C-terminal 6xHis tagged ectodomain of gH (EBV) protein (a.a. 1-344) (Genebank #: P03231) in complex with gp42 ectodomain (EBV)(Strain B95-8) (Genebank #: YP_401672)(a.a. 31-223), and gL(a.a. 25-137) (Genebanka #: CAD53428).
Nature
Recombinant
Tag/Conjugate
His
Purity
≥ 95%
Format
Liquid
Concentration
1 mg/ml
Buffer
PBS buffer
Preservative
None
Storage
Store at 2-8°C for short term. Store at -20°C for long term. Avoid multiple freeze/thaw cycles
Introduction
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
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Background
The Epstein-Barr virus (EBV), is also known as human herpesvirus 4. It has enveloped structure and double-stranded DNA genome. EBV is very widely infected with up to 95 percent of adults. This virus has strong associations with infectious mononucleosis, some forms of lymphoma and epithelial cell tumors. This viral capsid wraps around a 172 kb-long genome of linear double-stranded DNA that encodes more than 80 virus proteins and various non-coding RNAs and miRNAs.
The pathogenesis of EBV is like any herpesvirus — extremely complicated and dual-tipped, with predominant infections of B lymphocytes and epithelial cells. Each infection stage is made up of the concerted action of various surface glycoproteins that aid viral attachment, the production of fusion proteins and the binding of the viral envelope to the cell membrane or endosomal membrane. The EBVs slather the host cell with a complex of envelope glycoproteins – gp350/220, gp42, gH/gL and gB. When the virus strikes B lymphocytes, the glycoprotein gp350 binds to CD21 or CD35 on the surface of host cells, and this in turn binds the virus to the B cell. Then, gp42 of the gH/gL/gp42 heterotrimer binds to HLA-II molecules, which generates signals to recombine with the gH/gL complex and finally fusion of membranes through gB. In contrast, during epithelial cell infection, the gH/gL complex interacts with integrin receptors such as αvβ5, αvβ6, and αvβ8 through its KGD region and also binds to EphA2 receptor via gL. This interaction subsequently activates gB protein, triggering the fusion process between the viral envelope and the host cell membrane.
Figure 1. The process of EBV entry into host cells (Source: Bu GL, et al. 2022)
Such EBV glycoproteins are neutralising antibodies' targets. Their neutralising antibodies have different neutralising functions because of these different roles that these glycoproteins play in the viral infection process. gH/gL complex – a mixture of type I transmembrane protein gH and secreted protein gL – is a key glycoprotein for EBV's assault on B lymphocytes and epithelial cells, and one that antibodies are keen to kill. Antibodies directed against gH/gL can demonstrate high neutralization efficacy in dual infection models. gp42 is essential for EBV infection of B lymphocytes. Neutralizing antibodies against gp42 can effectively block the virus from infecting B cells, but they show no neutralizing activity in epithelial cell models.
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Figure 1. The process of EBV entry into host cells
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