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Glycoprotein H of human cytomegalovirus is a type I transmembrane viral envelope protein encoded by UL75. It forms heterodimers with glycoprotein L (gL) and can combine with additional subunits (such as gO or UL128-131 family proteins), resulting in complexes that mediate virus entry into host cells[2][5][6][7]. The gH/gL complex functions by binding specific cellular receptors, thereby regulating the tropism of the virus and triggering membrane fusion by activating glycoprotein B (gB)[5][6][7]. These functions are critical for the initial infection of epithelial, endothelial, and other cell types, as well as cell-to-cell viral spread. gH, particularly as part of the gH/gL/UL128-131 complex, is a major antigenic target for neutralizing antibodies and candidate vaccines aiming to block CMV transmission and pathogenesis[6][7].
Inhibition of viral entry by blocking fusion and receptor interaction Neutralization of the virus by preventing binding to epithelial/endothelial cell receptors (antibody/vaccine responses)
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