Journal
ANGEWANDTE CHEMIE-INTERNATIONAL EDITION
Volume 56, Issue 29, Pages 8490-8494Publisher
WILEY-V C H VERLAG GMBH
DOI: 10.1002/anie.201703059
Keywords
chemokine-binding proteins; leucine; peptide ligation; protein synthesis; sulfation
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Funding
- University of Sydney
- Monash Univerity
- Australian Research Council [DP160101324, FT130100150]
- Australian Research Council [FT130100150] Funding Source: Australian Research Council
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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 bselenoleucine 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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