Giuseppe
Emeritus
J Virol.. [Epub ahead of print]
Structure, receptor binding and antigenicity of influenza virus hemagglutinins from the 1957 H2N2 pandemic.
Xu R, McBride R, Paulson JC, Basler CF, Wilson IA. - Dept. of Molecular Biology, Dept. of Chemical Physiology, Skaggs Institute for Chemical Biology, The Scripps Research Institute, 10550 North Torrey Pines Road, La Jolla, CA 92037, USA; Dept. of Microbiology, Mount Sinai School of Medicine, New York, NY 10029, USA.
The hemagglutinin (HA) envelope protein of influenza viruses mediates essential viral functions including receptor binding and membrane fusion and is the major viral antigen for antibody neutralization. The 1957 H2N2 subtype (Asian flu) was one of the three great influenza pandemics of the last century and caused one million deaths globally from 1957 to 1968. Three crystal structures of 1957 H2 HAs have been determined at 1.60-1.75 A resolutions to investigate the structural basis for their antigenicity and evolution from avian to human binding specificity that contributed to its introduction into the human population. These structures, which represent the highest recorded resolutions yet recorded for a complete ectodomain of a glycosylated viral surface antigen, along with glycan microarray binding analysis, suggest that a hydrophobicity switch at residue 226 and elongation of receptor-binding site were both critical for avian H2 HA to acquire human receptor specificity. H2 influenza viruses continue to circulate in birds and pigs, and, therefore, remain a substantial threat for transmission to humans. The H2 HA structure also reveals a highly conserved epitope that could be harnessed in design of a broader and more universal influenza A virus vaccine.
PMID: 20007271 [PubMed - as supplied by publisher]
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Structure, receptor binding and antigenicity of influenza virus hemagglutinins from the 1957 H2N2 pandemic.
Xu R, McBride R, Paulson JC, Basler CF, Wilson IA. - Dept. of Molecular Biology, Dept. of Chemical Physiology, Skaggs Institute for Chemical Biology, The Scripps Research Institute, 10550 North Torrey Pines Road, La Jolla, CA 92037, USA; Dept. of Microbiology, Mount Sinai School of Medicine, New York, NY 10029, USA.
The hemagglutinin (HA) envelope protein of influenza viruses mediates essential viral functions including receptor binding and membrane fusion and is the major viral antigen for antibody neutralization. The 1957 H2N2 subtype (Asian flu) was one of the three great influenza pandemics of the last century and caused one million deaths globally from 1957 to 1968. Three crystal structures of 1957 H2 HAs have been determined at 1.60-1.75 A resolutions to investigate the structural basis for their antigenicity and evolution from avian to human binding specificity that contributed to its introduction into the human population. These structures, which represent the highest recorded resolutions yet recorded for a complete ectodomain of a glycosylated viral surface antigen, along with glycan microarray binding analysis, suggest that a hydrophobicity switch at residue 226 and elongation of receptor-binding site were both critical for avian H2 HA to acquire human receptor specificity. H2 influenza viruses continue to circulate in birds and pigs, and, therefore, remain a substantial threat for transmission to humans. The H2 HA structure also reveals a highly conserved epitope that could be harnessed in design of a broader and more universal influenza A virus vaccine.
PMID: 20007271 [PubMed - as supplied by publisher]
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