Molecular basis of the structure and function of H1 hemagglutinin of influenza virus.
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.
Faculty of Medicine, Thammasat University, Pathumthani, Thailand.
Nongluk
N
Sriwilaijaroen
Yasuo
Y
Suzuki
D000595:Amino Acid Sequence; D000818:Animals; D000956:Antigens, Viral / Q000276:immunology; D019267:Hemagglutinin Glycoproteins, Influenza Virus / Q000737:chemistry* / Q000276:immunology*; D006801:Humans; D008969:Molecular Sequence Data; D009975:Orthomyxoviridae / Q000276:immunology*; D011991:Receptors, Virus / Q000378:metabolism; D013329:Structure-Activity Relationship; D053586:Virus Internalization
D000956:Antigens, Viral; D019267:Hemagglutinin Glycoproteins, Influenza Virus; D011991:Receptors, Virus