Source:http://linkedlifedata.com/resource/pubmed/id/10081767
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Predicate | Object |
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
1
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pubmed:dateCreated |
1999-5-27
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pubmed:abstractText |
Monoclonal antibodies to the 28kDa glutathione S-transferase of Schistosoma bovis have been constructed in mice and used to characterize the epitope(s) potentially implied in the induction of anti-fecundity and anti-egg viability immune responses. Among the MoAbs produced three were particularly studied: Sb4-50 (IgG2a) and Sb4-56 (IgG1) which inhibited Sb28GST activity and Sb4-10 (IgG1) which did not. The use of overlapping peptides covering the entire amino acid sequence of Sb28GST, allowed us to define the linear epitopes recognized by these anti-Sb28GST MoAbs. Amino acid residues 202-211 were recognized by both MoAbs Sb4-50 and Sb4-56 and MoAb Sb4-10 recognized amino acid residues 58-67. Their capacity to inhibit GST activity suggested binding to the active site or to neighbouring regions, which include the C-terminal domain (a.a. 190-211) of the protein. When passively transferred into BALB/c mice MoAbs induced a significant reduction in egg hatching and an increase in immature eggs. Effects on worm burdens were, however, variable and no clear-cut association between the inhibition of enzyme activity and anti-fecundity or anti-viability activities was recorded. Our data indicate that beside the anti-fecundity and anti-viability immunity related to the impairment of GST activity, immune response to epitopes located in other regions of the molecule also contribute to the reduction of egg viability.
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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, Helminth,
http://linkedlifedata.com/resource/pubmed/chemical/Antibodies, Monoclonal,
http://linkedlifedata.com/resource/pubmed/chemical/Antigens, Helminth,
http://linkedlifedata.com/resource/pubmed/chemical/Epitopes, B-Lymphocyte,
http://linkedlifedata.com/resource/pubmed/chemical/Glutathione Transferase
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pubmed:status |
MEDLINE
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pubmed:month |
Jan
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pubmed:issn |
0141-9838
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:volume |
21
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
9-18
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pubmed:dateRevised |
2006-11-15
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pubmed:meshHeading |
pubmed-meshheading:10081767-Amino Acid Sequence,
pubmed-meshheading:10081767-Animals,
pubmed-meshheading:10081767-Antibodies, Helminth,
pubmed-meshheading:10081767-Antibodies, Monoclonal,
pubmed-meshheading:10081767-Antigens, Helminth,
pubmed-meshheading:10081767-Epitope Mapping,
pubmed-meshheading:10081767-Epitopes, B-Lymphocyte,
pubmed-meshheading:10081767-Glutathione Transferase,
pubmed-meshheading:10081767-Immunization, Passive,
pubmed-meshheading:10081767-Mice,
pubmed-meshheading:10081767-Mice, Inbred BALB C,
pubmed-meshheading:10081767-Molecular Sequence Data,
pubmed-meshheading:10081767-Ovum,
pubmed-meshheading:10081767-Schistosoma
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pubmed:year |
1999
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pubmed:articleTitle |
Definition and mapping of epitopes recognized by specific monoclonal antibodies to Schistosoma bovis 28 kDa glutathione S-transferase: relation with anti-egg viability immunity.
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pubmed:affiliation |
Centre d'Immunologie et de Biologie Parasitaire, Unité INSERM U-167, Institut Pasteur de Lille, France.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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