کد مقاله | کد نشریه | سال انتشار | مقاله انگلیسی | نسخه تمام متن |
---|---|---|---|---|
5915870 | 1163337 | 2009 | 9 صفحه PDF | دانلود رایگان |
عنوان انگلیسی مقاله ISI
Molecular and functional characterisation of the heat shock protein 10 of Strongyloides ratti
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کلمات کلیدی
gDNAEPFsHSPIL3StrongyloidesHspHBSSIPTGORFgenomic DNA - DNA ژنومیHanks balanced salt solution - Hanks محلول نمک را تعویض می کندE/S - I / OLC–MS/MS - LC-MS / MSw/v - W / VEST - استSodium dodecylsulfate-polyacrylamide gel electrophoresis - الکتروفورز ژل سدیم دودسیل سولفات - پلی آکریل آمیدSDS-PAGE - الکتروفورز ژل پلی آکریل آمیدEnzyme-linked immunosorbent assay - تست الیزاELISA - تست الیزاExpressed Sequence Tag - تکرار اظهار نظرexcretory/secretory - دفع کننده / ترشحاتspliced leader - رهبر تقسیم شدهGene organisation - سازمان ژنEarly pregnancy factor - فاکتور حاملگی زودرسopen reading frame - قاب خواندن بازInfective larvae - لاروهای عفونیweight/volume - وزن / حجمImmune response - پاسخ یا واکنش ایمنیHeat shock protein - پروتئین شوک حرارتsmall heat shock protein - پروتئین شوک حرارتی کوچکHelminth - کرم رودهliquid chromatography–tandem mass spectrometry - کروماتوگرافی مایع و اسپکترومتری توده دو طرفه
موضوعات مرتبط
علوم زیستی و بیوفناوری
بیوشیمی، ژنتیک و زیست شناسی مولکولی
زیست شناسی مولکولی
پیش نمایش صفحه اول مقاله
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چکیده انگلیسی
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 330Â bp encoding a polypeptide of 110 amino acids with an approximate molecular weight of 10Â kDa. 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.
ناشر
Database: Elsevier - ScienceDirect (ساینس دایرکت)
Journal: Molecular and Biochemical Parasitology - Volume 168, Issue 2, December 2009, Pages 149-157
Journal: Molecular and Biochemical Parasitology - Volume 168, Issue 2, December 2009, Pages 149-157
نویسندگان
Yasmina Tazir, Vera Steisslinger, Hanns Soblik, Abuelhassan Elshazly Younis, Svenja Beckmann, Christoph G. Grevelding, Hanno Steen, Norbert W. Brattig, Klaus D. Erttmann,