Tyrosine phosphorylation of measles virus P-phosphoprotein in persistently infected neuroblastoma cells

Virus Genes. 1996;13(3):203-10. doi: 10.1007/BF00366980.

Abstract

Replication and encapsidation of measles virus (MV) requires the interaction between the nuclear protein (N) and the phosphoprotein (P). It is known that both proteins are phosphorylated on serine and threonine residues. Recently we have shown that N is phosphorylated on tyrosine in persistently-infected mouse neuroblastoma cells (NS20Y/MS). Here, we show that P in NS20Y/MS is also phosphorylated on tyrosine. To investigate whether cellular tyrosine kinases can bind and phosphorylate P, a solid phase kinase assay was employed. We show that bacterially-expressed MV P fragments, were phosphorylated on tyrosine by purified mouse c-Src protein-tyrosine kinase and when mixed with uninfected neuroblastoma cell (NS20Y) extracts, these P fragments were phosphorylated on tyrosine in addition to serine and threonine. These results imply that MV P is a substrate for tyrosine phosphorylation by cellular tyrosine kinase(s).

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Animals
  • CSK Tyrosine-Protein Kinase
  • Measles virus / metabolism*
  • Mice
  • Neuroblastoma
  • Phosphoproteins / genetics
  • Phosphoproteins / metabolism*
  • Phosphorylation
  • Protein Binding
  • Protein-Tyrosine Kinases / metabolism*
  • Recombinant Fusion Proteins / genetics
  • Recombinant Fusion Proteins / metabolism
  • Serine / metabolism
  • Threonine / metabolism
  • Tumor Cells, Cultured
  • Tyrosine / metabolism*
  • Viral Proteins / genetics
  • Viral Proteins / metabolism*
  • Virus Latency
  • src-Family Kinases

Substances

  • P protein, Sendai virus
  • Phosphoproteins
  • Recombinant Fusion Proteins
  • Viral Proteins
  • Threonine
  • Tyrosine
  • Serine
  • Protein-Tyrosine Kinases
  • CSK Tyrosine-Protein Kinase
  • src-Family Kinases