Sulfation of the Human Cytomegalovirus Protein UL22A Enhances Binding to the Chemokine RANTES

Xiaoyi Wang, Julie Sanchez, Martin J. Stone, Richard J. Payne

Research output: Contribution to journalArticleResearchpeer-review

18 Citations (Scopus)

Abstract

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.

Original languageEnglish
Pages (from-to)8490-8494
Number of pages5
JournalAngewandte Chemie - International Edition
Volume56
Issue number29
DOIs
Publication statusPublished - 10 Jul 2017

Keywords

  • chemokine-binding proteins
  • leucine
  • peptide ligation
  • protein synthesis
  • sulfation

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