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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
2
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pubmed:dateCreated |
2011-4-19
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pubmed:abstractText |
We have utilized glycan microarray technology to determine the receptor binding properties of early isolates from the recent 2009 H1N1 human pandemic (pdmH1N1), and compared them to North American swine influenza isolates from the same year, as well as past seasonal H1N1 human isolates. We showed that the pdmH1N1 strains, as well as the swine influenza isolates examined, bound almost exclusively to glycans with ?2,6-linked sialic acid with little binding detected for ?2,3-linked species. This is highlighted by pair-wise comparisons between compounds with identical glycan backbones, differing only in the chemistry of their terminal linkages. The overall similarities in receptor binding profiles displayed by pdmH1N1 strains and swine isolates indicate that little or no adaptation appeared to be necessary in the binding component of HA for transmission from pig to human, and subsequent human to human spread.
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pubmed:grant |
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pubmed:language |
eng
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pubmed:journal |
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pubmed:citationSubset |
IM
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pubmed:chemical |
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pubmed:status |
MEDLINE
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pubmed:month |
May
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pubmed:issn |
1096-0341
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pubmed:author |
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pubmed:copyrightInfo |
Copyright © 2011 Elsevier Inc. All rights reserved.
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pubmed:issnType |
Electronic
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pubmed:day |
10
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pubmed:volume |
413
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
169-82
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pubmed:meshHeading |
pubmed-meshheading:21353280-Agglutination,
pubmed-meshheading:21353280-Animals,
pubmed-meshheading:21353280-Binding Sites,
pubmed-meshheading:21353280-Erythrocytes,
pubmed-meshheading:21353280-Hemagglutinins,
pubmed-meshheading:21353280-Humans,
pubmed-meshheading:21353280-Influenza, Human,
pubmed-meshheading:21353280-Influenza A Virus, H1N1 Subtype,
pubmed-meshheading:21353280-Microarray Analysis,
pubmed-meshheading:21353280-Models, Molecular,
pubmed-meshheading:21353280-Orthomyxoviridae Infections,
pubmed-meshheading:21353280-Pandemics,
pubmed-meshheading:21353280-Phylogeny,
pubmed-meshheading:21353280-Protein Binding,
pubmed-meshheading:21353280-Protein Conformation,
pubmed-meshheading:21353280-Receptors, Virus,
pubmed-meshheading:21353280-Seasons,
pubmed-meshheading:21353280-Swine,
pubmed-meshheading:21353280-Swine Diseases,
pubmed-meshheading:21353280-Virus Attachment
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pubmed:year |
2011
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pubmed:articleTitle |
Comparison of the receptor binding properties of contemporary swine isolates and early human pandemic H1N1 isolates (Novel 2009 H1N1).
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pubmed:affiliation |
Department of Microbiology and Immunology, Emory University School of Medicine, 1510 Clifton Rd, Atlanta, GA 30322, USA.
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pubmed:publicationType |
Journal Article,
Research Support, N.I.H., Extramural
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