Source:http://linkedlifedata.com/resource/pubmed/id/11017790
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| Predicate | Object |
|---|---|
| rdf:type | |
| lifeskim:mentions | |
| pubmed:issue |
1
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| pubmed:dateCreated |
2000-10-13
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| pubmed:abstractText |
Various lectins were tested for blocking rotavirus infection of MA104 cells and it was observed that galactose-specific lectins were the most inhibitory. Of these Ricinus agglutinin was able to inhibit infection (by human and animal strains) at concentrations as low as 10(-9) M. In addition, in a virus overlay protein blot assay Ricinus agglutinin competed with simian rotavirus SA11 for binding to solubilized MA104 proteins. Amino acid sequence comparisons revealed similarity between the ricin toxin B subunit (which contains two separate carbohydrate-binding motifs: single binding domains (SBD) 1 and 2) and rotavirus spike protein VP4. A filamentous phage display system was used to independently express the two binding domains and while SBD1 inhibited infection of MA104 cells by CRW8, NCDV, and to a lesser extent Wa, SBD2 blocked only CRW8 and NCDV infection. Furthermore inhibition of CRW8 infection was a direct result of phage inhibiting virus attachment to cells. When amino acid 248 within SBD2 was mutated from the ricin toxin to the Ricinus agglutinin sequence this phage clone showed reduced binding to galactose and was no longer able to inhibit virus infection. Thus, rotavirus recognizes galactose as an important component of the receptor on MA104 cells.
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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/Capsid Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Cell Extracts,
http://linkedlifedata.com/resource/pubmed/chemical/Galactose,
http://linkedlifedata.com/resource/pubmed/chemical/Peptide Fragments,
http://linkedlifedata.com/resource/pubmed/chemical/Peptide Library,
http://linkedlifedata.com/resource/pubmed/chemical/Receptors, Virus,
http://linkedlifedata.com/resource/pubmed/chemical/Ricin,
http://linkedlifedata.com/resource/pubmed/chemical/VP4 protein, Rotavirus
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| pubmed:status |
MEDLINE
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| pubmed:month |
Sep
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| pubmed:issn |
0042-6822
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| pubmed:author | |
| pubmed:copyrightInfo |
Copyright 2000 Academic Press.
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| pubmed:issnType |
Print
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| pubmed:day |
15
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| pubmed:volume |
275
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| pubmed:owner |
NLM
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| pubmed:authorsComplete |
Y
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| pubmed:pagination |
89-97
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| pubmed:dateRevised |
2004-11-17
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| pubmed:meshHeading |
pubmed-meshheading:11017790-Amino Acid Sequence,
pubmed-meshheading:11017790-Binding Sites,
pubmed-meshheading:11017790-Capsid,
pubmed-meshheading:11017790-Capsid Proteins,
pubmed-meshheading:11017790-Cell Extracts,
pubmed-meshheading:11017790-Cell Line,
pubmed-meshheading:11017790-Dose-Response Relationship, Drug,
pubmed-meshheading:11017790-Galactose,
pubmed-meshheading:11017790-Humans,
pubmed-meshheading:11017790-Immunoenzyme Techniques,
pubmed-meshheading:11017790-Peptide Fragments,
pubmed-meshheading:11017790-Peptide Library,
pubmed-meshheading:11017790-Protein Binding,
pubmed-meshheading:11017790-Protein Structure, Tertiary,
pubmed-meshheading:11017790-Receptors, Virus,
pubmed-meshheading:11017790-Ricin,
pubmed-meshheading:11017790-Rotavirus,
pubmed-meshheading:11017790-Solubility,
pubmed-meshheading:11017790-Substrate Specificity
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| pubmed:year |
2000
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| pubmed:articleTitle |
Rotavirus infection of MA104 cells is inhibited by Ricinus lectin and separately expressed single binding domains.
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| pubmed:affiliation |
Department of Microbiology and Immunology, University of Melbourne, Parkville, Victoria, 3052, Australia.
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| pubmed:publicationType |
Journal Article
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