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Sulfation of the Human Cytomegalovirus Protein UL22A Enhances Binding to the Chemokine RANTES
Author(s) -
Wang Xiaoyi,
Sanchez Julie,
Stone Martin J.,
Payne Richard J.
Publication year - 2017
Publication title -
angewandte chemie international edition
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 5.831
H-Index - 550
eISSN - 1521-3773
pISSN - 1433-7851
DOI - 10.1002/anie.201703059
Subject(s) - sulfation , chemokine , tyrosine , chemistry , cytomegalovirus , biochemistry , chemokine receptor , microbiology and biotechnology , biology , virus , virology , herpesviridae , receptor , viral disease
UL22A is an 83 amino acid chemokine‐binding protein produced by human cytomegalovirus that likely assists the virus in dampening the host antiviral response. We proposed that UL22A is sulfated on two tyrosine residues and tested this hypothesis through the chemical synthesis of a small library of differentially sulfated protein variants. The (sulfo)proteins were efficiently prepared using a novel β‐selenoleucine motif to facilitate one‐pot ligation–deselenization chemistry. Tyrosine sulfation of UL22A proved critical for RANTES binding, with the doubly sulfated variant exhibiting an improvement in binding of 2.5 orders of magnitude compared to the unmodified protein.