EBV Glycoprotein H (Ectodomain) [His] (DAG2018)

EBV Glycoprotein H (aa 1 - 679) (Ectodomain) [His], recombinant protein from HEK 293 cells

Product Overview
C-terminal 6xHis tagged ectodomain of gH (EBV) protein (a.a. 1-679)
≥ 95%
Each vial contains 100 μg of purified protein in PBS.
1 mg/ml
2-8°C short term, -20°C long term
The Epstein–Barr virus (EBV), also called human herpesvirus 4 (HHV-4), is a virus of the herpes family and is one of the most common viruses in humans. It is best known as the cause of infectious mononucleosis (glandular fever). It is also associated with particular forms of cancer, such as Hodgkin's lymphoma, Burkitt's lymphoma, nasopharyngeal carcinoma, and central nervous system lymphomas associated with HIV. There is evidence that infection with the virus is associated with a higher risk of certain autoimmune diseases, especially dermatomyositis, systemic lupus erythematosus, rheumatoid arthritis and multiple sclerosis. Infection with EBV occurs by the oral transfer of saliva
Antigen Description
The amino terminus of gH has been implicated as being critical to its role in support of cell fusion. Potentially alpha helical residues 377–397 of the gH homolog of herpes simplex virus have been proposed to represent an internal fusion peptide and similar motifs are found in equivalent positions in other herpesviruses. Residues that are part of a heptad repeat sequence just downstream of this peptide are also essential to fusion. Peptides corresponding to a putative coiled-coil domain in human cytomegalovirus gH between residues 108 and 128 inhibit membrane fusion. Mutations in residues 52–79 of EBVgH which are also predicted, although perhaps less robustly, to be part of a coil-coiled domain, impact fusion with both B cells and epithelial cells. However, residues close to the transmembrane domain of herpes simplex virus gH have also been shown to be essential and our work is consistent with this.
Epstein–Barr virus; Herpesviridae; Gammaherpesvirinae; Lymphocryptovirus; Human herpesvirus 4; HHV-4; EBV; gH protein; EBV gH protein; Epstein–Barr virus gH protein


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Immunization with Components of the Viral Fusion Apparatus Elicits Antibodies That Neutralize Epstein-Barr Virus in B Cells and Epithelial Cells


Authors: Bu, Wei; Joyce, M. Gordon; Hanh Nguyen; Banh, Dalton V.; Aguilar, Fiona; Tariq, Zeshan; Yap, Moh Lan; Tsujimura, Yusuke; Gillespie, Rebecca A.; Tsybovsky, Yaroslav; Andrews, Sarah F.; Narpala, Sandeep R.; McDermott, Adrian B.; Rossmann, Michael G.; Yasutomi, Yasuhiro; Nabel, Gary J.; Kanekiyo, Masaru; Cohen, Jeffrey I.

Epstein-Barr virus (EBV) causes infectious mononucleosis and is associated with epithelial-cell cancers and B cell lymphomas. An effective EBV vaccine is not available. We found that antibodies to the EBV glycoprotein gH/gL complex were the principal components in human plasma that neutralized infection of epithelial cells and that antibodies to gH/gL and gp42 contributed to B cell neutralization. Immunization of mice and nonhuman primates with nanoparticle vaccines that displayed components of the viral-fusion machinery EBV gH/gL or gH/gL/gp42 elicited antibodies that potently neutralized both epithelial-cell and B cell infection. Immune serum from nonhuman primates inhibited EBV-glycoprotein-mediated fusion of epithelial cells and B cells and targeted an epitope critical for virus-cell fusion. Therefore, unlike the leading EBV gp350 vaccine candidate, which only protects B cells from infection, these EBV nanoparticle vaccines elicit antibodies that inhibit the virus-fusion apparatus and provide cell-type-independent protection from virus infection.

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


Authors: Backovic, Marija; Leser, George P.; Lamb, Robert A.; Longnecker, Richard; Jardetzky, Theodore S.

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, WY112-113 and WLIY193-196, 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 11 viral fusion proteins, but not of HSV-1 gB. (C) 2007 Elsevier Inc. All rights reserved.

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