Human cytomegalovirus envelope glycoprotein surface antigens (HCMV glycoproteins)

Human cytomegalovirus (HCMV) envelope glycoprotein surface antigens are a diverse group of proteins, including gB, gH, gL, gO, gM, gN, and the UL128-131A subunits, that are critical for viral infectivity [3, 11, 12]. These proteins facilitate the attachment of the virus to host cell receptors and mediate the fusion of the viral envelope with the host cell membrane [9, 14, 20]. Specifically, glycoprotein B (gB) serves as the essential fusion protein, while the trimeric (gH/gL/gO) and pentameric (gH/gL/UL128/UL130/UL131A) complexes determine the virus's ability to infect different cell types like fibroblasts and epithelial cells [1, 5, 11, 15]. In clinical disease, these antigens are the primary targets for neutralizing antibodies, making them central to the development of vaccines and passive immunotherapies [1, 3, 4]. HCMV infection is a leading cause of congenital birth defects and significant morbidity in transplant recipients, where viral entry into host tissues leads to systemic disease [3, 12]. Therapeutic strategies, such as the mRNA-1647 vaccine and monoclonal antibodies like RG7667, target these glycoproteins to block viral entry and prevent infection [4, 13, 19]. Despite their potential, the structural complexity and genetic polymorphism of certain glycoproteins present challenges for achieving universal and durable protection [3, 15].

Other names

Human cytomegalovirus surface antigensHCMV envelope glycoproteinsGlycoprotein B (gB)gH/gL complexPentameric complex (gH/gL/UL128/UL130/UL131A)Trimeric complex (gH/gL/gO)gM/gN complex

Neutralization of viral entry by blocking attachment to host receptors or inhibiting membrane fusion; induction of protective humoral and cellular immune responses.