Emergence of mutations and possible antigenic drift in the surface
glycoprotein of SARS-CoV-2 (COVID-19)
Abstract
Recently (2019), a novel coronavirus (SARS-CoV-2) first reported in
Wuhan, China has been declared a pandemic by the World Health
Organization and is rapidly spreading throughout the globe which is
associated with high morbidity and mortality, especially in the elderly
and those with existing chronic conditions. SARS-CoV-2 infects cells
through interaction of its surface glycoprotein with the human
angiotensin converting enzyme 2 (ACE-2). This study conducted a analysis
of mutation frequency in the surface glycoprotein of 796 sequenced
SARS-CoV-2 isolates from different geographical locations in the GISAID
and GenBank databases. Multiple sequence alignment analysis of the
surface glycoprotein identified 64 different mutations at the protein
level spanning multiple geographic locations globally. A cluster of
mutations was identified in the receptor binding domain (RBD) of the
surface glycoprotein. Significantly, the analysis showed that 68.5% of
the isolates contain a D614 residue compared to 31.5% which contain a
G614 suggesting virus is spreading in two forms. Furthermore, our
investigation found that one isolate from Belgium had acquired 5
cumulative mutations in the surface glycoprotein indicating possible
antigenic drift. The findings of this study are of critical importance
for the design of vaccines and novel drugs against this severe acute
respiratory syndrome coronavirus.