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The Tembusu virus envelope glycoprotein (E protein) is the primary structural component on the surface of the Tembusu virus (TMUV) virion, a member of the Flaviviridae family. It plays a critical role in the viral life cycle by mediating attachment to host cell receptors and facilitating the fusion of the viral envelope with the host endosomal membrane during entry [1]. Structurally, the E protein is organized into three distinct domains (DI, DII, and DIII), with DIII being the primary site for receptor binding and a major target for neutralizing antibodies [2]. TMUV primarily affects waterfowl, causing significant economic losses in the poultry industry due to severe egg drop syndrome and neurological symptoms [3]. As the most immunogenic protein of the virus, the E protein is the central focus for the development of diagnostic tools, subunit vaccines, and therapeutic monoclonal antibodies aimed at blocking viral infection [4]. Experimental strategies targeting this protein include the use of RNA interference and small molecule inhibitors designed to disrupt its conformational changes required for fusion [5].
Neutralization of viral entry by blocking receptor binding or inhibiting pH-dependent membrane fusion.
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