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The HCMV Pentameric complex is a critical glycoprotein assembly on the surface of the human cytomegalovirus (HCMV) envelope. It comprises five subunits: glycoprotein H (gH), glycoprotein L (gL), and three viral proteins: UL128, UL130, and UL131A. This complex is essential for efficient infection of epithelial, endothelial, and myeloid lineage cells. The Pentameric complex binds host cell surface receptors—most notably neuropilin-2 (NRP2) and thrombomodulin (THBD)—to mediate viral attachment and entry. These interactions drive HCMV’s broad cellular tropism and are considered central for transmission and pathogenicity. Monoclonal antibodies targeting conformational epitopes on the Pentamer can effectively neutralize viral infectivity in susceptible cells, highlighting this complex as an important candidate for vaccine and therapeutic antibody development[1][4].
Mechanisms involve neutralization by monoclonal antibodies preventing receptor binding and subsequent cell entry
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