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In a search for molecules involved in the interaction between intestinal nematodes and mammalian mucosal host cells, we performed MS to iden-tify excretory–secretory proteins from Strongyloides ratti. | IFEBS Journal Stage-specific excretory-secretory small heat shock proteins from the parasitic nematode Strongyloides ratti - putative links to host s intestinal mucosal defense system Abuelhassan Elshazly Younis1 Frank Geisinger1 Irene Ajonina-Ekoti2 Hanns Soblik1 Hanno Steen3 Makedonka Mitreva4 Klaus D. Erttmann1 Markus Perbandt5 6 Eva Liebau2 and Norbert W. Brattig1 1 Bernhard Nocht Institute for TropicalMedicine Hamburg Germany 2 Institute of AnimalPhysiology Muenster Germany 3 Proteomics Center at Children s HospitalBoston Harvard Medical School Boston MA USA 4 The Genome Institute Washington University Schoolof Medicine St Louis MO USA 5 Department of Chemistry Laboratory for StructuralBiology of Infection and Inflammation University of Hamburg Germany 6 Department of MedicalMicrobiology Virology and Hygiene University MedicalCenter Hamburg-Eppendorf Germany Keywords excretory-secretory proteins heat shock proteins HSP-17 immune response Strongyloides Correspondence N. Brattig AE Younis Bernhard Nocht Institute for Tropical Medicine Bernhard-Nocht-Strasse 74 20359 Hamburg Germany Fax 49 42818 400 Tel. 49 42818 530 E-mail nbrattig@bni-hamburg.de abssan2000@yahoo.com Received 24 March 2011 revised 7 July 2011 accepted 13 July 2011 doi 10.1111 j.1742-4658.2011.08248.x In a search for molecules involved in the interaction between intestinal nematodes and mammalian mucosal host cells we performed MS to identify excretory-secretory proteins from Strongyloides ratti. In the excretory-secretory proteins of the parasitic female stage we detected in addition to other peptides peptides homologous with the Caenorhabditis elegans heat shock protein HSP -17 named Sra-HSP-17.1 19 kDa and Sra-HSP-17.2 18 kDa with 49 amino acid identity. The full-length cDNAs 483 bp and 474 bp respectively were identified and the genomic organization was analyzed. To allow further characterization the proteins were recombinantly expressed and purified. Profiling of transcription by .
