Differential receptor binding affinities of influenza hemagglutinins on glycan arrays.
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.
Liao
Hsin-Yu
HY
Genomics Research Center, Academia Sinica, 128 Academia Road, Section 2, Nankang, Taipei 115, Taiwan.
Hsu
Che-Hsiung
CH
Wang
Shih-Chi
SC
Liang
Chi-Hui
CH
Yen
Hsin-Yung
HY
Su
Ching-Yao
CY
Chen
Chien-Hung
CH
Jan
Jia-Tsrong
JT
Ren
Chien-Tai
CT
Chen
Chung-Hsuan
CH
Cheng
Ting-Jen R
TJ
Wu
Chung-Yi
CY
Wong
Chi-Huey
CH
D002240:Carbohydrate Sequence; D002460:Cell Line; D006031:Glycosylation; D019267:Hemagglutinin Glycoproteins, Influenza Virus / Q000378:metabolism*; D006801:Humans; D053118:Influenza A Virus, H1N1 Subtype / Q000378:metabolism*; D011134:Polysaccharides / Q000378:metabolism*; D011485:Protein Binding; D011991:Receptors, Virus / Q000378:metabolism*
D019267:Hemagglutinin Glycoproteins, Influenza Virus; D011134:Polysaccharides; D011991:Receptors, Virus