Source:http://linkedlifedata.com/resource/pubmed/id/15478796
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Predicate | Object |
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
2
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pubmed:dateCreated |
2004-10-13
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pubmed:databankReference | |
pubmed:abstractText |
In this study, we characterized a novel Babesia bovis cDNA clone obtained by immunoscreening the cDNA expression phage library with B. bovis-infected bovine serum. The genetic analyses showed that it contained an open reading frame of 993 bp, which was considered to encode B. bovis L-lactate dehydrogenase (BbLDH: E.C. 1.1.1.27) because of the strikingly high amino acid identities of its gene product to the LDHs of Plasmodium falciparum and Toxoplasma gondii. Immunological analyses with the anti-recombinant BbLDH mouse serum showed that 36 kDa of the native BbLDH was expressed not only in the cytoplasm of intra- and extraerythrocytic parasites but also along the membrane of infected erythrocytes. The kinetic properties of recombinant BbLDH proved a certain enzymatic activity of LDH, and the activity was significantly inhibited by the addition of gossypol, a competitive inhibitor of protozoan LDHs. Moreover, 100 microM of the gossypol irretrievably arrested the in vitro growth of B. bovis. The results demonstrated that BbLDH provides a suitable drug target for the design of novel babesial chemotherapeutics.
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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, Protozoan,
http://linkedlifedata.com/resource/pubmed/chemical/DNA, Complementary,
http://linkedlifedata.com/resource/pubmed/chemical/DNA, Protozoan,
http://linkedlifedata.com/resource/pubmed/chemical/Enzyme Inhibitors,
http://linkedlifedata.com/resource/pubmed/chemical/Gossypol,
http://linkedlifedata.com/resource/pubmed/chemical/L-Lactate Dehydrogenase
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pubmed:status |
MEDLINE
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pubmed:month |
Aug
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pubmed:issn |
0166-6851
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:volume |
136
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
165-72
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pubmed:dateRevised |
2006-11-15
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pubmed:meshHeading |
pubmed-meshheading:15478796-Amino Acid Sequence,
pubmed-meshheading:15478796-Animals,
pubmed-meshheading:15478796-Antibodies, Protozoan,
pubmed-meshheading:15478796-Babesia bovis,
pubmed-meshheading:15478796-Babesiosis,
pubmed-meshheading:15478796-Cattle,
pubmed-meshheading:15478796-Cattle Diseases,
pubmed-meshheading:15478796-Cloning, Molecular,
pubmed-meshheading:15478796-DNA, Complementary,
pubmed-meshheading:15478796-DNA, Protozoan,
pubmed-meshheading:15478796-Enzyme Inhibitors,
pubmed-meshheading:15478796-Female,
pubmed-meshheading:15478796-Genes, Protozoan,
pubmed-meshheading:15478796-Gossypol,
pubmed-meshheading:15478796-L-Lactate Dehydrogenase,
pubmed-meshheading:15478796-Mice,
pubmed-meshheading:15478796-Mice, Inbred BALB C,
pubmed-meshheading:15478796-Molecular Sequence Data
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pubmed:year |
2004
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pubmed:articleTitle |
Identification of Babesia bovis L-lactate dehydrogenase as a potential chemotherapeutical target against bovine babesiosis.
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pubmed:affiliation |
National Research Center for Protozoan Diseases, Obihiro University of Agriculture and Veterinary Medicine, Inada-cho, Obihiro, Hokkaido 080-8555, Japan.
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pubmed:publicationType |
Journal Article,
In Vitro,
Research Support, Non-U.S. Gov't
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