Human cytomegalovirus glycoprotein H complex (gH complex)

The human cytomegalovirus glycoprotein H complex is a critical multi-protein envelope complex composed of glycoprotein H (gH) paired with glycoprotein L (gL) and either glycoprotein O (gO) or a set of proteins (UL128, UL130, UL131A). The trimeric gH/gL/gO complex acts as an essential viral ligand for host cell receptors, especially platelet-derived growth factor receptor alpha (PDGFR-α), enabling viral entry into fibroblasts and other cell types. The pentameric gH/gL/UL128-131 complex expands viral tropism, allowing infection of epithelial and endothelial cells. Together, these complexes mediate virus-cell attachment, membrane fusion, and cell-type specificity of cytomegalovirus infection. Both are among the most potent neutralizing antibody targets in vaccine and therapeutic development. The gH complex’s functionality is essential for viral infectivity, playing a central role in cytomegalovirus pathogenesis and a focal point for current strategies in antiviral research and immunoprophylaxis.

Other names

gH/gL complexgH/gL/gO complex (Trimer complex)gH/gL/UL128-131 complex (Pentamer complex)CMV gH complexHCMV glycoprotein H complex

Neutralizing antibodies (naturally induced or therapeutic) can block binding of the complex to host receptors or interfere with its function in viral entry. Entry inhibitors may prevent interaction with cellular receptors such as PDGFR-α, and thus viral infection of host cells. Vaccine-induced immunity targets the conformational structure of these glycoproteins to elicit neutralizing antibody responses.