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Epstein-Barr virus glycoprotein H (gH) is one of the essential envelope glycoproteins of the γ-herpesvirus EBV required for viral entry into host cells. Together with glycoprotein L (gL), it forms a heterodimeric complex that acts as a core part of the viral membrane fusion machinery, enabling penetration of the viral membrane into B cells and epithelial cells. The gH/gL complex is responsible for initiating membrane fusion by binding to cellular receptors (such as integrins and EphA2), and its structure features multiple domains including integrin binding motifs vital for epithelial cell entry. gH is a major target of neutralizing antibodies and is the focus of therapeutic and vaccine development, given its key role in EBV infection and associated malignant diseases, such as lymphomas and nasopharyngeal carcinoma. Its function and immunogenic properties make it a prominent therapeutic target as well as a marker for assessing EBV infection and immunity [1][4][5][6][9][7].
Inhibition of viral membrane fusion and entry, Antibody-mediated neutralization
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