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Predicate | Object |
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
8
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pubmed:dateCreated |
1994-6-30
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pubmed:abstractText |
Jacalin is a multimeric plant lectin able to interact with the lymphocyte cell-surface molecule CD4, a known receptor for the human immunodeficiency virus type 1 (HIV-1). Moreover, jacalin is able to block HIV-1 infection of CD4+ lymphoblastoid cells. Here we studied whether jacalin prevents HIV-1 gp120-CD4 interactions. We found (i) that jacalin did not inhibit HIV-1 Lai-induced syncytium formation that requires gp120-CD4 interactions; (ii) that jacalin prevented neither rgp120 binding to cell-surface CD4 nor sCD4 binding to viral envelope proteins expressed at the surface of HIV-1-infected lymphoblastoid cells; (iii) that jacalin did not compete for binding to CD4 with anti-CD4 mAb specific for the CDR2- or CDR3-like regions of the D1 domain of CD4; (iv) that jacalin did not bind a recombinant soluble molecule containing the D1/D2 domains of CD4; and, (iv) that jacalin binding to CD4 is inhibited by sugars known to interact with the lectinic-site of jacalin. These data have implications for the understanding of the mechanism by which jacalin blocks HIV-1 infection of CD4+ 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/4-nitrophenylgalactoside,
http://linkedlifedata.com/resource/pubmed/chemical/Acetylgalactosamine,
http://linkedlifedata.com/resource/pubmed/chemical/Antigens, CD4,
http://linkedlifedata.com/resource/pubmed/chemical/Antiviral Agents,
http://linkedlifedata.com/resource/pubmed/chemical/HIV Envelope Protein gp120,
http://linkedlifedata.com/resource/pubmed/chemical/Lectins,
http://linkedlifedata.com/resource/pubmed/chemical/Nitrophenylgalactosides,
http://linkedlifedata.com/resource/pubmed/chemical/Plant Lectins,
http://linkedlifedata.com/resource/pubmed/chemical/jacalin
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pubmed:status |
MEDLINE
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pubmed:month |
Jun
|
pubmed:issn |
0161-5890
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pubmed:author | |
pubmed:issnType |
Print
|
pubmed:volume |
31
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
569-75
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pubmed:dateRevised |
2006-11-15
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pubmed:meshHeading |
pubmed-meshheading:8196669-Acetylgalactosamine,
pubmed-meshheading:8196669-Antigens, CD4,
pubmed-meshheading:8196669-Antiviral Agents,
pubmed-meshheading:8196669-Binding, Competitive,
pubmed-meshheading:8196669-Binding Sites,
pubmed-meshheading:8196669-Cell Line,
pubmed-meshheading:8196669-Cell Line, Transformed,
pubmed-meshheading:8196669-HIV Envelope Protein gp120,
pubmed-meshheading:8196669-HIV-1,
pubmed-meshheading:8196669-Humans,
pubmed-meshheading:8196669-Lectins,
pubmed-meshheading:8196669-Nitrophenylgalactosides,
pubmed-meshheading:8196669-Plant Lectins
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pubmed:year |
1994
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pubmed:articleTitle |
Jacalin, a lectin with anti-HIV-1 properties, and HIV-1 gp120 envelope protein interact with distinct regions of the CD4 molecule.
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pubmed:affiliation |
CRBM-UPR 9008 du CNRS, Institut de Biologie-Faculté de Médecine, Montpellier, France.
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pubmed:publicationType |
Journal Article,
Comparative Study,
Research Support, Non-U.S. Gov't
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