Sites of phosphorylation of P and V proteins from Hendra and Nipah viruses: newly emerged members of Paramyxoviridae

Virus Res. 2003 Mar;92(1):55-65. doi: 10.1016/s0168-1702(02)00313-1.

Abstract

Hendra (HeV) and Nipah (NiV) viruses are newly emerged, zoonotic viruses and their genomes have nucleotide and predicted amino acid homologies placing them in the subfamily Paramyxoviridae. The polymerase-associated phosphoproteins (P proteins) of paramyxoviruses have been shown, by direct and indirect methods, to be highly phosphorylated. In this study, a comprehensive comparison of in vivo phosphorylation of HeV and NiV P proteins, derived from virus particles, was achieved by a direct approach using electrospray ionization ion trap mass spectrometry (ESI-IT-MS). Phosphorylation sites for the P proteins were determined at Ser-224 and Thr-239 in HeV and at Ser-240 and Ser-472 in NiV. These phosphorylation patterns do not appear to be consistent with those reported for other paramyxoviruses. Protein V, a product of a frame shift in the P protein gene, was identified by specific antibodies in HeV preparations but not in NiV. HeV V protein was found to contain phosphoserine but not phosphothreonine. In addition, P proteins from both viruses were found to be modified by N-terminal acetylation.

MeSH terms

  • Amino Acid Sequence
  • Animals
  • Binding Sites
  • Chlorocebus aethiops
  • Humans
  • Molecular Sequence Data
  • Paramyxovirinae / genetics
  • Paramyxovirinae / metabolism*
  • Phosphorylation
  • Sequence Homology, Amino Acid
  • Spectrometry, Mass, Electrospray Ionization
  • Vero Cells
  • Viral Proteins / chemistry
  • Viral Proteins / genetics
  • Viral Proteins / metabolism*

Substances

  • Viral Proteins