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Virus Genes. 2010 Jun;40(3):307-19. doi: 10.1007/s11262-010-0455-x. Epub 2010 Feb 17.

Characteristics of Epstein-Barr virus envelope protein gp42.

Author information

1
Department of Microbiology and Immunology, The Feinberg School of Medicine, Northwestern University, Chicago, IL 60611, USA.

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.

PMID:
20162447
PMCID:
PMC2854865
DOI:
10.1007/s11262-010-0455-x
[Indexed for MEDLINE]
Free PMC Article

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