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What We Know About SARS-CoV-2 One Year Later: Part 2
Sponsored Content by ACROBiosystemsApr 14 2021
The S protein of SARS-CoV had been studied extensively before the SARS-CoV-2 outbreak. Among other structural proteins of SARS-CoV-2, the S protein was discovered to be highly immunogenic and effective at neutralizing antibodies recovered from SARS patients were directed at S protein.
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Research into therapeutics and vaccines against SARS-CoV-2 was focused immediately on the S protein. Although the four structural proteins of the novel SARS-CoV share over 90% in sequence identity with SARS-CoV-2, S protein consisting of S1 and S2 subunits diverged had just 77% sequence similarity.
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The S1 subunit contains the NTD or the N-terminal domain and Receptor binding domain (RBD), which binds to the human angiotensin-converting enzyme-2 (ACE2) mainly through direct interaction with the receptor-binding motif (RBM).
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Brazilian SARS-CoV-2 P.1 variant shows resistance to antibody neutralization
Researchers in the United States say the severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) variant – P.1 – that has recently emerged in Brazil shows a worrying level of resistance to neutralization by antibodies.
The SARS-CoV-2 virus is the agent responsible for the coronavirus disease 2019 (COVID-19) pandemic that poses an ongoing threat to mankind and has now claimed the lives of more than 2.56 million people globally.
The team from Columbia University in New York found that as well as being resistant to several neutralizing monoclonal antibodies (mAbs), the P.1 variant is also over six times more resistant to neutralization by convalescent plasma and more than twice as resistant to sera from vaccinees than the wildtype virus.
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