The major site of phosphorylation within the Rous sarcoma virus MA protein is not required for replication

Timothy D. Nelle, Michael F. Verderame, Jonathan Leis, John W. Wills

Research output: Contribution to journalArticle

6 Scopus citations

Abstract

About one-third of the MA protein in Rous sarcoma virus (RSV) is phosphorylated. Previous analyses of this fraction have suggested that serine residues 68 and 106 are the major sites of phosphorylation. As a follow-up to that study, we have characterized mutants which have these putative phosphorylation sites changed to alanine, either separately or together. None of the substitutions (S68A, S106A, or S68/106A) had an effect on the budding efficiency or infectivity of the virus. Upon examination of the 32P- labeled viral proteins, we found that the S68A substitution did not affect phosphorylation in vivo at all. In contrast, the S106A substitution prevented all detectable phosphorylation of MA, suggesting that there is only one major site of phosphorylation in MA. We also found that the RSV MA protein is phosphorylated on tyrosine, but the amount was low and detectable only with large numbers of virions and an antibody specific for phosphotyrosine.

Original languageEnglish (US)
Pages (from-to)1103-1107
Number of pages5
JournalJournal of virology
Volume72
Issue number2
DOIs
StatePublished - Feb 1998

All Science Journal Classification (ASJC) codes

  • Microbiology
  • Immunology
  • Insect Science
  • Virology

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