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 language | English |
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Pages (from-to) | 8490-8494 |
Number of pages | 5 |
Journal | Angewandte Chemie - International Edition |
Volume | 56 |
Issue number | 29 |
DOIs | |
Publication status | Published - 10 Jul 2017 |
Keywords
- chemokine-binding proteins
- leucine
- peptide ligation
- protein synthesis
- sulfation