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Human cytomegalovirus glycoprotein pentameric complex is a multimeric viral envelope assembly consisting of five subunits: gH, gL, UL128, UL130, and UL131A. This complex mediates entry of HCMV into epithelial and endothelial cells by binding to specific host receptors including neuropilin-2 (NRP2), thrombomodulin (THBD), and olfactory receptor OR14I1. It is the principal target of potently neutralizing antibodies and a central focus of vaccine design. The Pentamer’s presence dictates viral cell tropism—absent or mutated complexes restrict infection to fibroblasts. Structural and functional studies show that Pentamer induces membrane fusion upon receptor engagement and is essential for the broad pathogenicity of HCMV. Antibody therapeutics and vaccine candidates are being developed to block Pentamer-mediated entry, representing a promising strategy for prevention and treatment of HCMV-associated disease.
Inhibition of viral entry by blocking Pentamer–host receptor interaction; Neutralization of viral fusion/entry process by antibody binding
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