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

Borza CM, Morgan AJ, Turk SM, Hutt-Fletcher LM
J Virol. 2004 78 (10): 5007-14

PMID: 15113881 · PMCID: PMC400351 · DOI:10.1128/jvi.78.10.5007-5014.2004

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.

MeSH Terms (13)

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

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