Source:http://linkedlifedata.com/resource/pubmed/id/10544117
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
2
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pubmed:dateCreated |
1999-11-18
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pubmed:abstractText |
The infection of epithelial cells by some animal rotavirus strains requires the presence of sialic acid (SA) on the cell surface. Recently, we isolated rhesus rotavirus variants, named nar, whose infectivity, like that of human rotaviruses, is not dependent on SA. In this work, we have determined the binding properties of these SA-dependent and -independent rotavirus strains to MA104 cells. The half-time of attachment of the SA-dependent porcine rotavirus YM and reassortant virus DS1xRRV was found to be about 10 times longer in neuraminidase-treated cells than in untreated cells. On the other hand, human rotaviruses Wa and DS1, and the variant nar3, bound to cells two to three times more rapidly in the absence of SA. To investigate whether the SA-independent cellular structure recognized by the variant and human rotaviruses was the same, we used an infection assay designed to detect competition for cell surface molecules at both attachment and post-attachment steps. In this assay, human rotavirus Wa efficiently competed the infectivity of YM in untreated cells and that of the variant nar3 in untreated, as well as neuraminidase-treated, cells. This competition was nonreciprocal, since YM and nar3 did not compete, but rather increased three- to fivefold the infectivity of Wa. In contrast, a two-direction competition between the variant nar3 and DS1xRRV was found. Similar results were obtained when psoralen-inactivated viruses were used as competitors, indicating that the competition observed was during the early stages of infection. Altogether, these results suggest the existence of multiple interactions between rotaviruses and the cell surface and revealed the existence of common steps during the entry of human and animal rotavirus strains.
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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/Antibodies, Monoclonal,
http://linkedlifedata.com/resource/pubmed/chemical/Ficusin,
http://linkedlifedata.com/resource/pubmed/chemical/N-Acetylneuraminic Acid,
http://linkedlifedata.com/resource/pubmed/chemical/Neuraminidase,
http://linkedlifedata.com/resource/pubmed/chemical/Receptors, Virus
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pubmed:status |
MEDLINE
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pubmed:month |
Oct
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pubmed:issn |
0042-6822
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pubmed:author | |
pubmed:copyrightInfo |
Copyright 1999 Academic Press.
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pubmed:issnType |
Print
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pubmed:day |
25
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pubmed:volume |
263
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
450-9
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pubmed:dateRevised |
2008-11-21
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pubmed:meshHeading |
pubmed-meshheading:10544117-Adsorption,
pubmed-meshheading:10544117-Animals,
pubmed-meshheading:10544117-Antibodies, Monoclonal,
pubmed-meshheading:10544117-Binding, Competitive,
pubmed-meshheading:10544117-Cell Line,
pubmed-meshheading:10544117-Ficusin,
pubmed-meshheading:10544117-Genetic Variation,
pubmed-meshheading:10544117-Humans,
pubmed-meshheading:10544117-Kinetics,
pubmed-meshheading:10544117-Macaca mulatta,
pubmed-meshheading:10544117-N-Acetylneuraminic Acid,
pubmed-meshheading:10544117-Neuraminidase,
pubmed-meshheading:10544117-Reassortant Viruses,
pubmed-meshheading:10544117-Receptors, Virus,
pubmed-meshheading:10544117-Rotavirus,
pubmed-meshheading:10544117-Swine,
pubmed-meshheading:10544117-Virus Replication
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pubmed:year |
1999
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pubmed:articleTitle |
Entry of rotaviruses is a multistep process.
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pubmed:affiliation |
Departamento de Genética y Fisiología Molecular, Instituto de Biotecnología, Universidad Nacional Autónoma de México, Cuernavaca, Morelos, 62250, Mexico.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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