Giuseppe
Emeritus
Virology. 2009 Jul 21. [Epub ahead of print]
The hemagglutinin structure of an avian H1N1 influenza A virus.
Lin T, Wang G, Li A, Zhang Q, Wu C, Zhang R, Cai Q, Song W, Yuen KY. School of Life Sciences, Xiamen University, Xiamen, China; State Key Laboratory for Emerging Infectious Diseases, Department of Microbiology and the Research Center of Infection and Immunology, The University of Hong Kong, Pokfulam, Hong Kong SAR, PR China.
The interaction between hemagglutinin (HA) and receptors is a kernel in the study of evolution and host adaptation of H1N1 influenza A viruses. The notion that the avian HA is associated with preferential specificity for receptors with Siaalpha2,3Gal glycosidic linkage over those with Siaalpha2,6Gal linkage is not all consistent with the available data on H1N1 viruses. By x-ray crystallography, the HA structure of an avian H1N1 influenza A virus, as well as its complexes with the receptor analogs, was determined. The structures revealed no preferential binding of avian receptor analogs over that of the human analog, suggesting that the HA/receptor binding might not be as stringent as is commonly believed in determining the host receptor preference for some subtypes of influenza viruses, such as the H1N1 viruses. The structure also showed difference in glycosylation despite the preservation of related sequences, which may partly contribute to the difference between structures of human and avian origin.
PMID: 19628241 [PubMed - as supplied by publisher]
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34: Virus Res. 2009 Jul 14. [Epub ahead of print]
Molecular and phylogenetic analysis and vaccine strain match of human influenza a(h3n2) viruses isolated in northern greece between 2004 and 2008.
Melidou A, Exindari M, Gioula G, Chatzidimitriou D, Pierroutsakos Y, Diza-Mataftsi E. National Influenza Centre for Northern Greece, B Laboratory of Microbiology, School of Medicine, Aristotle University of Thessaloniki, Thessaloniki, Greece.
PMID: 19615420 [PubMed - as supplied by publisher]
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The hemagglutinin structure of an avian H1N1 influenza A virus.
Lin T, Wang G, Li A, Zhang Q, Wu C, Zhang R, Cai Q, Song W, Yuen KY. School of Life Sciences, Xiamen University, Xiamen, China; State Key Laboratory for Emerging Infectious Diseases, Department of Microbiology and the Research Center of Infection and Immunology, The University of Hong Kong, Pokfulam, Hong Kong SAR, PR China.
The interaction between hemagglutinin (HA) and receptors is a kernel in the study of evolution and host adaptation of H1N1 influenza A viruses. The notion that the avian HA is associated with preferential specificity for receptors with Siaalpha2,3Gal glycosidic linkage over those with Siaalpha2,6Gal linkage is not all consistent with the available data on H1N1 viruses. By x-ray crystallography, the HA structure of an avian H1N1 influenza A virus, as well as its complexes with the receptor analogs, was determined. The structures revealed no preferential binding of avian receptor analogs over that of the human analog, suggesting that the HA/receptor binding might not be as stringent as is commonly believed in determining the host receptor preference for some subtypes of influenza viruses, such as the H1N1 viruses. The structure also showed difference in glycosylation despite the preservation of related sequences, which may partly contribute to the difference between structures of human and avian origin.
PMID: 19628241 [PubMed - as supplied by publisher]
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34: Virus Res. 2009 Jul 14. [Epub ahead of print]
Molecular and phylogenetic analysis and vaccine strain match of human influenza a(h3n2) viruses isolated in northern greece between 2004 and 2008.
Melidou A, Exindari M, Gioula G, Chatzidimitriou D, Pierroutsakos Y, Diza-Mataftsi E. National Influenza Centre for Northern Greece, B Laboratory of Microbiology, School of Medicine, Aristotle University of Thessaloniki, Thessaloniki, Greece.
PMID: 19615420 [PubMed - as supplied by publisher]
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