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.