Use of gHgL for attachment of Epstein-Barr virus to epithelial cells compromises infection

J Virol. 2004 May;78(10):5007-14. doi: 10.1128/jvi.78.10.5007-5014.2004.

Abstract

Epstein-Barr virus (EBV) is a lymphotropic herpesvirus. However, access to B lymphocytes during primary infection may be facilitated by replication in mucosal epithelial cells. Attachment and penetration of EBV into these two cell types are fundamentally different. Both the distribution of receptors and the cellular origin of the virus impact the efficiency of infection. Epithelial cells potentially offer a wide range of receptors with which virus can interact. We report here on analyses of epithelial cells expressing different combinations of receptors. We find that the stoichiometry of the virus glycoprotein complex that includes gHgL and gp42 affects the use of gHgL not just for entry into epithelial cells but also for attachment. Penetration can be mediated efficiently with either a coreceptor for gp42 or gHgL, but the use of gHgL for attachment as well as penetration greatly compromises its ability to mediate entry.

Publication types

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

MeSH terms

  • Cell Line, Tumor
  • Epithelial Cells / virology
  • Glycoproteins / analysis
  • Glycoproteins / physiology
  • Herpesvirus 4, Human / physiology*
  • Histocompatibility Antigens Class II / physiology
  • Humans
  • Membrane Glycoproteins / physiology*
  • Molecular Chaperones / physiology*
  • Polyethylene Glycols / pharmacology
  • Receptors, Complement 3d / physiology
  • Receptors, Virus / physiology
  • Viral Envelope Proteins / physiology*
  • Viral Proteins / physiology*

Substances

  • Glycoproteins
  • Histocompatibility Antigens Class II
  • Membrane Glycoproteins
  • Molecular Chaperones
  • Receptors, Complement 3d
  • Receptors, Virus
  • Viral Envelope Proteins
  • Viral Proteins
  • glycoprotein H, Herpesvirus 4
  • glycoprotein L, Human herpesvirus 4
  • Polyethylene Glycols