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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 |
2004-8-4
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pubmed:databankReference |
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pubmed:abstractText |
Clonorchis sinensis is a Chinese liver fluke that chronically resides in the biliary tract. The fatty acid-binding protein (FABP) is known to play an important role in the intracellular transport of long-chain fatty acids that are obtained by the fluke from the host. Although FABP has stimulated considerable interest as a vaccine target candidate, the nature of FABP from C. sinensis (CsFABP) remains unclear. In this paper, we describe the cloning and expression of recombinant FABP and immune cross-reaction by Western blot analysis. Sequence analysis revealed that the CsFABP cDNA contained a single open reading frame (ORF) coding for 134 amino acids with an estimated molecular mass of a 15.2 kDa. The DNA sequence of CsFABP cDNA showed significant homology to schistosome cytosolic FABPs, with a 49% amino acid sequence identity and 89% similarity to Schistosoma japonicum. This DNA also showed a high sequence similarity at the amino acid level to S. mansoni (Sm14; 83%) and Fasciola hepatica (80%). The CsFABP cDNA was cloned into expression vector pET28a, expressed in Escherichia coli and the recombinant protein purified by affinity chromatography. The recombinant CsFABP was cross-reacted with sera obtained from patients with fascioliasis and paragonimiasis. These results suggest that CsFABP may be useful as a vaccine for clonorchiasis.
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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 |
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pubmed:status |
MEDLINE
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pubmed:month |
Aug
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pubmed:issn |
0932-0113
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:volume |
93
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
339-43
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pubmed:dateRevised |
2005-11-17
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pubmed:meshHeading |
pubmed-meshheading:15197581-Amino Acid Sequence,
pubmed-meshheading:15197581-Animals,
pubmed-meshheading:15197581-Antibodies, Helminth,
pubmed-meshheading:15197581-Base Sequence,
pubmed-meshheading:15197581-Blotting, Western,
pubmed-meshheading:15197581-Carrier Proteins,
pubmed-meshheading:15197581-Cloning, Molecular,
pubmed-meshheading:15197581-Clonorchis sinensis,
pubmed-meshheading:15197581-Cross Reactions,
pubmed-meshheading:15197581-DNA, Complementary,
pubmed-meshheading:15197581-DNA, Helminth,
pubmed-meshheading:15197581-Escherichia coli,
pubmed-meshheading:15197581-Fasciola hepatica,
pubmed-meshheading:15197581-Fascioliasis,
pubmed-meshheading:15197581-Fatty Acid-Binding Proteins,
pubmed-meshheading:15197581-Helminth Proteins,
pubmed-meshheading:15197581-Humans,
pubmed-meshheading:15197581-Molecular Sequence Data,
pubmed-meshheading:15197581-Molecular Weight,
pubmed-meshheading:15197581-Open Reading Frames,
pubmed-meshheading:15197581-Paragonimiasis,
pubmed-meshheading:15197581-Recombinant Proteins,
pubmed-meshheading:15197581-Schistosoma japonicum,
pubmed-meshheading:15197581-Schistosoma mansoni,
pubmed-meshheading:15197581-Sequence Alignment,
pubmed-meshheading:15197581-Sequence Analysis, DNA,
pubmed-meshheading:15197581-Sequence Homology, Amino Acid
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pubmed:year |
2004
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pubmed:articleTitle |
Expression and cross-species reactivity of fatty acid-binding protein of Clonorchis sinensis.
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pubmed:affiliation |
Department of Parasitology and Institute of Tropical Medicine, BK 21 Project for Medical Science, Yonsei University College of Medicine, 134 Shinchondong, Seodaemungu, 120-752 Seoul, Korea.
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pubmed:publicationType |
Journal Article
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