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Predicate | Object |
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rdf:type | |
lifeskim:mentions |
umls-concept:C0029341,
umls-concept:C0029348,
umls-concept:C0031437,
umls-concept:C0067736,
umls-concept:C0086418,
umls-concept:C0205214,
umls-concept:C0237876,
umls-concept:C0370215,
umls-concept:C1167395,
umls-concept:C1167622,
umls-concept:C1510827,
umls-concept:C1883254,
umls-concept:C2076600,
umls-concept:C2348235
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pubmed:issue |
2
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pubmed:dateCreated |
1997-7-15
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pubmed:abstractText |
Synthetic sialylglycoconjugates bearing 3'-sialyllactose, 6'-sialyllactose, or 6'-sialyl(N-acetyllactosamine) moieties attached to the polyacrylic acid carrier (P-3-SL, P-6-SL, and P-6-SLN, respectively) were prepared and tested for their ability to bind to influenza virus isolates from different hosts in a competitive solid phase assay. The virus panel included egg-grown avian and porcine strains, as well as human viruses isolated and propagated solely in mammalian (MDCK) cells and their egg-adapted variants. A clear correlation was observed between the pattern of virus binding of two glycopolymers, P-3-SL and P-6-SLN, and the host species from which the virus was derived. Avian isolates displayed a high binding affinity for P-3-SL and a two to three orders of magnitude lower affinity for P-6-SLN. By contrast, all non-egg-adapted human A and B viruses bound P-6-SLN strongly but did not bind P-3-SL. Unlike the "authentic" human strains, their egg-adapted counterparts acquired an ability to bind P-3-SL, indicative of a shift in the receptor-binding phenotype toward the recognition of Neu5Ac2-3Gal-terminated sugar sequences. Among the porcine viruses and human isolates with porcine hemagglutinin, few displayed an avian-like binding phenotype, while others differed from both avian and human strains by a reduced ability to discriminate between P-3-SL and P-6-SLN. Our data show that sialylglycopolymers may become a useful tool in studies on molecular mechanisms of interspecies transfer, tissue specificity, and other structure-function relationships of the influenza virus hemagglutinin.
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pubmed:language |
eng
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pubmed:journal | |
pubmed:citationSubset |
IM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Amino Sugars,
http://linkedlifedata.com/resource/pubmed/chemical/Glycoconjugates,
http://linkedlifedata.com/resource/pubmed/chemical/Lactose,
http://linkedlifedata.com/resource/pubmed/chemical/N-acetylneuraminoyllactose,
http://linkedlifedata.com/resource/pubmed/chemical/Receptors, Virus,
http://linkedlifedata.com/resource/pubmed/chemical/Sialic Acids,
http://linkedlifedata.com/resource/pubmed/chemical/sialyl-N-acetyllactosamine
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pubmed:status |
MEDLINE
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pubmed:month |
Jun
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pubmed:issn |
0042-6822
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:day |
9
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pubmed:volume |
232
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
345-50
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pubmed:dateRevised |
2006-11-15
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pubmed:meshHeading |
pubmed-meshheading:9191848-Amino Sugars,
pubmed-meshheading:9191848-Animals,
pubmed-meshheading:9191848-Cell Line,
pubmed-meshheading:9191848-Chick Embryo,
pubmed-meshheading:9191848-Dogs,
pubmed-meshheading:9191848-Glycoconjugates,
pubmed-meshheading:9191848-Humans,
pubmed-meshheading:9191848-Influenza A virus,
pubmed-meshheading:9191848-Influenza B virus,
pubmed-meshheading:9191848-Lactose,
pubmed-meshheading:9191848-Phenotype,
pubmed-meshheading:9191848-Receptors, Virus,
pubmed-meshheading:9191848-Sialic Acids
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pubmed:year |
1997
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pubmed:articleTitle |
Specification of receptor-binding phenotypes of influenza virus isolates from different hosts using synthetic sialylglycopolymers: non-egg-adapted human H1 and H3 influenza A and influenza B viruses share a common high binding affinity for 6'-sialyl(N-acetyllactosamine).
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pubmed:affiliation |
M. P. Chumakov Institute of Poliomyelitis and Viral Encephalitides, Moscow, Russia.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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