Human cytomegalovirus envelope glycoprotein complex (HCMV glycoproteins)

Human cytomegalovirus (HCMV) virion surface glycoproteins and envelope antigens are a group of proteins embedded in the viral lipid bilayer that are essential for the virus's ability to infect host cells. The primary components include glycoprotein B (gB), which acts as the core fusion machinery, and the gH/gL complexes, which exist as either a trimer (gH/gL/gO) or a pentamer (gH/gL/UL128/UL130/UL131A). These complexes determine the virus's cell tropism, allowing it to enter fibroblasts, epithelial cells, and endothelial cells by interacting with specific host receptors like PDGFR-alpha or Neuropilin-2 (Citations: UniProt P06473, PubMed: 26194953). As the primary targets for neutralizing antibodies, these glycoproteins are the focus of vaccine development (e.g., mRNA-1647) and monoclonal antibody therapies designed to prevent or treat HCMV infection (Citations: Moderna, PubMed: 31534003). In clinical settings, targeting these antigens is particularly important for preventing congenital CMV transmission and managing infections in transplant recipients. Therapeutic strategies typically involve blocking the initial attachment or the subsequent fusion process required for viral entry into the host cytoplasm.

Other names

Human cytomegalovirus virion surface glycoproteinsHCMV envelope antigensCMV surface proteinsGlycoprotein B (gB)Glycoprotein H (gH)Glycoprotein L (gL)Pentameric complex (gH/gL/UL128/UL130/UL131A)Trimeric complex (gH/gL/gO)

Neutralization of viral entry by blocking attachment to host receptors or inhibiting the membrane fusion process required for viral delivery into the host cytoplasm.