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Iranian Red Crescent Medical Journal، جلد ۱۸، شماره ۶، صفحات ۰-۰
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| عنوان فارسی |
Cloning, Expression, and Purification of Pseudomonas aeruginosa Flagellin, and Characterization of the Elicited Anti-Flagellin Antibody |
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| چکیده فارسی مقاله |
Conclusions The r-B-flagellin carried antigenic epitopes just like the native flagellin, while the polyclonal antibody raised against it exhibited functional activity. Results The polyclonal antibodies raised against this r-B-flagellin inhibited the motility of the homologous PAO1 strain of P. aeruginosa, which significantly decreased the invasion of the PAO1 strain into the A549 cells and also enhanced the opsonophagocytosis of this strain. However, our polyclonal antibody showed little effect on the heterologous PAK strain. Materials and Methods In the current experimental study, the r-B-flagellin gene was isolated from the P. aeruginosa PAO1 strain by PCR. It was cloned into the pET-28a vector and then transformed into the E. coli BL21 strain. Next, r-B-flagellin was overexpressed and affinity purified by Ni-NTA agarose-affinity chromatography, followed by on-column resolubilization. Polyclonal antisera against the recombinant flagellin were raised in rabbits, and the functional activity of the anti-r-B-flagellin antibody was determined by in vitro assays. Background Pseudomonas aeruginosa is an important opportunistic human pathogen that causes serious infections in immunocompromised hosts. The single polar flagellum is an important factor in both virulence and colonization. Objectives As flagellin is the major component of the flagellar filament, the main aims of the present study are to identify, clone, express, and purify the recombinant type B flagellin (r-B-flagellin) of P. aeruginosa, as well as to evaluate the functional activity of the rabbit polyclonal antibody raised against this r-B-flagellin. |
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| کلیدواژه‌های فارسی مقاله |
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| عنوان انگلیسی |
Cloning, Expression, and Purification of Pseudomonas aeruginosa Flagellin, and Characterization of the Elicited Anti-Flagellin Antibody |
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| چکیده انگلیسی مقاله |
Conclusions The r-B-flagellin carried antigenic epitopes just like the native flagellin, while the polyclonal antibody raised against it exhibited functional activity. Results The polyclonal antibodies raised against this r-B-flagellin inhibited the motility of the homologous PAO1 strain of P. aeruginosa, which significantly decreased the invasion of the PAO1 strain into the A549 cells and also enhanced the opsonophagocytosis of this strain. However, our polyclonal antibody showed little effect on the heterologous PAK strain. Materials and Methods In the current experimental study, the r-B-flagellin gene was isolated from the P. aeruginosa PAO1 strain by PCR. It was cloned into the pET-28a vector and then transformed into the E. coli BL21 strain. Next, r-B-flagellin was overexpressed and affinity purified by Ni-NTA agarose-affinity chromatography, followed by on-column resolubilization. Polyclonal antisera against the recombinant flagellin were raised in rabbits, and the functional activity of the anti-r-B-flagellin antibody was determined by in vitro assays. Background Pseudomonas aeruginosa is an important opportunistic human pathogen that causes serious infections in immunocompromised hosts. The single polar flagellum is an important factor in both virulence and colonization. Objectives As flagellin is the major component of the flagellar filament, the main aims of the present study are to identify, clone, express, and purify the recombinant type B flagellin (r-B-flagellin) of P. aeruginosa, as well as to evaluate the functional activity of the rabbit polyclonal antibody raised against this r-B-flagellin. |
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| نویسندگان مقاله |
بهادر بهروز | bahador behrouz
department of microbiology, school of medicine, tehran university of medical sciences, tehran, ir iran
سازمان اصلی تایید شده: دانشگاه علوم پزشکی تهران (Tehran university of medical sciences)
نور امیرمظفری | nour amirmozafari
department of microbiology, school of medicine, iran university of medical sciences, tehran, ir iran; department of microbiology, school of medicine, iran university of medical sciences, tehran, ir iran. tel 98-2188058649
سازمان اصلی تایید شده: دانشگاه علوم پزشکی ایران (Iran university of medical sciences)
نیما خرم آبادی | nima khoramabadi
department of bacteriology, faculty of medical sciences, tarbiat modares university, tehran, ir iran
سازمان اصلی تایید شده: دانشگاه تربیت مدرس (Tarbiat modares university)
محبوبه بحرودی | mahboobeh bahroudi
department of microbiology, school of medicine, tehran university of medical sciences, tehran, ir iran
سازمان اصلی تایید شده: دانشگاه علوم پزشکی تهران (Tehran university of medical sciences)
پریسا legaee | parisa legaee
department of microbiology, school of medicine, iran university of medical sciences, tehran, ir iran
سازمان اصلی تایید شده: دانشگاه علوم پزشکی ایران (Iran university of medical sciences)
مهدی مهدوی | mehdi mahdavi
department of immunology, pasteur institute of iran, tehran, ir iran
سازمان اصلی تایید شده: انستیتو پاستور ایران (Pasteur institute of iran)
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| نشانی اینترنتی |
http://www.ircmj.com/index.php?page=article&article_id=28271 |
| فایل مقاله |
فایلی برای مقاله ذخیره نشده است |
| کد مقاله (doi) |
10.5812/ircmj.28271 |
| زبان مقاله منتشر شده |
fa |
| موضوعات مقاله منتشر شده |
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| نوع مقاله منتشر شده |
research-article |
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