Herpes simplex virus type 2 surface glycoprotein

Herpes simplex virus type 2 surface glycoproteins are a group of membrane-anchored proteins incorporated into the viral envelope and are required for the virus to attach, fuse with, and enter host cells. Major glycoproteins include gB, gC, gD, gE, gG, gH, gI, gK, gL, gM, and gN, each with specific roles: for example, glycoprotein B (gB) and glycoprotein D (gD) mediate initial binding and membrane fusion, while glycoprotein G (gG) is important for virus-cell interactions and is utilized as a serological marker for HSV-2 infections[1][2][3][4][5][9]. Glycoproteins mediate attachment to cellular receptors like heparan sulfate proteoglycans, nectins, and HVEM, and are often targeted by antiviral therapeutics either directly or via inhibition of their interaction with host cell receptors[3][4][8]. Some, such as gG, have specific mucin-like features and are involved in immune evasion[2]. Drugs targeting these glycoproteins—especially those inhibiting viral attachment or fusion—can block infection at early stages, making these glycoproteins important therapeutic targets[2][6][8]. Antibodies against glycoprotein G (gG-2) are especially valuable as biomarkers to differentiate HSV-2 from HSV-1 infection[9].

Other names

HSV-2 glycoprotein (gB, gC, gD, gE, gG, gH, gI, gK, gL, gM, gN)

Block attachment to cell surface glycosaminoglycans by mimicking heparan sulfate (e.g., PI-88, heparin, SB105, SB105_A10); Inhibit fusion by interfering with glycoprotein-mediated membrane merging.