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The Human cytomegalovirus Pentameric glycoprotein complex (HCMV Pentamer) is a heteropentameric membrane-proximal protein complex composed of five subunits: glycoprotein H (gH), glycoprotein L (gL), UL128, UL130, and UL131A. It is essential for HCMV infection of epithelial, endothelial, and certain myeloid lineage cells by binding to host entry receptors, notably neuropilin-2 (NRP2). The Pentamer is a major target for potent virus-neutralizing antibodies and is central to vaccine and antibody therapeutic development. Disruption of the Pentamer or its interaction with cellular receptors can prevent HCMV cell entry, making it a validated antiviral target. It is distinct from the gH/gL/gO trimeric complex, which mediates entry into fibroblasts[2][3][4][6][9][8].
Blockade of viral attachment and entry (by neutralizing antibodies or vaccines), Inhibition of receptor binding (neuropilin-2, NRP2), Potential interference with assembly or function
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