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Crystal Structure of Epstein-Barr virus gp42 protein
Structural highlights
FunctionGP42_EBVB9 Plays a role in virion attachment to host B-lymphocytes, through binding to leukocyte antigen (HLA) class II and subsequently participates in fusion of the virion with host membranes. May act as a tropism switch that directs fusion with B-lymphocytes and inhibits fusion with epithelial cells.[1] Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMedEpstein-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 alpha helix bordering the essential hydrophobic pocket suggest a structural mechanism for triggering fusion. Structure of Epstein-Barr virus glycoprotein 42 suggests a mechanism for triggering receptor-activated virus entry.,Kirschner AN, Sorem J, Longnecker R, Jardetzky TS Structure. 2009 Feb 13;17(2):223-33. PMID:19217393[2] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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