Mutations in SARS-CoV-2 spike protein receptor-binding domains may
result in escape variants resistant to therapeutics and vaccines

Date:
March 1, 2022
Source:
PLOS
Summary:
The SARS-CoV-2 virus is continuously evolving and structural changes
to the virus may impact the efficacy of antibody therapies and
vaccines. A study describes the structural and functional landscape
of neutralizing antibodies against SARS-CoV-2 spike protein and
discuss the effects of mutations on the virus spike protein that
may allow it to evade antibody responses.



FULL STORY ==========================================================================
The SARS-CoV-2 virus is continuously evolving and structural changes to
the virus may impact the efficacy of antibody therapies and vaccines. A
study publishing Feb. 17 in PLOS Pathogens by Anshumali Mittal at the University of Pittsburgh, USA and colleagues describes the structural
and functional landscape of neutralizing antibodies against SARS-CoV-2
spike protein and discuss the effects of mutations on the virus spike
protein that may allow it to evade antibody responses.


==========================================================================
All viruses mutate as they evolve, and most mutations have either negative
or neutral effects on viral fitness. However, some mutations give viruses
a selective advantage, making them more infectious, transmittable, and resistant to antibody responses and therapeutics. To better understand
the relationship between immune responses to SARS-CoV-2 virus and how
mutations may allow the virus to escape neutralization, researchers
conducted a review of the literature, comprising approximately 139
studies. They synthesized research on emerging SARS-CoV-2 variants,
described the structural basis of how antibodies may neutralize
SARS-CoV-2, and mapped out the spike protein mutations or "escape
variants" that resist antibody binding and neutralization.

The researchers summarized the structure-based classification of the
spike protein receptor-binding domains (RBD) that target antibodies
to better understand the molecular mechanisms of neutralization. They
also further described the RBD escape mutations for several antibodies
that resist vaccine- elicited and therapeutically relevant antibodies
binding. Future studies are needed, however, to better understand how
these mutations may affect illness severity and mortality.

According to the authors, "The potency of therapeutic antibodies
and vaccines partly depends on how readily the virus can escape
neutralization. The SARS- CoV-2 virus will continue to evolve
resulting in the emergence of escape variants; therefore, worldwide
genomic surveillance, better vaccination drive, development of
broadly neutralizing antibodies, and new drugs are vital to combat
COVID-19." Mittal adds, "Structure-based escape maps combined
with computational modelling are valuable tools to understand how
mutations at each residue affect the binding of an antibody, and can
be utilized to facilitate the rational design of escape-resistant
antibody therapeutics, vaccines and other countermeasures." ========================================================================== Story Source: Materials provided by PLOS. Note: Content may be edited
for style and length.


========================================================================== Journal Reference:
1. Anshumali Mittal, Arun Khattri, Vikash Verma. Structural and
antigenic
variations in the spike protein of emerging SARS-CoV-2
variants. PLOS Pathogens, 2022; 18 (2): e1010260 DOI:
10.1371/journal.ppat.1010260 ==========================================================================

Link to news story: https://www.sciencedaily.com/releases/2022/03/220301162006.htm

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