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

Ji Sook Lee, Taisoon Yong

Research output: Contribution to journalArticle

17 Citations (Scopus)

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.

Original languageEnglish
Pages (from-to)339-343
Number of pages5
JournalParasitology Research
Volume93
Issue number5
DOIs
Publication statusPublished - 2004 Jan 1

Fingerprint

Clonorchis sinensis
fatty acid-binding proteins
Fatty Acid-Binding Proteins
Fasciola hepatica
Complementary DNA
Recombinant Proteins
recombinant proteins
Vaccines
Clonorchiasis
Paragonimiasis
Fascioliasis
biliary tract
vaccines
Schistosoma japonicum
Amino Acids
liver flukes
Trematoda
fascioliasis
amino acids
Schistosoma

All Science Journal Classification (ASJC) codes

  • Parasitology
  • veterinary(all)
  • Insect Science
  • Infectious Diseases

Cite this

@article{c4ee1ecf4cfe486fb988fdedd964165f,
title = "Expression and cross-species reactivity of fatty acid-binding protein of Clonorchis sinensis",
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.",
author = "Lee, {Ji Sook} and Taisoon Yong",
year = "2004",
month = "1",
day = "1",
doi = "10.1007/s00436-004-1139-z",
language = "English",
volume = "93",
pages = "339--343",
journal = "Parasitology Research",
issn = "0932-0113",
publisher = "Springer Verlag",
number = "5",

}

Expression and cross-species reactivity of fatty acid-binding protein of Clonorchis sinensis. / Lee, Ji Sook; Yong, Taisoon.

In: Parasitology Research, Vol. 93, No. 5, 01.01.2004, p. 339-343.

Research output: Contribution to journalArticle

TY - JOUR

T1 - Expression and cross-species reactivity of fatty acid-binding protein of Clonorchis sinensis

AU - Lee, Ji Sook

AU - Yong, Taisoon

PY - 2004/1/1

Y1 - 2004/1/1

N2 - 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.

AB - 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.

UR - http://www.scopus.com/inward/record.url?scp=4143113357&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=4143113357&partnerID=8YFLogxK

U2 - 10.1007/s00436-004-1139-z

DO - 10.1007/s00436-004-1139-z

M3 - Article

C2 - 15197581

AN - SCOPUS:4143113357

VL - 93

SP - 339

EP - 343

JO - Parasitology Research

JF - Parasitology Research

SN - 0932-0113

IS - 5

ER -