Linked Life Data

3997874

Source:http://linkedlifedata.com/resource/pubmed/id/3997874

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
12
pubmed:dateCreated
1985-7-25
pubmed:abstractText
Human and animal influenza A isolates of the H3 serotype preferentially bind SA alpha 2,6Gal or SA alpha 2,3Gal linkages (where SA represents sialic acid), respectively, on cell-surface sialyloligosaccharides. Previously, we have demonstrated selection of SA alpha 2,3Gal-specific receptor variants of several human viruses which differed from the parent viruses by a single amino acid at residue 226 of the hemagglutinin which is located in the receptor binding pocket (Rogers, G. N., Paulson, J.C., Daniels, R.S., Skehel, J.J., Wilson, I.A., and Wiley, D.C. (1983) Nature 304, 76-78). In this report, the selection in the reverse direction was accomplished starting with a SA alpha 2,3Gal-specific avian virus, A/duck/Ukraine/1/63 (H3N7), yielding SA alpha 2,6Gal-specific variants that exhibit the receptor binding properties characteristic of the human isolates. Selection was again mediated at residue 226 of the hemagglutinin, in this case changing from Gln in the parent virus to Leu in the variants. Although the SA alpha 2,6Gal-specific avian virus variants were stable to passage in MDCK cells, they exhibited dramatic reversion to the SA alpha 2,3Gal-specific phenotype of the parent virus during a single passage in chicken embryos. This was in contrast to the SA alpha 2,6Gal-specific human virus isolates which were stable to passage in both hosts. The reversion of the avian virus variants in eggs provides compelling evidence for host-mediated selection of influenza virus receptor variants.
pubmed:grant
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Jun
pubmed:issn
0021-9258
pubmed:author
pubmed:issnType
Print
pubmed:day
25
pubmed:volume
260
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
7362-7
pubmed:dateRevised
2008-11-21
pubmed:meshHeading
pubmed-meshheading:3997874-Animals, pubmed-meshheading:3997874-Carbohydrate Sequence, pubmed-meshheading:3997874-Cell Line, pubmed-meshheading:3997874-Chick Embryo, pubmed-meshheading:3997874-Dogs, pubmed-meshheading:3997874-Ducks, pubmed-meshheading:3997874-Erythrocyte Membrane, pubmed-meshheading:3997874-Galactose, pubmed-meshheading:3997874-Genetic Variation, pubmed-meshheading:3997874-Hemagglutinin Glycoproteins, Influenza Virus, pubmed-meshheading:3997874-Hemagglutinins, Viral, pubmed-meshheading:3997874-Humans, pubmed-meshheading:3997874-Influenza A virus, pubmed-meshheading:3997874-Kidney, pubmed-meshheading:3997874-N-Acetylneuraminic Acid, pubmed-meshheading:3997874-Oligosaccharides, pubmed-meshheading:3997874-Receptors, Cell Surface, pubmed-meshheading:3997874-Receptors, Immunologic, pubmed-meshheading:3997874-Serotyping, pubmed-meshheading:3997874-Sialic Acids, pubmed-meshheading:3997874-Species Specificity
pubmed:year
1985
pubmed:articleTitle
Host-mediated selection of influenza virus receptor variants. Sialic acid-alpha 2,6Gal-specific clones of A/duck/Ukraine/1/63 revert to sialic acid-alpha 2,3Gal-specific wild type in ovo.
pubmed:publicationType
Journal Article, Research Support, U.S. Gov't, P.H.S., Research Support, U.S. Gov't, Non-P.H.S., Research Support, Non-U.S. Gov't