Prediction of tyrosine sulfation sites in animal viruses
Autor: | Willy Hsu, Samuel Louie, Justin Liu, Grace L. Rosenquist, Hugh B. Nicholas, Brian L. Chang, Henry C. Lin, Melinda Young, Kevin Tsai |
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Rok vydání: | 2003 |
Předmět: |
Tyrosine sulfation
viruses Molecular Sequence Data Sus scrofa Biophysics Hemagglutinins Viral Sequence Homology Hemagglutinin (influenza) Biochemistry Virus Conserved sequence Viral Proteins Sulfation Species Specificity Sequence Analysis Protein Animals Humans Amino Acid Sequence Horses Tyrosine Molecular Biology Peptide sequence Conserved Sequence chemistry.chemical_classification biology Sulfates virus diseases Cell Biology Amino acid Ducks chemistry Influenza A virus biology.protein Capsid Proteins Cattle Receptors Chemokine Sequence Alignment Algorithms |
Zdroj: | Biochemical and Biophysical Research Communications. 312:1154-1158 |
ISSN: | 0006-291X |
DOI: | 10.1016/j.bbrc.2003.11.047 |
Popis: | 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. |
Databáze: | OpenAIRE |
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