Glycoprotein H (human cytomegalovirus) (gH (HCMV))

Glycoprotein H (gH) is a conserved envelope protein encoded by the UL75 gene of human cytomegalovirus (HCMV). On the viral surface, gH forms two major oligomeric complexes: the trimer (gH/gL/gO) and the pentamer (gH/gL/UL128-131A). The "CMV trimer" specifically refers to the complex of gH/gL/gO, while the "pentamer" is a complex of gH/gL with the viral proteins UL128, UL130, and UL131A[2][6][7]. The trimer mediates entry into fibroblasts, primarily by interacting with the platelet-derived growth factor receptor alpha (PDGFRα), while the pentamer is required for efficient entry into epithelial and endothelial cells[2][6][7]. These complexes act by triggering membrane fusion through activation of the viral fusogen glycoprotein B (gB), and are major targets for neutralizing antibodies, making gH a critical antiviral target for both vaccine and biologic drug development[2][8]. The structure of gH in these complexes determines cell tropism and the efficiency of viral infection[2][6]. Both naturally occurring and engineered antibodies can neutralize HCMV by binding to gH-associated complexes, and vaccines under development often include gH as a key antigenic component[8]. Glycoprotein H itself is not a receptor, enzyme, or traditional drug target class, but functions as an essential component of viral entry machinery, making it a therapeutic target for vaccines and monoclonal antibodies[2][7][8].

Other names

gHUL75 glycoproteinHCMV gH

Neutralizing antibodies block gH/gL trimer/pentamer interaction with cellular receptors, preventing viral entry[8]. Experimental inhibitors or antibodies disrupt the formation or function of the gH/gL complexes, blocking fusion/entry[2].