Structure of Epstein-Barr Virus Glycoprotein 42 Suggests a Mechanism for Triggering Receptor-Activated Virus Entry

Austin N. Kirschner, Jessica Sorem, Richard Longnecker, Theodore S. Jardetzky*

*Corresponding author for this work

Research output: Contribution to journalArticle

42 Scopus citations

Abstract

Epstein-Barr virus requires glycoproteins gH/gL, gB, and gp42 to fuse its lipid envelope with B cells. Gp42 is a type II membrane protein consisting of a flexible N-terminal region, which binds gH/gL, and a C-terminal lectin-like domain that binds to the B-cell entry receptor human leukocyte antigen (HLA) class II. Gp42 triggers membrane fusion after HLA binding, a process that requires simultaneous binding to gH/gL and a functional hydrophobic pocket in the lectin domain adjacent to the HLA binding site. Here we present the structure of gp42 in its unbound form. Comparisons to the previously determined structure of a gp42:HLA complex reveals additional N-terminal residues forming part of the gH/gL binding site and structural changes in the receptor binding domain. Although the core of the lectin domain remains similar, significant shifts in two loops and an α helix bordering the essential hydrophobic pocket suggest a structural mechanism for triggering fusion.

Original languageEnglish (US)
Pages (from-to)223-233
Number of pages11
JournalStructure
Volume17
Issue number2
DOIs
StatePublished - Feb 13 2009

Keywords

  • MICROBIO
  • PROTEINS

ASJC Scopus subject areas

  • Structural Biology
  • Molecular Biology

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