tetano
Editor, Senior Moderator
J Am Chem Soc. 2010 Sep 30. [Epub ahead of print]
Differential Receptor Binding Affinities of Influenza Hemagglutinins on Glycan Arrays.
Liao HY, Hsu CH, Wang SC, Liang CH, Yen HY, Su CY, Chen CH, Jan JT, Ren CT, Chen CH, Cheng TJ, Wu CY, Wong CH.
Genomics Research Center, Academia Sinica, 128 Academia Road, Section 2, Nankang, Taipei 115, Taiwan, Institute of Biochemistry and Molecular Biology, National Yang-Ming University, Taipei 112, Taiwan, Chemical Biology and Molecular Biophysics, Taiwan International Graduate Program, Academia Sinica, Taiwan, Institute of Bioinformatics and Structural Biology, National Tsing-Hua University, Hsin-Chu 300, Taiwan and Institute of Biochemical Sciences, National Taiwan University, Taipei, Taiwan.
Abstract
A library of 27 sialosides, including seventeen 2,3-linked and ten 2,6-linked glycans, has been prepared to construct a glycan array and used to profile the binding specificity of different influenza hemagglutinins (HA) subtypes, especially from the 2009 swine-originated H1N1 and seasonal influenza viruses. It was found that the HAs from the 2009 H1N1 and the seasonal Brisbane strain share similar binding profiles yet different binding affinities toward various α2,6 sialosides. Analysis of the binding profiles of different HA subtypes indicate that a minimum set of 5 oligosaccharides can be used to differentiate influenza H1, H3, H5, H7, and H9 subtypes. In addition, the glycan array was used to profile the binding pattern of different influenza viruses. It was found that most binding patterns of viruses and HA proteins are similar and that glycosylation at Asn27 is essential for receptor binding.
PMID: 20882975 [PubMed - as supplied by publisher]
http://www.ncbi.nlm.nih.gov/pubmed/20882975
Differential Receptor Binding Affinities of Influenza Hemagglutinins on Glycan Arrays.
Liao HY, Hsu CH, Wang SC, Liang CH, Yen HY, Su CY, Chen CH, Jan JT, Ren CT, Chen CH, Cheng TJ, Wu CY, Wong CH.
Genomics Research Center, Academia Sinica, 128 Academia Road, Section 2, Nankang, Taipei 115, Taiwan, Institute of Biochemistry and Molecular Biology, National Yang-Ming University, Taipei 112, Taiwan, Chemical Biology and Molecular Biophysics, Taiwan International Graduate Program, Academia Sinica, Taiwan, Institute of Bioinformatics and Structural Biology, National Tsing-Hua University, Hsin-Chu 300, Taiwan and Institute of Biochemical Sciences, National Taiwan University, Taipei, Taiwan.
Abstract
A library of 27 sialosides, including seventeen 2,3-linked and ten 2,6-linked glycans, has been prepared to construct a glycan array and used to profile the binding specificity of different influenza hemagglutinins (HA) subtypes, especially from the 2009 swine-originated H1N1 and seasonal influenza viruses. It was found that the HAs from the 2009 H1N1 and the seasonal Brisbane strain share similar binding profiles yet different binding affinities toward various α2,6 sialosides. Analysis of the binding profiles of different HA subtypes indicate that a minimum set of 5 oligosaccharides can be used to differentiate influenza H1, H3, H5, H7, and H9 subtypes. In addition, the glycan array was used to profile the binding pattern of different influenza viruses. It was found that most binding patterns of viruses and HA proteins are similar and that glycosylation at Asn27 is essential for receptor binding.
PMID: 20882975 [PubMed - as supplied by publisher]
http://www.ncbi.nlm.nih.gov/pubmed/20882975