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Predicate | Object |
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
34
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pubmed:dateCreated |
1997-9-15
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pubmed:abstractText |
Echovirus 22 (EV22) is a picornavirus forming a distinct molecular cluster together with echovirus 23. EV22 has an Arg-Gly-Asp (RGD) peptide motif in its capsid protein VP1; similar motifs are known to mediate many cell-cell and microbe-host interactions. To identify peptide sequences that specifically bind to EV22 and potentially play a role in receptor recognition, we have used here peptide libraries displayed in filamentous phage. We isolated an EV22-binding motif CLRSG(R/F)GC. The synthetic CLRSGRGC peptide was able to inhibit EV22 infection. The infection was also inhibited by an RGD-containing peptide representing the C terminus of the EV22 capsid protein VP1 and CWDDGWLC (an RGD-binding peptide; Pasqualini, R., Koivunen, E., and Ruoslahti, E. (1995) J. Cell Biol. 130, 1189-1196). As the EV22-recognizing sequence LRSG is found in the integrin beta1 chain and the entire LRSGRG hexapeptide occurs in the matrix metalloproteinase 9 (MMP-9), we carried out blocking experiments with anti-integrin and anti-MMP-9 antibodies. EV22 infection could be blocked in cell cultures with anti-alphav, -beta1, and, to a lesser extent, with anti-MMP-9 antibodies. These results imply that EV22 recognizes preferentially alphavbeta1-integrin as a cellular receptor and MMP-9 may also play a role in the cell-surface interactions of the virus.
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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/Collagenases,
http://linkedlifedata.com/resource/pubmed/chemical/Integrins,
http://linkedlifedata.com/resource/pubmed/chemical/Matrix Metalloproteinase 9,
http://linkedlifedata.com/resource/pubmed/chemical/Oligopeptides,
http://linkedlifedata.com/resource/pubmed/chemical/Peptide Library,
http://linkedlifedata.com/resource/pubmed/chemical/Receptors, Virus,
http://linkedlifedata.com/resource/pubmed/chemical/arginyl-glycyl-aspartic acid
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pubmed:status |
MEDLINE
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pubmed:month |
Aug
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pubmed:issn |
0021-9258
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:day |
22
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pubmed:volume |
272
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
21176-80
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pubmed:dateRevised |
2006-11-15
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pubmed:meshHeading |
pubmed-meshheading:9261123-Amino Acid Sequence,
pubmed-meshheading:9261123-Capsid,
pubmed-meshheading:9261123-Collagenases,
pubmed-meshheading:9261123-Consensus Sequence,
pubmed-meshheading:9261123-Enterovirus,
pubmed-meshheading:9261123-Enterovirus B, Human,
pubmed-meshheading:9261123-Humans,
pubmed-meshheading:9261123-Immunologic Techniques,
pubmed-meshheading:9261123-Integrins,
pubmed-meshheading:9261123-Matrix Metalloproteinase 9,
pubmed-meshheading:9261123-Molecular Sequence Data,
pubmed-meshheading:9261123-Oligopeptides,
pubmed-meshheading:9261123-Peptide Library,
pubmed-meshheading:9261123-Receptors, Virus,
pubmed-meshheading:9261123-Sequence Alignment,
pubmed-meshheading:9261123-Sequence Homology, Amino Acid,
pubmed-meshheading:9261123-Tumor Cells, Cultured
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pubmed:year |
1997
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pubmed:articleTitle |
Cell-surface interactions of echovirus 22.
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pubmed:affiliation |
National Public Health Institute, Mannerheimintie 166, FIN-00300 Helsinki, Finland. timo.pulli@ktl.fi
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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