Molecular and functional characterisation of the heat shock protein 10 of Strongyloides ratti

Strongyloides stercoralis and S. ratti are intestinal parasitic nematodes infecting rats and humans, respectively. Both present extraordinary life cycles comprising a free-living generation in addition to parasitic stages. In search of molecules possibly involved in parasite–host interaction, we per...

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Bibliographic Details
Published in:Molecular and biochemical parasitology 2009-12, Vol.168 (2), p.149-157
Main Authors: Tazir, Yasmina, Steisslinger, Vera, Soblik, Hanns, Younis, Abuelhassan Elshazly, Beckmann, Svenja, Grevelding, Christoph G., Steen, Hanno, Brattig, Norbert W., Erttmann, Klaus D.
Format: Article
Language:English
Subjects:
Animals
Antibodies, Helminth - blood
Antigens, Helminth - chemistry
Antigens, Helminth - genetics
Antigens, Helminth - immunology
Antigens, Helminth - metabolism
Base Sequence
Chaperonin 10 - chemistry
Chaperonin 10 - genetics
Chaperonin 10 - immunology
Chaperonin 10 - metabolism
Chaperonin 60 - metabolism
Dimerization
DNA, Helminth - chemistry
DNA, Helminth - genetics
Excretory/secretory product
Gene Expression Profiling
Gene organisation
Heat shock protein
Helminth
Immune response
Molecular Sequence Data
Molecular Weight
Protein Binding
Protein Interaction Mapping
Rats
Rats, Wistar
Sequence Analysis, DNA
Strongyloides
Strongyloides ratti - physiology
Two-Hybrid System Techniques
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Summary:Strongyloides stercoralis and S. ratti are intestinal parasitic nematodes infecting rats and humans, respectively. Both present extraordinary life cycles comprising a free-living generation in addition to parasitic stages. In search of molecules possibly involved in parasite–host interaction, we performed mass spectrometry to identify excretory/secretory products of S. ratti. Amongst others we detected homologs of the heat shock proteins HSP10 and HSP60 (Sr-HSP10 and Sr-HSP60). HSPs are well known as chaperones involved in stress responses of cells, but recent studies suggest additional roles of small HSPs for parasite biology including immune modulation. To characterise Sr-HSP10, we cloned its full-length cDNA, analysed the genomic organisation, tested its presumptive role as an interaction partner of Sr-HSP60, studied its transcription in the parasite, and expressed the protein to test its immune responses. The cDNA contains an open reading frame of 330bp encoding a polypeptide of 110 amino acids with an approximate molecular weight of 10kDa. The Sr-HSP10 protein is highly homologous to that of the human pathogen S. stercoralis with only eight amino acid substitutions. Analysis of the genomic organisation of the Sr-HSP10 locus revealed that the gene is linked head-to-head to the gene encoding Sr-HSP60, and both share a bidirectional promoter. RT-PCR experiments indicated potential independent expression of the Sr-HSPs genes. In situ hybridisation results demonstrate Sr-HSP10 transcription in the gut area. Mammalian and yeast two-hybrid assays show dimerisation of Sr-HSP10, but no binding to recombinant Sr-HSP60. Immunisation experiments finally revealed a strong immunogenicity of Sr-HSP10 and provided evidence for a role in regulating the host–parasite interaction.
ISSN:0166-6851
1872-9428
DOI:10.1016/j.molbiopara.2009.07.007