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Beschreibung

Herpes Simplex Virus envelope Glycoprotein D (UniProt: Q69091) is also known as gD. The envelope of herpes simplex virus (HSV) is complex and contains at least 10 virus-encoded glycoproteins, some of which mediate virus entry into the host cell. HSV virus enters the cell by first fusing its envelope with a membrane of the host cell. Five viral envelope glycoproteins are reported to be involved in this entry process. Binding of glycoprotein D of HSV to a cell surface receptor is required to trigger membrane fusion during entry into host cells. Glycoproteins C and B promote attachment by interacting with cell surface proteoglycans and then glycoprotein D binds to the herpes virus entry mediator (HVEM) receptor that initiates a process that ultimately leads to glycoprotein B-mediated membrane fusion. Glycoprotein D is synthesized with a signal peptide (aa 1-25) that is subsequently cleaved off. It is a homodimeric protein that contains two zinc-binding sites (aa 64 and 264). The ectodomain region of glycoprotein D contains three sites for the addition of N-linked oligosaccharides (N-CHO) and six cysteine residues arranged into three disulfide bonds. During virion morphogenesis, glycoprotein D probably accumulates in the endosomes and trans-Golgi where secondary envelopment occurs. (Ref.: Whitbeck JC et al. (1997). J. Virol. 71(8), p. 6083 6093, Nicola, AV et al. (1998). J Virol. 72(5): 3595-3601, Giovine, PD et al. (2011). PLos Pathog. 7(9), e1002277).