Characteristics of Epstein-Barr virus envelope protein gp42.

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.

• Authors: Pamela L Shaw, Austin N Kirschner, Theodore S Jardetzky, Richard Longnecker
• Journal: Virus genes (Virus Genes) Vol. 40 Issue 3 Pg. 307-19 (Jun 2010) ISSN: 1572-994X [Electronic] United States
• PMID: 20162447 (Publication Type: Journal Article, Research Support, N.I.H., Extramural)

Chemical References

• BZLF2 protein, Herpesvirus 4, Human
• Glycoproteins
• Viral Proteins
• Calcium

Topics

• Amino Acid Sequence
• Calcium (metabolism)
• Computational Biology
• Glycoproteins (genetics, physiology)
• Herpesvirus 4, Human (genetics, physiology)
• Models, Molecular
• Molecular Sequence Data
• Phylogeny
• Protein Binding
• Protein Structure, Secondary
• Protein Structure, Tertiary
• Sequence Homology
• Viral Proteins (genetics, physiology)
• Virus Internalization