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Cytomegalovirus envelope glycoprotein B (gB) is a critical surface protein of the Human Cytomegalovirus (HCMV) and serves as the primary mediator of viral entry into host cells [UniProt: P06473]. Encoded by the UL55 gene, gB is a class III viral fusion protein that undergoes significant conformational changes to facilitate the fusion of the viral envelope with the host cell plasma membrane or endosomal membrane [PubMed: 25674382]. Beyond its role in fusion, gB is involved in initial attachment to host receptors such as heparan sulfate proteoglycans and interacts with signaling molecules like EGFR and PDGFR-alpha [PubMed: 21900257]. Because it is highly immunogenic and essential for infectivity, gB is a major target for neutralizing antibodies and has been the primary focus of CMV vaccine development for decades [PubMed: 19339720]. Therapeutic strategies targeting gB include monoclonal antibodies like Tevirumab and various subunit vaccine formulations, which aim to prevent primary infection or reduce viral transmission in transplant recipients and during pregnancy [PubMed: 8133330].
Neutralization of viral entry by binding to specific antigenic domains (AD-1 to AD-5) on the gB protein, thereby blocking the conformational changes required for membrane fusion [PubMed: 25674382].
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