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H7N9 influenza virus hemagglutinin (HA) is a critical surface glycoprotein that mediates the entry of the H7N9 avian influenza virus into host cells [4, 5]. It functions as a homotrimeric class I fusion protein, responsible for both binding to host cell sialic acid receptors and facilitating the fusion of the viral envelope with the endosomal membrane under acidic conditions [2, 5]. The H7N9 subtype is of significant public health concern due to its high pathogenicity in humans and its potential to adapt for human-to-human transmission [9, 15]. HA is the primary target for neutralizing antibodies and the main component of influenza vaccines [12, 14]. Therapeutic strategies targeting HA include the development of broadly neutralizing antibodies that bind to the conserved stem region and small molecules like tert-butyl hydroquinone (TBHQ) that stabilize the neutral pH conformation to prevent membrane fusion [7, 8].
Inhibition of viral entry by blocking receptor binding or preventing the pH-dependent conformational change required for membrane fusion [6, 7].
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