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rdf:type |
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lifeskim:mentions |
umls-concept:C0017082,
umls-concept:C0034848,
umls-concept:C0036638,
umls-concept:C0524637,
umls-concept:C0678594,
umls-concept:C1167622,
umls-concept:C1441414,
umls-concept:C1527178,
umls-concept:C1553874,
umls-concept:C1578820,
umls-concept:C1705938
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pubmed:issue |
4
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pubmed:dateCreated |
1980-7-12
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pubmed:abstractText |
The binding of Sendai virus to polystyrene petri dishes to which various gangliosides of defined structures had been adsorbed was determined. The ganglioside-bound virus was visualized either by a water vapor condensation method or by a hemadsorption method. By either assay, specific virus binding of high affinity was demonstrated to the gangliosides GT1a, GQ1b, and GPlc which have a common end sequence in the oligosaccharide moiety: NeuAc alpha 2 leads to 8NeuAc alpha 2 leads to 3Gal beta 1 leads to 3GalNAc leads to. Binding also occurred to the GD1a and GT1b gangliosides, which have the same end carbohydrate sequence except for the terminal N-acetylneuraminic acid, but the affinity was only 1-9% of that of the gangliosides with a terminal disialosyl linkage. It is proposed that the structure NeuAc alpha 2 leads to 8NeuAc alpha 2 leads to 3Gal beta 1 leads to 3GalNAc is the recognition-specific structure of the receptor for Sendai virus that is present on cell membrane gangliosides and possibly also glycoproteins. Binding tests to plastic-adsorbed glycolipids are suggested to be a useful tool for identification of the receptor recognition structure.
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pubmed:commentsCorrections |
http://linkedlifedata.com/resource/pubmed/commentcorrection/6246515-176657,
http://linkedlifedata.com/resource/pubmed/commentcorrection/6246515-181911,
http://linkedlifedata.com/resource/pubmed/commentcorrection/6246515-4125267,
http://linkedlifedata.com/resource/pubmed/commentcorrection/6246515-422571,
http://linkedlifedata.com/resource/pubmed/commentcorrection/6246515-4348510,
http://linkedlifedata.com/resource/pubmed/commentcorrection/6246515-4364586,
http://linkedlifedata.com/resource/pubmed/commentcorrection/6246515-438198,
http://linkedlifedata.com/resource/pubmed/commentcorrection/6246515-4707310,
http://linkedlifedata.com/resource/pubmed/commentcorrection/6246515-621516,
http://linkedlifedata.com/resource/pubmed/commentcorrection/6246515-71329,
http://linkedlifedata.com/resource/pubmed/commentcorrection/6246515-7353026,
http://linkedlifedata.com/resource/pubmed/commentcorrection/6246515-7354254,
http://linkedlifedata.com/resource/pubmed/commentcorrection/6246515-793997
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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 |
Apr
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pubmed:issn |
0027-8424
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:volume |
77
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
1947-50
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pubmed:dateRevised |
2009-11-18
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pubmed:meshHeading |
pubmed-meshheading:6246515-Adsorption,
pubmed-meshheading:6246515-Binding Sites,
pubmed-meshheading:6246515-Gangliosides,
pubmed-meshheading:6246515-Models, Biological,
pubmed-meshheading:6246515-Parainfluenza Virus 1, Human,
pubmed-meshheading:6246515-Plastics,
pubmed-meshheading:6246515-Receptors, Virus,
pubmed-meshheading:6246515-Structure-Activity Relationship
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pubmed:year |
1980
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pubmed:articleTitle |
Sendai virus receptor: proposed recognition structure based on binding to plastic-adsorbed gangliosides.
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pubmed:publicationType |
Journal Article
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