PubMed:10611486 JSONTXT

{"project":"IAV-Glycan_IAV_human_2","denotations":[{"id":"T1","span":{"begin":0,"end":12},"obj":"substitution"},{"id":"T2","span":{"begin":155,"end":167},"obj":"sialic acid"},{"id":"T3","span":{"begin":209,"end":218},"obj":"receptor"},{"id":"T4","span":{"begin":329,"end":341},"obj":"sialic acid"},{"id":"T5","span":{"begin":463,"end":465},"obj":"H3"},{"id":"T6","span":{"begin":582,"end":594},"obj":"sialic acid"},{"id":"T7","span":{"begin":606,"end":608},"obj":"H3"}],"text":"Substitution of amino acid residue in influenza A virus hemagglutinin affects recognition of sialyl-oligosaccharides containing N-glycolylneuraminic acid.\nSialic acids are essential components of cell surface receptors used by influenza viruses. To determine the molecular mechanisms of viral recognition of two major species of sialic acids, N-acetylneuraminic acid (Neu5Ac) and N-glycolylneuraminic acid (Neu5Gc), we tested the binding reactivity of nine human H3 influenza A viruses to sialylglycolipids containing type II sugar chain and different molecular species of terminal sialic acids. All human H3 viruses tested except A/Memphis/1/71 bound both Neu5Ac and Neu5Gc. Nucleotide sequence analysis suggests that amino acids at 143, 155, and 158 are linked to the viral recognition of Neu5Gc."}

{"project":"IAV-Glycan_IAV_H3_human","denotations":[{"id":"T1","span":{"begin":155,"end":167},"obj":"sialic acid"},{"id":"T2","span":{"begin":329,"end":341},"obj":"sialic acid"},{"id":"T3","span":{"begin":582,"end":594},"obj":"sialic acid"}],"text":"Substitution of amino acid residue in influenza A virus hemagglutinin affects recognition of sialyl-oligosaccharides containing N-glycolylneuraminic acid.\nSialic acids are essential components of cell surface receptors used by influenza viruses. To determine the molecular mechanisms of viral recognition of two major species of sialic acids, N-acetylneuraminic acid (Neu5Ac) and N-glycolylneuraminic acid (Neu5Gc), we tested the binding reactivity of nine human H3 influenza A viruses to sialylglycolipids containing type II sugar chain and different molecular species of terminal sialic acids. All human H3 viruses tested except A/Memphis/1/71 bound both Neu5Ac and Neu5Gc. Nucleotide sequence analysis suggests that amino acids at 143, 155, and 158 are linked to the viral recognition of Neu5Gc."}

{"project":"IAV-Glycan_IAV_human","denotations":[{"id":"T1","span":{"begin":155,"end":167},"obj":"sialic acid"},{"id":"T2","span":{"begin":329,"end":341},"obj":"sialic acid"},{"id":"T3","span":{"begin":582,"end":594},"obj":"sialic acid"}],"text":"Substitution of amino acid residue in influenza A virus hemagglutinin affects recognition of sialyl-oligosaccharides containing N-glycolylneuraminic acid.\nSialic acids are essential components of cell surface receptors used by influenza viruses. To determine the molecular mechanisms of viral recognition of two major species of sialic acids, N-acetylneuraminic acid (Neu5Ac) and N-glycolylneuraminic acid (Neu5Gc), we tested the binding reactivity of nine human H3 influenza A viruses to sialylglycolipids containing type II sugar chain and different molecular species of terminal sialic acids. All human H3 viruses tested except A/Memphis/1/71 bound both Neu5Ac and Neu5Gc. Nucleotide sequence analysis suggests that amino acids at 143, 155, and 158 are linked to the viral recognition of Neu5Gc."}

{"project":"IAV-Glycan_IAV_H3","denotations":[{"id":"T1","span":{"begin":155,"end":167},"obj":"sialic acid"},{"id":"T2","span":{"begin":329,"end":341},"obj":"sialic acid"},{"id":"T3","span":{"begin":582,"end":594},"obj":"sialic acid"}],"text":"Substitution of amino acid residue in influenza A virus hemagglutinin affects recognition of sialyl-oligosaccharides containing N-glycolylneuraminic acid.\nSialic acids are essential components of cell surface receptors used by influenza viruses. To determine the molecular mechanisms of viral recognition of two major species of sialic acids, N-acetylneuraminic acid (Neu5Ac) and N-glycolylneuraminic acid (Neu5Gc), we tested the binding reactivity of nine human H3 influenza A viruses to sialylglycolipids containing type II sugar chain and different molecular species of terminal sialic acids. All human H3 viruses tested except A/Memphis/1/71 bound both Neu5Ac and Neu5Gc. Nucleotide sequence analysis suggests that amino acids at 143, 155, and 158 are linked to the viral recognition of Neu5Gc."}