Sulfation of the Human Cytomegalovirus Protein UL22A Enhances Binding to the Chemokine RANTES
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ArticleAbstract
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 ...
See moreUL22A 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.
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See moreUL22A 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.
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Date
2017-05-09Publisher
WileyLicence
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This is the peer reviewed version of the following article: X. Wang, J. Sanchez, M. J. Stone, R. J. Payne, Angew. Chem. Int. Ed. 2017 , 56 , 8490., which has been published in final form at doi.org/10.1002/ange.201703059. This article may be used for non-commercial purposes in accordance with Wiley Terms and Conditions for Use of Self-Archived Versions.Faculty/School
Faculty of ScienceShare