کد مقاله | کد نشریه | سال انتشار | مقاله انگلیسی | نسخه تمام متن |
---|---|---|---|---|
8645783 | 1569793 | 2018 | 9 صفحه PDF | دانلود رایگان |
عنوان انگلیسی مقاله ISI
Characterization of ML0314c of Mycobacterium leprae and deciphering its role in the immune response in leprosy patients
دانلود مقاله + سفارش ترجمه
دانلود مقاله ISI انگلیسی
رایگان برای ایرانیان
کلمات کلیدی
PBSNBTBCIPMTBMycobacterium lepraeEpitopes - اپیتوپ هاnitro blue tetrazolium - تترازولیم نیترو آبیcircular dichroism - رنگ تابی دورانیWorld Health Organization - سازمان بهداشت جهانیphosphate buffer saline - فسفات بافر شورMycobacterium tuberculosis - مایکوباکتریوم توبرکلوزیسLipids - چربیهاoptical density - چگالی نوریCarboxyl esterase - کربوکسیل استرازWHO - که
موضوعات مرتبط
علوم زیستی و بیوفناوری
بیوشیمی، ژنتیک و زیست شناسی مولکولی
ژنتیک
پیش نمایش صفحه اول مقاله
![عکس صفحه اول مقاله: Characterization of ML0314c of Mycobacterium leprae and deciphering its role in the immune response in leprosy patients Characterization of ML0314c of Mycobacterium leprae and deciphering its role in the immune response in leprosy patients](/preview/png/8645783.png)
چکیده انگلیسی
Mycobacterium leprae has a reduced genome size due to the reductive evolution over a long period of time. Lipid metabolism plays an important role in the life cycle and pathogenesis of this bacterium. In comparison to 26 lip genes (Lip A-Z) of M. tuberculosis, M. leprae retained only three orthologs indicating their importance in its life cycle. ML0314c (LipU) is one of them. It is conserved throughout the mycobacterium species. Bioinformatics analysis showed the presence of an α/β hydrolase fold and 'GXSXG' characteristic of the esterases/lipases. The gene was expressed in E. coli and purified to homogeneity. It showed preference towards short chain esters with pNP-acetate as the preferred substrate. The enzyme showed optimal activity at 45 °C and pH 8.0. ML0314c protein was stable between temperatures ranging from 20 to 60 °C and pH 5.0-8.0, i.e., relatively acidic and neutral conditions. The active site residues predicted bioinformatically were confirmed to be Ser168, Glu267, and His297 by site directed mutagenesis. E-serine, DEPC and Tetrahydrolipstatin (THL) completely inhibited the activity of ML0314c. The protein was localized in cell wall and extracellular medium. Several antigenic epitopes were predicted in ML0314c. Protein elicited strong humoral immune response in leprosy patients, whereas, a reduced immune response was observed in the relapsed cases. No humoral response was observed in treatment completed patients. Overexpression of ml0314c in the surrogate host M. smegmatis showed marked difference in the colony morphology and growth rate. In conclusion, ML0314c is a secretary carboxyl esterase that could modulate the immune response in leprosy patients.
ناشر
Database: Elsevier - ScienceDirect (ساینس دایرکت)
Journal: Gene - Volume 643, 15 February 2018, Pages 26-34
Journal: Gene - Volume 643, 15 February 2018, Pages 26-34
نویسندگان
Gurkamajit Kaur, Aashish Sharma, Tarun Narang, Sunil Dogra, Jagdeep Kaur,