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Molecular basis of the structure and function of H1 hemagglutinin of influenza virus.

Abstract

Influenza virus hemagglutinin (HA) contains antigenic sites recognized by the host immune system, cleavage sites cleaved by host proteases, receptor binding sites attaching to sialyl receptors on the target cell, and fusion peptides mediating membrane fusion. Change in an amino acid(s) in these sites may affect the potential of virus infection and spread within and between hosts. Influenza viruses with H1 HA infect birds, pigs and humans and have caused two of the four pandemics in the past 100 years: 1918 pandemic that killed 21-50 million people and 2009 pandemic that caused more than 18,000 deaths. Understanding the relationship between antigenic structure and immune specificity, the receptor binding specificity in virus transmission, how the cleavage site controls pathogenicity, and how the fusion peptide causes membrane fusion for the entry of influenza virus into the host cell should provide information to find more effective ways to prevent and control influenza.

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  • Authors

    Sriwilaijaroen N, Suzuki Y

    Institution

    Faculty of Medicine, Thammasat University, Pathumthani, Thailand.

    Source

    Proceedings of the Japan Academy. Series B, Physical and biological sciences 88:6 2012 pg 226-49

    MeSH

    Amino Acid Sequence
    Animals
    Antigens, Viral
    Hemagglutinin Glycoproteins, Influenza Virus
    Humans
    Molecular Sequence Data
    Orthomyxoviridae
    Receptors, Virus
    Structure-Activity Relationship
    Virus Internalization

    Pub Type(s)

    Journal Article
    Review

    Language

    eng

    PubMed ID

    22728439