دوره 20، شماره 80 - ( 5-1391 )                   جلد 20 شماره 80 صفحات 11-1 | برگشت به فهرست نسخه ها

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Dakterzada F, Mohabati Mobarez A, Habibi Roudkenar M, Forouzandeh M. Cloning and Expression of N-teminal Domain of Pseudomonas aeruginosa Flagellin and Evaluation of Antibodies Raised against it on Motility Inhibition of Pseudomonas aeruginosa. J Adv Med Biomed Res 2012; 20 (80) :1-11
URL: http://journal.zums.ac.ir/article-1-1826-fa.html
دکتر زاده فریده، محبتی مبارز اشرف، حبیبی رود کنار مهریار، فروزنده مقدم مهدی. کلونینگ و بیان دومین انتهای آمینی فلاژلین پسودوموناس آئروژینوزا و ارزیابی آنتی‌بادی‌های تولید شده بر علیه آن در مهار حرکت پسودوموناس آئروژینوزا. Journal of Advances in Medical and Biomedical Research. 1391; 20 (80) :1-11

URL: http://journal.zums.ac.ir/article-1-1826-fa.html


1- ، mmmobarez@modares.ac.ir
چکیده:   (176636 مشاهده)

Background and Objective: Pseudomonas aeruginosa is an opportunistic pathogen that causes severe and lethal infections in immunocompromised individuals. This bacterium possesses a single polar flagellum. Flagellum and its subunit Flagellin play important roles in the pathogenesis of P. aeruginosa. Flagellin induces immune responses by interaction of its N-terminal domain with TLR-5. Our main aims of this study were cloning and expression of N-terminal domains of flagellin and evaluation of antibodies raised against it on motility inhibition of P. aeruginosa. Material and Methods: The DNA sequence coding for the first 161 amino acids of flagellin was PCR amplified and cloned into a pET-28a expression vector. Recombinant protein was over expressed in BL-21(DE3), and purified by Ni-NTA resin. The immune reactivity of recombinant truncated flagellin was evaluated by Western blotting. The recombinant protein was injected into a rabbit and antibodies raised against it were evaluated for the cell motility inhibition of P. aeruginosa 8821M. Results: The N-terminal domain of Flagellin was successfully overexpressed in Escherichia coli BL-21(DE3) host strain. Anti-native and anti-N-terminal flagellin antibodies reacted with the recombinant protein. Motility inhibition assay demonstrated that polyclonal antiserum against N-teminal flagellin is able to inhibit the motility of P. aeruginosa 8821M. Conclusion: The N-terminal domain of flagellin may be used for development of a new recombinant vaccine against P. aeruginosa infections.

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نوع مطالعه: کارآزمایی بالینی |
دریافت: 1391/4/21 | پذیرش: 1393/3/31 | انتشار: 1393/3/31

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