Open AccessA Norovirus Uses Bile Salts To Escape Antibody Recognition While Enhancing Receptor Binding
Author(s) -
Alexis Williams,
Michael B. Sherman,
Hong Q. Smith,
Stefan Taube,
B. Montgomery Pettitt,
Christiane E. Wobus,
Thomas J. Smith
Publication year - 2021
Publication title -
journal of virology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 2.617
H-Index - 292
eISSN - 1070-6321
pISSN - 0022-538X
DOI - 10.1128/jvi.00176-21
Subject(s) - biology , antibody , capsid , norovirus , caliciviridae , biophysics , receptor , allosteric regulation , immune escape , virology , microbiology and biotechnology , virus , biochemistry , immune system , genetics
The major feature of calicivirus capsids is the 90 protruding domains (P domains) that are the site of cell receptor attachment and antibody epitopes. We demonstrated previously that these P domains are highly mobile and that bile causes these “floating” P domains in mouse norovirus (MNV) to contract onto the shell surface.
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