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Hemagglutinin (HA), neuraminidase (NA), and matrix protein 1 (M1) are principal proteins of the Influenza A virus particle. HA is a surface glycoprotein mediating viral attachment to host cell sialic acid and membrane fusion. NA is another surface glycoprotein that cleaves sialic acid residues, thereby facilitating viral release from infected cells. M1 is the most abundant structural protein, forming the underlying matrix layer that shapes the virion and regulates assembly and budding. Each is essential for viral replication, immune recognition, and pathogenicity, representing key targets for antiviral therapy and vaccine development.
Neutralizing antibodies block Hemagglutinin's viral attachment and membrane fusion. Neuraminidase inhibitors competitively block Neuraminidase's active site, preventing sialic acid cleavage and viral release. No approved drugs directly target Matrix protein 1; Matrix protein 2 (M2) is targeted by amantadine and rimantadine, which inhibit viral uncoating, but M1 itself is not.
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