Health
Antibodies that protect the identified covid-19
Boston : Scientists have identified human antibodies that could potentially prevent or limit the SARS-CoV-2 infection that causes COVID-19 disease.
Researchers at the University of Massachusetts Medical School (UMMS) in the United States have discovered and characterized a cross-reactive human monoclonal antibody (MAB) against the SARS-CoV-2 spike protein that blocks ACE2 receptor binding in airway mucosal tissues. It was
A study published in Nature Communications goes back 16 years to the origin of this rapid and important discovery. It was when UMMS researchers developed an effective IgG monoclonal antibody against the similar virus SARS.
When SARS-CoV-2 began to be recognized and spread, researchers found that the first MAB could help with this new infection.
They revived the old SARS program, harvested frozen cells developed 16 years ago, and thawed them to determine if what worked with one new coronavirus worked with another. The process to start has started.
Despite the 90% similarity between the two coronaviruses, the researchers said the monoclonal antibodies did not show the current binding to coronaviruses.
The team has drawn that experience in another research program to develop “secretory IgA (sIgA)” antibodies that play a key role in mucosal surface immunity.
This approach worked and generated antibodies with binding affinity and neutralizing activity.
This antibody was called MAb362.
“I was excited to learn that antibodies to SARS-CoV-2 were more effective at binding and neutralizing the virus when they were in the sIgA isotype of the antibody compared to normal circulating IgG antibodies,” he said. Professor Mark Klempner said. Medicine at UMMS.
“Naturally, sIgA antibodies coat mucosal surfaces such as respiratory, gastrointestinal infection (GI) and GU tracts, which are stabilized by mucosal layers on these surfaces, where pathogens to host cells It plays an important role in preventing the binding of .. and thus preventing infection,” Klempner said.
Based on these results, the team worked with biochemistry professor Celia Schiffer and her graduate student Shurong Hou to see if they could understand the nature of the effects of IgA antibodies.
They found that MAb 362 shares a very similar framework with another SARS antibody, MAb 80R, which has a crystal structure complexed with SAb-CoV.
Molecular models have revealed highly conserved protective epitopes within the receptor binding domain of the S protein. MAb362 neutralizes the authentic SARS-CoV-2 virus by directly competing for binding of the S protein to the hACE2 receptor.
“Thus, our study, which began during the coffee break conversation, yielded a unique IgA antibody that could be applied via mucosal administration, in combination with other systemic treatments for direct mucosal protection. Klempner said. PTI SAR SAR
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