An N-terminal domain of herpes simplex virus type Ig E is capable of forming stable complexes with gI

J Virol. 2001 Dec;75(23):11897-901. doi: 10.1128/JVI.75.23.11897-11901.2001.

Abstract

Using limited proteolytic analyses, we show that gE present in soluble herpes simplex virus type 1 gE-gI complexes is cleaved into a C-terminal (CgE) and an N-terminal (NgE) domain. The domain boundary is in the vicinity of residue 188 of mature gE. NgE, but not CgE, forms a stable complex with soluble gI.

Publication types

  • Research Support, Non-U.S. Gov't
  • Research Support, U.S. Gov't, P.H.S.

MeSH terms

  • Amino Acid Sequence
  • Animals
  • Antibodies, Monoclonal / immunology
  • CHO Cells
  • Cricetinae
  • Electrophoresis, Polyacrylamide Gel
  • Glycoproteins / chemistry
  • Glycoproteins / immunology
  • Glycoproteins / metabolism
  • Glycoproteins / physiology*
  • Herpesvirus 1, Human / immunology
  • Herpesvirus 1, Human / physiology*
  • Protein Binding
  • Viral Envelope Proteins / chemistry
  • Viral Envelope Proteins / immunology
  • Viral Envelope Proteins / metabolism
  • Viral Envelope Proteins / physiology*

Substances

  • Antibodies, Monoclonal
  • Glycoproteins
  • Viral Envelope Proteins