Characteristics of Epstein-Barr virus envelope protein gp42.

Shaw PL, Kirschner AN, Jardetzky TS, Longnecker R
Virus Genes. 2010 40 (3): 307-19

PMID: 20162447 · PMCID: PMC2854865 · DOI:10.1007/s11262-010-0455-x

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.

MeSH Terms (14)

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

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