<?xml version="1.0" encoding="utf-8"?>
<journal>
<title>Journal of Advances in Medical and Biomedical Research</title>
<title_fa>Journal of Advances in Medical and Biomedical Research</title_fa>
<short_title>J Adv Med Biomed Res</short_title>
<subject>Medical Sciences</subject>
<web_url>http://journal.zums.ac.ir</web_url>
<journal_hbi_system_id>52</journal_hbi_system_id>
<journal_hbi_system_user>journal52</journal_hbi_system_user>
<journal_id_issn>1606-9366</journal_id_issn>
<journal_id_issn_online>2676-6264</journal_id_issn_online>
<journal_id_pii></journal_id_pii>
<journal_id_doi>10.30699/jambr</journal_id_doi>
<journal_id_iranmedex></journal_id_iranmedex>
<journal_id_magiran></journal_id_magiran>
<journal_id_sid></journal_id_sid>
<journal_id_nlai></journal_id_nlai>
<journal_id_science></journal_id_science>
<language>en</language>
<pubdate>
	<type>jalali</type>
	<year>1391</year>
	<month>4</month>
	<day>1</day>
</pubdate>
<pubdate>
	<type>gregorian</type>
	<year>2012</year>
	<month>7</month>
	<day>1</day>
</pubdate>
<volume>20</volume>
<number>80</number>
<publish_type>online</publish_type>
<publish_edition>1</publish_edition>
<article_type>fulltext</article_type>
<articleset>
	<article>


	<language>fa</language>
	<article_id_doi></article_id_doi>
	<title_fa>کلونینگ و بیان دومین انتهای آمینی فلاژلین پسودوموناس آئروژینوزا و ارزیابی آنتی‌بادی‌های تولید شده بر علیه آن در مهار حرکت پسودوموناس آئروژینوزا</title_fa>
	<title>Cloning and Expression of N-teminal Domain of Pseudomonas aeruginosa Flagellin and Evaluation of Antibodies Raised against it on Motility Inhibition of Pseudomonas aeruginosa</title>
	<subject_fa></subject_fa>
	<subject></subject>
	<content_type_fa>کارآزمایی بالینی</content_type_fa>
	<content_type>Clinical Trials</content_type>
	<abstract_fa></abstract_fa>
	<abstract>&lt;p&gt;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.&lt;/p&gt;</abstract>
	<keyword_fa></keyword_fa>
	<keyword>Keywords: Cloning, Motility inhibition, N-terminal domains of flagellin, Pseudomonas aeruginosa</keyword>
	<start_page>1</start_page>
	<end_page>11</end_page>
	<web_url>http://journal.zums.ac.ir/browse.php?a_code=A-10-4-636&amp;slc_lang=fa&amp;sid=1</web_url>


<author_list>
	<author>
	<first_name>Farideh</first_name>
	<middle_name></middle_name>
	<last_name>Dakterzada</last_name>
	<suffix></suffix>
	<first_name_fa>فریده</first_name_fa>
	<middle_name_fa></middle_name_fa>
	<last_name_fa>دکتر زاده</last_name_fa>
	<suffix_fa></suffix_fa>
	<email></email>
	<code>5200319475328460059850</code>
	<orcid>5200319475328460059850</orcid>
	<coreauthor>No</coreauthor>
	<affiliation>Dept. of Bacteriology, Faculty of Medical Sciences, Tarbiat Modares University, Tehran, Iran.</affiliation>
	<affiliation_fa></affiliation_fa>
	 </author>


	<author>
	<first_name>Ashraf</first_name>
	<middle_name></middle_name>
	<last_name>Mohabati Mobarez</last_name>
	<suffix></suffix>
	<first_name_fa>اشرف</first_name_fa>
	<middle_name_fa></middle_name_fa>
	<last_name_fa>محبتی مبارز</last_name_fa>
	<suffix_fa></suffix_fa>
	<email>mmmobarez@modares.ac.ir</email>
	<code>5200319475328460059851</code>
	<orcid>5200319475328460059851</orcid>
	<coreauthor>Yes
</coreauthor>
	<affiliation>Dept. of Bacteriology, Faculty of Medical Sciences, Tarbiat Modares University, Tehran, Iran.</affiliation>
	<affiliation_fa></affiliation_fa>
	 </author>


	<author>
	<first_name>Mahyar</first_name>
	<middle_name></middle_name>
	<last_name>Habibi Roudkenar</last_name>
	<suffix></suffix>
	<first_name_fa>مهریار</first_name_fa>
	<middle_name_fa></middle_name_fa>
	<last_name_fa>حبیبی رود کنار</last_name_fa>
	<suffix_fa></suffix_fa>
	<email></email>
	<code>5200319475328460059852</code>
	<orcid>5200319475328460059852</orcid>
	<coreauthor>No</coreauthor>
	<affiliation>Research Center, Iranian Blood Transfusion Organization, Tehran, Iran</affiliation>
	<affiliation_fa></affiliation_fa>
	 </author>


	<author>
	<first_name>Mehdi</first_name>
	<middle_name></middle_name>
	<last_name>Forouzandeh</last_name>
	<suffix></suffix>
	<first_name_fa>مهدی</first_name_fa>
	<middle_name_fa></middle_name_fa>
	<last_name_fa>فروزنده مقدم</last_name_fa>
	<suffix_fa></suffix_fa>
	<email></email>
	<code>5200319475328460059853</code>
	<orcid>5200319475328460059853</orcid>
	<coreauthor>No</coreauthor>
	<affiliation>Dept. of Biotechnology, Faculty of Medical Sciences, Tarbiat Modares University, Tehran, Iran.</affiliation>
	<affiliation_fa></affiliation_fa>
	 </author>


</author_list>


	</article>
</articleset>
</journal>
