Prediction of tyrosine sulfation sites in animal viruses

Henry C. Lin, Kevin Tsai, Brian L. Chang, Justin Liu, Melinda Young, Willy Hsu, Samuel Louie, Hugh B. Nicholas, Grace L. Rosenquist

Research output: Contribution to journalArticlepeer-review

13 Scopus citations


Post-translational modification of proteins by tyrosine sulfation enhances the affinity of extracellular ligand-receptor interactions important in the immune response and other biological processes in animals. For example, sulfated tyrosines in polyomavirus and varicella-zoster virus may help modulate host cell recognition and facilitate viral attachment and entry. Using a Position-Specific-Scoring-Matrix with an accuracy of 96.43%, we analyzed the possibility of tyrosine sulfation in all 1517 animal viruses available in the Swiss-Prot database. From a total of 97,729 tyrosines, we predicted 5091 sulfated tyrosine sites from 1024 viruses. Our site predictions in hemagglutinin of influenza A, VP4 of rotavirus, and US28 of cytomegalovirus strongly suggest an important link between tyrosine sulfation and viral disease mechanisms. In each of these three viral proteins, we observed highly conserved amino acid sequences surrounding predicted sulfated tyrosine sites. Tyrosine sulfation appears to be much more common in animal viruses than is currently recognized.

Original languageEnglish (US)
Pages (from-to)1154-1158
Number of pages5
JournalBiochemical and Biophysical Research Communications
Issue number4
StatePublished - Dec 26 2003


  • Cytomegalovirus
  • Influenza A
  • Post-translational modification
  • Rotavirus
  • Sulfation
  • Tyrosine
  • Virus

ASJC Scopus subject areas

  • Biochemistry
  • Biophysics
  • Molecular Biology


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