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Virology. 2007 Nov 10;368(1):102-13. Epub 2007 Jul 25.

Characterization of EBV gB indicates properties of both class I and class II viral fusion proteins.

Author information

1
Department of Biochemistry, Molecular Biology, Cell Biology, Northwestern University, Evanston, IL 60208, USA.

Abstract

To gain insight into Epstein-Barr virus (EBV) glycoprotein B (gB), recombinant, secreted variants were generated. The role of putative transmembrane regions, the proteolytic processing and the oligomerization state of the gB variants were investigated. Constructs containing 2 of 3 C-terminal hydrophobic regions were secreted, indicating that these do not act as transmembrane anchors. The efficiency of cleavage of the gB furin site was found to depend on the nature of C-terminus. All of the gB constructs formed rosette structures reminiscent of the postfusion aggregates formed by other viral fusion proteins. However, substitution of putative fusion loop residues, WY(112-113) and WLIY(193-196), with less hydrophobic amino acids from HSV-1 gB, produced trimeric protein and abrogated the ability of the EBV gB ectodomains to form rosettes. These data demonstrate biochemical features of EBV gB that are characteristic of other class I and class II viral fusion proteins, but not of HSV-1 gB.

PMID:
17655906
PMCID:
PMC2131761
DOI:
10.1016/j.virol.2007.06.031
[Indexed for MEDLINE]
Free PMC Article

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