Human cytomegalovirus envelope glycoprotein B and other surface glycoproteins (HCMV gB and surface glycoproteins)

Human cytomegalovirus (HCMV) envelope glycoproteins, specifically glycoprotein B (gB) and the pentameric complex (gH/gL/UL128/UL130/UL131A), are essential mediators of viral entry into host cells. Glycoprotein B acts as a class III viral fusion protein, facilitating the fusion of the viral envelope with the host cell membrane (UniProt: P06473). The pentameric complex is crucial for the infection of epithelial, endothelial, and myeloid cells, thereby determining the virus's broad tissue tropism (PubMed: 26134242). These surface proteins are the primary targets for neutralizing antibodies produced by the host immune system during natural infection. Consequently, they are the focus of therapeutic interventions, including monoclonal antibodies like RG7667 and vaccine candidates such as mRNA-1647, which aim to prevent viral entry (ClinicalTrials.gov: NCT05085301). Targeting these glycoproteins is a key strategy for preventing congenital CMV transmission and managing severe infections in transplant recipients and other immunocompromised individuals (PubMed: 31534005).

Other names

HCMV gBHCMV gH/gL complexHCMV pentameric complexUL55UL75UL115UL128/130/131A complexEnvelope glycoprotein BEnvelope glycoprotein HEnvelope glycoprotein L

Neutralization of viral entry by binding to specific epitopes on gB or the pentameric complex, thereby blocking attachment to host receptors or inhibiting membrane fusion between the viral envelope and the host cell membrane (PubMed: 26134242, PubMed: 30108114).