-2 variants of concern, including all Omicron variants.

“We hope that this humanized antibody will prove to be as effective in neutralizing SARS-CoV-2 in patients as has been demonstrated in previous preclinical evaluations.” research.

Alt and his colleague Sai Luo first inserted two human gene segments into mice to push B cells to rapidly produce a range of humanized antibodies. Mice were then exposed to the SARS-CoV-2 spike protein from the original strain of virus. In response, the engineered mice produced nine strains of humanized antibodies that bound spikes.

Working with scientists at Duke University, the team found that three of the nine lineages of antibodies were potent neutralizers of the original virus strain. The SP1-77 antibody and other members of its family showed very broad activity neutralizing alpha, beta, gamma, delta, and all previous and current Omicron strains.

What makes SP1-77 novel and unique is where it binds to the spike protein. Most existing antibodies, whether therapeutic or made in response to vaccines, bind to spike receptor-binding domains (RBDs) at specific locations, allowing SARS-CoV-2 to target cellular ACE2. Prevents binding to receptors. infection.

SP1-77 also binds to RBD, but in a manner that does not block virus binding to the ACE2 receptor. Rather, the researchers found that SP1-77 prevented the virus from fusing its outer membrane with that of target cells. This prevents the final step needed to open the door to infection.

Like HIV, SARS-CoV-2 is a rapidly evolving RNA virus that can evade even the first vaccines and boosters. In particular, the omicron mutant containing numerous mutations in the spike protein showed great resistance to most previous SARS-CoV-2 neutralizing antibodies and antibodies induced by vaccination. For example, in India, the Omicron subvariant BA.2.75 is causing a spike in infections.

That’s what makes SP1-77 such an interesting and forward-looking discovery.

“SP1-77 binds to the spike protein at a site not previously mutated in any SARS-CoV-2 variant,” said Tomas Kirchhausen, a senior investigator at Boston Children’s Hospital.

Next, researchers plan to test SP1-77 in vivoIf antibodies continue to show broad neutralizing activity against SARS-CoV-2 variants in vivoThe team says SP1-77 has potential as a therapeutic agent for current and evolving VOCs.

“Also, SP1-77 may be useful in cocktails with other neutralizing antibodies such as LY-CoV1404. This antibody potently neutralizes all tested VOCs via the ACE2 blocking mechanism. ’” explains the researchers in their paper. scientific immunology.

Ultimately, scientists agree that SP1-77’s non-traditional neutralization mechanisms may inspire the design of new SARS-CoV-2 vaccines.

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