Fasciola hepatica: Molecular cloning, nucleotide sequence, and expression of a gene encoding a polypeptide homologous to a Schistosoma mansoni fatty acid-binding protein

José Rodríguez-Pérez, JoséR Rodrǵuez-Medina, Mariano Garcia-Blanco, George V. Hillyer

Research output: Contribution to journalArticle

93 Citations (Scopus)

Abstract

Immunization of mice with an antigenic polypeptide from Fasciola hepatica adult worms and having an apparent molecular mass of 12,000 Da (Fh12) has been shown to reduce the worm burden from challenge infection with Schistosoma mansoni by more than 50%. Moreover, mice infected with S. mansoni develop antibodies to Fh12 after 5-6 weeks of infection, indicating that this Fasciola-derived antigen is a cross-reactive, cross-protective protein. A λgt11 F. hepatica cDNA library was constructed from poly(A)+ RNA extracted from adult worms. A cDNA encoding a cross-reactive polypeptide (Fh15) was cloned by screening the F. hepatica λgt11 library with a monospecific, polyclonal rabbit antiserum against pure, native Fh12. The cDNA was sequenced and the predicted amino acid sequence revealed an open reading frame encoding a 132-amino-acid protein with a predicted molecular weight of 14,700 Da. This protein has significant homology to a 14-kDa S. mansoni fatty acid-binding protein. Comparison of the protective-inducing activity of recombinant Fh15 with that of purified Fh12 against schistosomes and Fasciola is warranted.

Original languageEnglish (US)
Pages (from-to)400-407
Number of pages8
JournalExperimental Parasitology
Volume74
Issue number4
DOIs
StatePublished - 1992
Externally publishedYes

Fingerprint

Fasciola hepatica
Fatty Acid-Binding Proteins
Schistosoma mansoni
Molecular Cloning
Fasciola
Gene Expression
Peptides
Complementary DNA
Schistosomiasis mansoni
Proteins
Gene Library
Open Reading Frames
Libraries
Immune Sera
Amino Acid Sequence
Immunization
Molecular Weight
Rabbits
Antigens
Amino Acids

Keywords

  • cDNA clones
  • Fasciola hepatica
  • Fatty acid-binding protein
  • Schistosoma mansoni
  • Trematodes

ASJC Scopus subject areas

  • Immunology
  • Parasitology
  • Infectious Diseases

Cite this

Fasciola hepatica : Molecular cloning, nucleotide sequence, and expression of a gene encoding a polypeptide homologous to a Schistosoma mansoni fatty acid-binding protein. / Rodríguez-Pérez, José; Rodrǵuez-Medina, JoséR; Garcia-Blanco, Mariano; Hillyer, George V.

In: Experimental Parasitology, Vol. 74, No. 4, 1992, p. 400-407.

Research output: Contribution to journalArticle

@article{67e1cd88c9854e2d898c67c9b5c55887,
title = "Fasciola hepatica: Molecular cloning, nucleotide sequence, and expression of a gene encoding a polypeptide homologous to a Schistosoma mansoni fatty acid-binding protein",
abstract = "Immunization of mice with an antigenic polypeptide from Fasciola hepatica adult worms and having an apparent molecular mass of 12,000 Da (Fh12) has been shown to reduce the worm burden from challenge infection with Schistosoma mansoni by more than 50{\%}. Moreover, mice infected with S. mansoni develop antibodies to Fh12 after 5-6 weeks of infection, indicating that this Fasciola-derived antigen is a cross-reactive, cross-protective protein. A λgt11 F. hepatica cDNA library was constructed from poly(A)+ RNA extracted from adult worms. A cDNA encoding a cross-reactive polypeptide (Fh15) was cloned by screening the F. hepatica λgt11 library with a monospecific, polyclonal rabbit antiserum against pure, native Fh12. The cDNA was sequenced and the predicted amino acid sequence revealed an open reading frame encoding a 132-amino-acid protein with a predicted molecular weight of 14,700 Da. This protein has significant homology to a 14-kDa S. mansoni fatty acid-binding protein. Comparison of the protective-inducing activity of recombinant Fh15 with that of purified Fh12 against schistosomes and Fasciola is warranted.",
keywords = "cDNA clones, Fasciola hepatica, Fatty acid-binding protein, Schistosoma mansoni, Trematodes",
author = "Jos{\'e} Rodr{\'i}guez-P{\'e}rez and Jos{\'e}R Rodrǵuez-Medina and Mariano Garcia-Blanco and Hillyer, {George V.}",
year = "1992",
doi = "10.1016/0014-4894(92)90202-L",
language = "English (US)",
volume = "74",
pages = "400--407",
journal = "Experimental Parasitology",
issn = "0014-4894",
publisher = "Academic Press Inc.",
number = "4",

}

TY - JOUR

T1 - Fasciola hepatica

T2 - Molecular cloning, nucleotide sequence, and expression of a gene encoding a polypeptide homologous to a Schistosoma mansoni fatty acid-binding protein

AU - Rodríguez-Pérez, José

AU - Rodrǵuez-Medina, JoséR

AU - Garcia-Blanco, Mariano

AU - Hillyer, George V.

PY - 1992

Y1 - 1992

N2 - Immunization of mice with an antigenic polypeptide from Fasciola hepatica adult worms and having an apparent molecular mass of 12,000 Da (Fh12) has been shown to reduce the worm burden from challenge infection with Schistosoma mansoni by more than 50%. Moreover, mice infected with S. mansoni develop antibodies to Fh12 after 5-6 weeks of infection, indicating that this Fasciola-derived antigen is a cross-reactive, cross-protective protein. A λgt11 F. hepatica cDNA library was constructed from poly(A)+ RNA extracted from adult worms. A cDNA encoding a cross-reactive polypeptide (Fh15) was cloned by screening the F. hepatica λgt11 library with a monospecific, polyclonal rabbit antiserum against pure, native Fh12. The cDNA was sequenced and the predicted amino acid sequence revealed an open reading frame encoding a 132-amino-acid protein with a predicted molecular weight of 14,700 Da. This protein has significant homology to a 14-kDa S. mansoni fatty acid-binding protein. Comparison of the protective-inducing activity of recombinant Fh15 with that of purified Fh12 against schistosomes and Fasciola is warranted.

AB - Immunization of mice with an antigenic polypeptide from Fasciola hepatica adult worms and having an apparent molecular mass of 12,000 Da (Fh12) has been shown to reduce the worm burden from challenge infection with Schistosoma mansoni by more than 50%. Moreover, mice infected with S. mansoni develop antibodies to Fh12 after 5-6 weeks of infection, indicating that this Fasciola-derived antigen is a cross-reactive, cross-protective protein. A λgt11 F. hepatica cDNA library was constructed from poly(A)+ RNA extracted from adult worms. A cDNA encoding a cross-reactive polypeptide (Fh15) was cloned by screening the F. hepatica λgt11 library with a monospecific, polyclonal rabbit antiserum against pure, native Fh12. The cDNA was sequenced and the predicted amino acid sequence revealed an open reading frame encoding a 132-amino-acid protein with a predicted molecular weight of 14,700 Da. This protein has significant homology to a 14-kDa S. mansoni fatty acid-binding protein. Comparison of the protective-inducing activity of recombinant Fh15 with that of purified Fh12 against schistosomes and Fasciola is warranted.

KW - cDNA clones

KW - Fasciola hepatica

KW - Fatty acid-binding protein

KW - Schistosoma mansoni

KW - Trematodes

UR - http://www.scopus.com/inward/record.url?scp=0026871072&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=0026871072&partnerID=8YFLogxK

U2 - 10.1016/0014-4894(92)90202-L

DO - 10.1016/0014-4894(92)90202-L

M3 - Article

C2 - 1592092

AN - SCOPUS:0026871072

VL - 74

SP - 400

EP - 407

JO - Experimental Parasitology

JF - Experimental Parasitology

SN - 0014-4894

IS - 4

ER -