Characteristics of Epstein-Barr virus envelope protein gp42

Pamela L. Shaw, Austin N. Kirschner, Theodore S. Jardetzky, Richard Longnecker*

*Corresponding author for this work

Research output: Contribution to journalReview article

11 Scopus citations

Abstract

Epstein-Barr virus (EBV) glycoprotein 42 (gp42) is a membrane protein essential for fusion and entry of EBV into host B-lymphocytes. Gp42 is a member of the protein-fold family C-type lectin or lectin-like domains (CLECT or CTLD) and specifically is classified as a natural-killer receptor (NKR)-like CLECT. Literature review and phylogenetic comparison show that EBV gp42 shares a common structure with other NKR-like CLECTs and possibly with many viral CTLDs, but does not appear to exhibit some common binding characteristics of many CTLDs, such as features required for calcium binding. The flexible N-terminal region adjacent to the CTLD fold is important for binding to other EBV glycoproteins and for a cleavage site that is necessary for infection of host cells. From structural studies of gp42 unbound and bound to receptor and extensive mutational analysis, a general model of how gp42 triggers membrane fusion utilizing both the flexible N-terminal region and the CTLD domain has emerged.

Original languageEnglish (US)
Pages (from-to)307-319
Number of pages13
JournalVirus Genes
Volume40
Issue number3
DOIs
StatePublished - Jun 1 2010

Keywords

  • EBV
  • Epstein-Barr virus
  • Glycoprotein
  • Gp42
  • Herpesvirus
  • Viral entry

ASJC Scopus subject areas

  • Molecular Biology
  • Genetics
  • Virology

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