Human cytomegalovirus envelope glycoprotein (HCMV envelope glycoprotein)

Human cytomegalovirus envelope glycoproteins are integral membrane proteins found on the surface of HCMV virions. The major glycoproteins include glycoprotein B (gB), which is essential for membrane fusion and viral entry and functions as a class III viral fusogen; the glycoprotein H/L complex (gH/gL), which mediates receptor binding; and complexes such as gM/gN and gpUL132, which contribute to virion assembly and host cell membrane reorganization. Additionally, the HCMV envelope contains viral G protein-coupled receptors (vGPCRs: pUL33, pUL78, pUS27, pUS28), some of which bind host chemokines and modulate immune responses. These glycoproteins are targets for neutralizing antibodies, therapeutic monoclonal antibodies, and vaccine development. The envelope glycoproteins display structural and antigenic diversity, complicated by extensive glycosylation and genetic variation, which shape their immunogenic properties and affect both disease pathogenesis and therapeutic intervention.

Other names

HCMV glycoproteinHCMV gB (glycoprotein B)HCMV gH/gL complex (glycoprotein H/glycoprotein L)HCMV gM/gN complex (glycoprotein M/glycoprotein N)HCMV gpUL132Viral G protein-coupled receptors (vGPCRs): pUL33, pUL78, pUS27, pUS28

Neutralization of viral entry by blocking glycoprotein-mediated fusion or receptor interaction (e.g., monoclonal antibodies); Inhibition of antigenic domains recognized by the immune system