The Native Antigen Company manufacturers highly purified Herpesvirus receptors using state-of-the-art expression and purification techniques. On request we can also undertake custom preparation of recombinant and native proteins for a broad range of disease states.
Herpesvirus Receptors Background
Herpesviruses comprise a large family of DNA viruses that cause infections and certain diseases in humans. There are eight herpesviruses for which humans are the primary host, including;
- Herpes simplex virus 1
- Herpes simplex virus 2
- Varicella-zoster virus
- Epstein-Barr virus
- Human herpesvirus-6
- Human herpesvirus-7
- Kaposi’s sarcoma herpes virus
The herpesvirus genome consists of a non-segmented, linear, double-stranded DNA molecule of approximately 120-250 kbp and encoding 70-200 genes. Herpesvirions consist of an envelope, a tegument, a nucleoscapsid and a core. Virions are 120-260 nm in diameter, and may be spherical to pleomorphic in shape with numerous evenly dispersed glycoprotein surface projections. The round nucleocapsid exhibits icosahedral symmetry and is approximately 100 nm in diameter. Viral DNA is located in the core of the mature virion.
Herpesviruses can utilise multiple Herpesvirus receptors during viral entry although some are considered binding receptors only, with binding being reversible and primarily aimed to concentrate virus on the cell surface without activating membrane fusion. Others are considered entry receptors, where binding triggers membrane fusion.
The entry of herpes simplex virus (HSV) into cells occurs in three steps. In the first, two viral glycoproteins, gC and gB, bind to heparan sulfate proteoglycans. Most, but not all, herpesviruses make their initial contact with cells by binding to glycosaminoglycans, usually heparan sulfate, on cell surface proteoglycans. This interaction is a conserved across the Herpesviridae family, likely directed to promote virus entry and endocytosis. In the second step, another glycoprotein, gD, interacts with at least one protein receptor, including nectin 1, an intercellular adhesion molecule, herpesvirus entry mediator (HVEM), a member of tumor necrosis factor α receptor family or 3-O-sulfated HS (3-OS HS). In the third step, gH, gL, and gB execute the fusion of viral envelope with the cell membrane, either plasma or endosomal. Other specific receptors that bind gB independently of HS to drive viral fusion include paired immunoglobulin-like receptor (PILRα), Myelin-associated glycoprotein (MAG) and Non-muscle myosin heavy chain (NMHC)-IIA. Receptors for gH/gL also include αvβ6- and αvβ8-integrins.
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We are pleased to offer a highly purified recombinant Herpesvirus receptor protein, manufactured in mammalian cells using bespoke expression and purification methods.
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