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The Sendai virus fusion (F) protein at the hemagglutinin-neuraminidase (HN) interface is a critical structural site for the entry of the Sendai virus (SeV), a member of the Paramyxoviridae family, into host cells. The F protein is a class I viral fusion protein that mediates the merging of the viral envelope with the host cell membrane, a process that is triggered by the binding of the HN protein to sialic acid receptors on the cell surface. The physical interaction between the HN and F proteins at this specific interface is essential for transmitting the triggering signal that induces the F protein to undergo a massive irreversible conformational change from a metastable pre-fusion state to a stable post-fusion state. Because this interaction is a prerequisite for viral infectivity, the HN-F interface represents a high-value target for the development of antiviral therapeutics. Small molecules or peptides designed to bind at this interface can effectively block the triggering mechanism, thereby preventing viral entry and subsequent respiratory infection. Understanding the precise molecular architecture of this interface is vital for designing broad-spectrum inhibitors against related human pathogens, such as human parainfluenza viruses.
Inhibition of the conformational transition of the fusion protein from a pre-fusion to a post-fusion state by blocking the essential interaction with the hemagglutinin-neuraminidase protein.
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