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2020 ; 122
(ä): 103849
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Bioinformatics studies on a function of the SARS-CoV-2 spike glycoprotein as the
binding of host sialic acid glycans
#MMPMID32658736
Robson B
Comput Biol Med
2020[Jul]; 122
(ä): 103849
PMID32658736
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SARS-CoV and SARS-CoV-2 do not appear to have functions of a hemagglutinin and
neuraminidase. This is a mystery, because sugar binding activities appear
essential to many other viruses including influenza and even most other
coronaviruses in order to bind to and escape from the glycans (sugars,
oligosaccharides or polysaccharides) characteristic of cell surfaces and saliva
and mucin. The S1 N terminal Domains (S1-NTD) of the spike protein, largely
responsible for the bulk of the characteristic knobs at the end of the spikes of
SARS-CoV and SARS-CoV-2, are here predicted to be "hiding" sites for recognizing
and binding glycans containing sialic acid. This may be important for infection
and the ability of the virus to locate ACE2 as its known main host cell surface
receptor, and if so it becomes a pharmaceutical target. It might even open up the
possibility of an alternative receptor to ACE2. The prediction method developed,
which uses amino acid residue sequence alone to predict domains or proteins that
bind to sialic acids, is naïve, and will be advanced in future work. Nonetheless,
it was surprising that such a very simple approach was so useful, and it can
easily be reproduced in a very few lines of computer program to help make quick
comparisons between SARS-CoV-2 sequences and to consider the effects of viral
mutations.