Polyomavirus major capsid protein VP1 is modified by tyrosine sulfuration.
Polyomavirus was propagated in primary mouse kidney cell monolayers and 35S-sulfate labeled by maintaining the infected cells in serum-free Eagle medium supplemented with 35S-labeled sodium sulfate. Sodium dodecyl sulfate-polyacrylamide gel electrophoresis of CsCI gradient-purified 35S-sulfate-labeled virions followed by fluorography indicated that the polyomavirus-coded major capsid protein VP1 incorporated this radiolabel. Two-dimensional gel electrophoresis followed by fluorography revealed 35S-sulfate incorporation into only two of the six VP1 isoelectric species (E and F). Amino acid analysis of 35S-sulfate labeled VP1 by enzymatic hydrolysis followed by two-dimensional thin-layer electrophoresis revealed the presence of 35S-sulfate-labeled tyrosine-O-sulfate.
D000818:Animals; D002213:Capsid / Q000378:metabolism*; D002460:Cell Line; D051379:Mice; D011120:Polyomavirus / Q000378:metabolism*; D011499:Protein Processing, Post-Translational; D013431:Sulfates / Q000378:metabolism; D014443:Tyrosine / Q000378:metabolism
D013431:Sulfates; D014443:Tyrosine