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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
5
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pubmed:dateCreated |
1993-5-24
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pubmed:abstractText |
Entamoeba histolytica adheres to human colonic mucins and colonic epithelial cells via a galactose-binding adhesin. The adhesin is a heterodimeric glycoprotein composed of 170- and 35-kDa subunits. Fragments of the hgl1 gene encoding the 170-kDa subunit were expressed as recombinant fusion proteins in Escherichia coli and reacted with anti-adhesin monoclonal antibodies (MAbs) or pooled human immune sera. The MAbs tested recognize seven distinct epitopes on the 170-kDa subunit and have distinct effects on the adherence and complement-inhibitory activities of the adhesin. All seven MAbs reacted with a fusion protein containing the cysteine-rich domain of the protein. Pooled human immune sera reacted with the same cysteine-rich domain as the MAbs and also with a construct containing the first 596 amino acids. Reactivity of three MAbs with the surface of intact trophozoites confirmed that the cysteine-rich domain was located extracellularly. The location of individual epitopes was fine mapped by constructing carboxy-terminal deletions in the cysteine-rich region of the fusion protein. The locations of adherence-enhancing and -inhibiting epitopes were partially distinguished, and the epitopes where complement-inhibitory MAbs bound were demonstrated to be near the adhesin's area of sequence identity with the human complement inhibitor CD59.
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pubmed:grant |
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pubmed:commentsCorrections |
http://linkedlifedata.com/resource/pubmed/commentcorrection/7682994-1372977,
http://linkedlifedata.com/resource/pubmed/commentcorrection/7682994-1381719,
http://linkedlifedata.com/resource/pubmed/commentcorrection/7682994-1452647,
http://linkedlifedata.com/resource/pubmed/commentcorrection/7682994-1460420,
http://linkedlifedata.com/resource/pubmed/commentcorrection/7682994-15463485,
http://linkedlifedata.com/resource/pubmed/commentcorrection/7682994-1563804,
http://linkedlifedata.com/resource/pubmed/commentcorrection/7682994-1576284,
http://linkedlifedata.com/resource/pubmed/commentcorrection/7682994-1692809,
http://linkedlifedata.com/resource/pubmed/commentcorrection/7682994-1937828,
http://linkedlifedata.com/resource/pubmed/commentcorrection/7682994-1987067,
http://linkedlifedata.com/resource/pubmed/commentcorrection/7682994-2000392,
http://linkedlifedata.com/resource/pubmed/commentcorrection/7682994-2014248,
http://linkedlifedata.com/resource/pubmed/commentcorrection/7682994-2388003,
http://linkedlifedata.com/resource/pubmed/commentcorrection/7682994-2536731,
http://linkedlifedata.com/resource/pubmed/commentcorrection/7682994-2538054,
http://linkedlifedata.com/resource/pubmed/commentcorrection/7682994-2580026,
http://linkedlifedata.com/resource/pubmed/commentcorrection/7682994-2580787,
http://linkedlifedata.com/resource/pubmed/commentcorrection/7682994-2869086,
http://linkedlifedata.com/resource/pubmed/commentcorrection/7682994-2871619,
http://linkedlifedata.com/resource/pubmed/commentcorrection/7682994-2888730,
http://linkedlifedata.com/resource/pubmed/commentcorrection/7682994-2890654,
http://linkedlifedata.com/resource/pubmed/commentcorrection/7682994-2890655,
http://linkedlifedata.com/resource/pubmed/commentcorrection/7682994-3047011,
http://linkedlifedata.com/resource/pubmed/commentcorrection/7682994-5432063,
http://linkedlifedata.com/resource/pubmed/commentcorrection/7682994-6271810
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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 |
http://linkedlifedata.com/resource/pubmed/chemical/Antibodies, Monoclonal,
http://linkedlifedata.com/resource/pubmed/chemical/Antibodies, Protozoan,
http://linkedlifedata.com/resource/pubmed/chemical/Antigens, Protozoan,
http://linkedlifedata.com/resource/pubmed/chemical/Antigens, Surface,
http://linkedlifedata.com/resource/pubmed/chemical/Cysteine,
http://linkedlifedata.com/resource/pubmed/chemical/Endopeptidase K,
http://linkedlifedata.com/resource/pubmed/chemical/Epitopes,
http://linkedlifedata.com/resource/pubmed/chemical/Galectins,
http://linkedlifedata.com/resource/pubmed/chemical/Hemagglutinins,
http://linkedlifedata.com/resource/pubmed/chemical/Membrane Glycoproteins,
http://linkedlifedata.com/resource/pubmed/chemical/Oligodeoxyribonucleotides,
http://linkedlifedata.com/resource/pubmed/chemical/Periodic Acid,
http://linkedlifedata.com/resource/pubmed/chemical/Recombinant Fusion Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Serine Endopeptidases
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pubmed:status |
MEDLINE
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pubmed:month |
May
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pubmed:issn |
0019-9567
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:volume |
61
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
1772-8
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pubmed:dateRevised |
2009-11-18
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pubmed:meshHeading |
pubmed-meshheading:7682994-Animals,
pubmed-meshheading:7682994-Antibodies, Monoclonal,
pubmed-meshheading:7682994-Antibodies, Protozoan,
pubmed-meshheading:7682994-Antigens, Protozoan,
pubmed-meshheading:7682994-Antigens, Surface,
pubmed-meshheading:7682994-Base Sequence,
pubmed-meshheading:7682994-Cysteine,
pubmed-meshheading:7682994-DNA Mutational Analysis,
pubmed-meshheading:7682994-Endopeptidase K,
pubmed-meshheading:7682994-Entamoeba histolytica,
pubmed-meshheading:7682994-Epitopes,
pubmed-meshheading:7682994-Extracellular Space,
pubmed-meshheading:7682994-Galectins,
pubmed-meshheading:7682994-Hemagglutinins,
pubmed-meshheading:7682994-Humans,
pubmed-meshheading:7682994-Membrane Glycoproteins,
pubmed-meshheading:7682994-Molecular Sequence Data,
pubmed-meshheading:7682994-Oligodeoxyribonucleotides,
pubmed-meshheading:7682994-Periodic Acid,
pubmed-meshheading:7682994-Recombinant Fusion Proteins,
pubmed-meshheading:7682994-Sequence Deletion,
pubmed-meshheading:7682994-Serine Endopeptidases
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pubmed:year |
1993
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pubmed:articleTitle |
Neutralizing monoclonal antibody epitopes of the Entamoeba histolytica galactose adhesin map to the cysteine-rich extracellular domain of the 170-kilodalton subunit.
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pubmed:affiliation |
Department of Medicine, University of Virginia, Charlottesville 22908.
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pubmed:publicationType |
Journal Article,
In Vitro,
Research Support, U.S. Gov't, P.H.S.,
Research Support, Non-U.S. Gov't
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