Herpes simplex virus 2 envelope glycoproteins (HSV-2 glycoproteins) (HSV-2 glycoproteins)

Herpes simplex virus 2 (HSV-2) envelope glycoproteins are a set of surface-exposed proteins, primarily including gB, gC, gD, gH, and gL, that collectively manage the complex process of viral entry into human host cells [1]. Glycoprotein D (gD) is the key receptor-binding protein that initiates infection by interacting with host cell receptors such as nectin-1 and herpesvirus entry mediator (HVEM) [2][3]. Following attachment, the fusion machinery consisting of gB and the gH/gL heterodimer facilitates the merger of the viral envelope with the host membrane, allowing the viral capsid to enter the cytoplasm [3][4]. Beyond entry, these glycoproteins play significant roles in immune evasion; for instance, gC binds to the host complement component C3b to inhibit immune-mediated viral clearance [5]. Because they are the primary targets for the host's neutralizing antibody response, they are the central focus of modern vaccine development (e.g., recombinant gD subunit vaccines) and monoclonal antibody therapies like UB-621 and HDIT101, which aim to block viral entry and spread [6][7]. Diagnostically, type-specific glycoproteins like gG-2 are utilized in serological assays to differentiate HSV-2 from HSV-1 infections [8].

Other names

HSV-2 surface proteinsHSV-2 gBHSV-2 gCHSV-2 gDHSV-2 gHHSV-2 gLHSV-2 gG-2Herpes simplex virus 2 viral envelope protein complex

Prevention of viral entry and infection by blocking the interaction between viral glycoproteins (primarily gD) and host cell receptors, or by inhibiting the conformational changes in gB and gH/gL required for membrane fusion and viral penetration.