Canine herpesvirus ORF2 is a membrane protein modified by N-linked glycosylation

Virus Res. 2002 Jul;87(1):1-9. doi: 10.1016/s0168-1702(01)00424-5.

Abstract

Canine herpesvirus (CHV) ORF2, located downstream of the glycoprotein C (gC) gene, has homologues with some of the alphaherpesviruses. To characterize CHV OFR2, a recombinant CHV carrying a LacZ gene in the ORF2 locus, and recombinant vaccinia virus expressing ORF2 protein were constructed. Northern blot analysis revealed ORF2 and a gamma2 class late gene, and its protein product was detectable in CHV-infected cells reacted with ORF2 protein antiserum. Tunicamycin and N-glycosidase F treatment revealed that the ORF2 protein was modified by N-linked glycosylation. Fractionation and immune fluorescence analyses of the CHV-infected cells showed the ORF2 as a membrane protein transportable to the surface of infected cells. In vitro, the ORF2 protein did not affect viral replication and cell-to-cell viral spreading. Present findings represent the first evidence pointing to the CHV ORF2 as a membrane protein modified by an N-linked glycosylation.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Animals
  • Blotting, Western / methods
  • Cell Line
  • Dogs
  • Female
  • Glycoproteins / genetics
  • Glycoproteins / metabolism*
  • Glycosylation
  • Herpesvirus 1, Canid / genetics*
  • Herpesvirus 1, Canid / growth & development
  • Mice
  • Mice, Inbred BALB C
  • Microscopy, Confocal
  • Open Reading Frames*
  • RNA, Viral
  • Recombination, Genetic
  • Viral Envelope Proteins / genetics
  • Viral Envelope Proteins / metabolism*

Substances

  • Glycoproteins
  • RNA, Viral
  • Viral Envelope Proteins