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Expression and cross-species reactivity of fatty acid-binding protein of Clonorchis sinensis

Authors
 Ji-Sook Lee Tai-Soon Yong 
Citation
 PARASITOLOGY RESEARCH, Vol.93(5) : 339-343, 2004 
Journal Title
 PARASITOLOGY RESEARCH 
ISSN
 0932-0113 
Issue Date
2004
MeSH
Amino Acid Sequence ; Animals ; Antibodies, Helminth/blood ; Base Sequence ; Blotting, Western ; Carrier Proteins/chemistry ; Carrier Proteins/genetics* ; Carrier Proteins/immunology* ; Carrier Proteins/metabolism ; Cloning, Molecular ; Clonorchis sinensis/genetics* ; Clonorchis sinensis/metabolism* ; Cross Reactions ; DNA, Complementary ; DNA, Helminth/chemistry ; Escherichia coli/genetics ; Escherichia coli/metabolism ; Fasciola hepatica/genetics ; Fascioliasis/immunology ; Fascioliasis/parasitology ; Fatty Acid-Binding Proteins ; Helminth Proteins/chemistry ; Helminth Proteins/genetics* ; Helminth Proteins/immunology ; Helminth Proteins/metabolism ; Humans ; Molecular Sequence Data ; Molecular Weight ; Open Reading Frames ; Paragonimiasis/immunology ; Paragonimiasis/parasitology ; Recombinant Proteins/chemistry ; Recombinant Proteins/immunology ; Recombinant Proteins/metabolism ; Schistosoma japonicum/genetics ; Schistosoma mansoni/genetics ; Sequence Alignment ; Sequence Analysis, DNA ; Sequence Homology, Amino Acid
Keywords
Adult Worm ; Schistosoma Mansoni ; Schistosoma Japonicum ; Fascioliasis ; Clonorchiasis
Abstract
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.
Full Text
http://link.springer.com/article/10.1007%2Fs00436-004-1139-z
DOI
10.1007/s00436-004-1139-z
Appears in Collections:
1. College of Medicine (의과대학) > Dept. of Environmental Medical Biology (환경의생물학교실) > 1. Journal Papers
Yonsei Authors
Yong, Tai Soon(용태순) ORCID logo https://orcid.org/0000-0002-3445-0769
URI
https://ir.ymlib.yonsei.ac.kr/handle/22282913/111265
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