These tools will no longer be maintained as of December 31, 2024. Archived website can be found here. PubMed4Hh GitHub repository can be found here. Contact NLM Customer Service if you have questions.
Pubmed for Handhelds
PUBMED FOR HANDHELDS
Search MEDLINE/PubMed
Title: Expression and cross-species reactivity of fatty acid-binding protein of Clonorchis sinensis. Author: Lee JS, Yong TS. Journal: Parasitol Res; 2004 Aug; 93(5):339-43. PubMed ID: 15197581. 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.[Abstract] [Full Text] [Related] [New Search]