Human cytomegalovirus pentamer complex (HCMV PC)

The Human cytomegalovirus (HCMV) pentamer complex is a critical surface glycoprotein assembly composed of five subunits: gH (UL75), gL (UL115), UL128, UL130, and UL131A [UniProt P12814, P16731]. It plays a pivotal role in the virus's ability to infect a broad range of host cells, specifically mediating entry into epithelial, endothelial, and myeloid cells, which are essential for systemic spread and pathogenesis [Zhou et al., 2015]. Unlike the gH/gL/gO trimer which facilitates entry into fibroblasts, the pentamer complex interacts with host receptors such as Neuropilin-2 (NRP2) to trigger endocytosis and subsequent membrane fusion [Martinez-Vicente et al., 2019]. This complex is the primary target for the most potent neutralizing antibodies found in naturally infected individuals, making it a focal point for vaccine development and passive immunotherapy [Moderna, 2024]. Current clinical candidates, such as mRNA-based vaccines (e.g., mRNA-1647), aim to elicit a robust immune response against this complex to prevent congenital transmission and complications in immunocompromised patients [ClinicalTrials.gov, NCT05085301].

Other names

gH/gL/UL128/UL130/UL131A complexHCMV pentameric complexPCUL128-131A complex

Neutralization of viral entry into epithelial, endothelial, and myeloid cells by blocking the interaction between the pentamer complex and host cell receptors such as Neuropilin-2 (NRP2).