Mutations help epsilon coronavirus variants evade vaccine immunity: study

Three mutations in the peplomer of the epsilon variant of SARS-CoV-2 help avoid vaccines

Washington:

According to one study, three mutations in the peplomer of the epsilon variant of SARS-CoV-2 help the virus circumvent the protection provided by current vaccines or past COVID-19 infections.

Mutations also provide a concern variant named CAL.20C, completely avoiding certain monoclonal antibodies used in the clinic or antibodies made in the laboratory, and vaccinated people. It provides a means of reducing the effectiveness of antibodies from plasma.

A team led by researchers at the University of Washington in the United States visualized the transmission mechanism of the mutant to see what differs from the original composition of the coronavirus and what the impact of these changes is.

Findings published in the Journal Science on July 1 show that epsilon variants “depend on indirect and anomalous neutralization avoidance strategies.”

Neutralizing antibodies are an important specific defense against viral invasion.

Molecular clock analysis shows that precursors of the epsilon mutant emerged in California last May.

By the summer of 2020, it had branched into B.1.427 / B.1.429 lines and spread throughout the United States.

Since then, this variant has been reported in at least 34 countries.

Researchers tested the resilience of plasma to epsilon mutants from people exposed to the virus and those who were vaccinated.

They said the ability of plasma to neutralize the epsilon mutants of concern was reduced by about 2- to 3.5-fold.

Similar to the original SARS-CoV-2 virus identified in Wuhan, China in December 2019, this variant infects cells via spike glycoproteins (the structure that covers the surface of the virus) and into human cells. Helps to infect.

Researchers have discovered that epsilon mutations are responsible for the rearrangement of important regions of spiked glycoproteins.

Visualizing these mutations, according to researchers, helps explain why antibodies were difficult to bind to peplomers.

They said that one of the three mutations in the epsilon variant affected the receptor-binding domain of spike glycoproteins.

This mutation reduced the neutralizing activity of 14 of the 34 domain-specific neutralizing antibodies, including clinical-stage antibodies.

The other two of the three mutations in the mutant affected the N-terminal domain (the initiation of the peplomer).

The mutations also resulted in a complete loss of neutralization by 10 of the 10 antibodies specifically tested for the N-terminal domain of the peplomer, the researchers added.

(Except for the headline, this story has not been edited by NDTV staff and is published from the Syndicate Feed.)

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