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Cloning and analysis of a Trichinella britovi gene encoding a cytoplasmic heat shock protein of 72 kDa

Published online by Cambridge University Press:  01 July 1999

M. VAYSSIER
Affiliation:
UMR INRA-AFSSA-ENVA, Biologie Moléculaire et Immunologie Parasitaires et Fongiques, 22 rue Pierre Curie, 94 703 Maisons-Alfort, France
F. LE GUERHIER
Affiliation:
UMR INRA-AFSSA-ENVA, Biologie Moléculaire et Immunologie Parasitaires et Fongiques, 22 rue Pierre Curie, 94 703 Maisons-Alfort, France
J. F. FABIEN
Affiliation:
UMR INRA-AFSSA-ENVA, Biologie Moléculaire et Immunologie Parasitaires et Fongiques, 22 rue Pierre Curie, 94 703 Maisons-Alfort, France
H. PHILIPPE
Affiliation:
Université Paris-Sud Laboratoire de Biologie Cellulaire bât 444, 91405 Orsay cedex France
C. VALLET
Affiliation:
UMR INRA-AFSSA-ENVA, Biologie Moléculaire et Immunologie Parasitaires et Fongiques, 22 rue Pierre Curie, 94 703 Maisons-Alfort, France
G. ORTEGA-PIERRES
Affiliation:
Departamento de Genética y Biologia Molecular, CINVESTAV, Mexico DF, Mexico
C. SOULE
Affiliation:
UMR INRA-AFSSA-ENVA, Biologie Moléculaire et Immunologie Parasitaires et Fongiques, 22 rue Pierre Curie, 94 703 Maisons-Alfort, France
C. PERRET
Affiliation:
UMR INRA-AFSSA-ENVA, Biologie Moléculaire et Immunologie Parasitaires et Fongiques, 22 rue Pierre Curie, 94 703 Maisons-Alfort, France
LIU MINGYUAN
Affiliation:
University of Agriculture and Animal Sciences, Changchun, China
M. VEGA-LOPEZ
Affiliation:
Departamento de Genética y Biologia Molecular, CINVESTAV, Mexico DF, Mexico
P. BOIREAU
Affiliation:
UMR INRA-AFSSA-ENVA, Biologie Moléculaire et Immunologie Parasitaires et Fongiques, 22 rue Pierre Curie, 94 703 Maisons-Alfort, France

Abstract

A gene encoding a protein of 646 amino acid residues with a molecular mass of 71·3 kDa showing homology to the cytoplasmic form of the 70 kDa heat shock protein was cloned and sequenced from the nematode parasite Trichinella britovi (Tb). The gene was expressed in vitro as a protein of 71 kDa that was immunoprecipitated by a Trichinella-infected rabbit serum. Monospecific polyclonal antibodies raised against the recombinant Tb Hsp70 expressed in Escherichia coli, recognized a protein of 70 kDa by Western blot analysis of Tb soluble antigen (muscular stage). Tb Hsp70 was located in the nuclei of the muscle larvae as determined by the indirect immunofluorescent pattern on cross-sections of the worm. The expression of this protein was not detected in adult worm nuclei suggesting a differential expression of Hsp70 between the 2 stages of Trichinella.

Type
Research Article
Copyright
1999 Cambridge University Press

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