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:: Volume 24, Issue 2 (summer 2014) ::
MEDICAL SCIENCES 2014, 24(2): 95-102 Back to browse issues page
Determination of antigenic determinants in the C-terminal 311 amino acids of Haps adhesion from Nontypeable Haemophilus influenza
Akram Tabatabaee 1, Seyed Davar Siadat2 , Seyed Fazllolah Mousavi3 , Mohammad Reza Aghasadeghi4
1- PhD of Microbiology, Department of Biology, Islamic Azad University, Science and Research Branch, Tehran, Iran , akram_tabatabaee@yahoo.com
2- PhD of Medical Microbiology,Department of Microbiology, Pasteur Institute of Iran, Tehran, Iran
3- PhD of Microbiology & Immunology, Department of Microbiology, Pasteur Institute of Iran, Tehran, Iran
4- PhD of Biologic Process,Department of Hepatitis and AIDS, Pasteur Institute of Iran, Tehran, Iran
Abstract:   (12824 Views)
Background: Haps protein plays central role in initial interaction of nontypeable Haemophilus influenzae (NTHi) with human respiratory epithelial cells. While other surface-exposed proteins of NTHi are highly variable, The HapS domain is highly conserved among H. influenzae strains. Recent studies demonstrated that HapS adhesive activity resides within the C-terminal 311 amino acids of the protein and also they showed that the C-terminal 311 amino acids of HapS (C-Haps) are capable of eliciting a protective immune response against NTHi colonization.
Materials and methods: The pET24a-chaps plasmid harboring c-haps sequence from NTHi PTCC1766 was constructed. The amino acid sequences of C-Haps of this study was aligned with C-Haps of three NTHi strains (N187, TN106, P860295) and antigenicity plot of studied rC-Haps was done bioinformatic software. The pET24a-chaps expression was conducted in E.coli BL21 (D3E) and its expression was confirmed by SDS-PAGE and Western blotting methods. The rC-Haps was purified via immobilized metal affinity chromatography.
Results: Amino acid sequence alignment of rCHaps sequence of current study and rC-Haps from the NTHi strains N187, TN106, P860295 showed more than %97 identity. Antigenicity plot identified 9 common highly antigenic domains that were located exactly in conserved regions among 4 different NTHi strains.
Conclusion: Due to presence of highly conserved antigenic epitopes among C-Haps of NTHi PTCC1766 and other NTHi strains, rC-Haps of current study could be theoretically a vaccine candidate against NTHi strains of different geographical areas.
Keywords: Nontypeable Haemophilus influenzae, Antigenic epitopes, C-Haps
Full-Text [PDF 444 kb]   (3842 Downloads)    
Semi-pilot: Experimental | Subject: Microbiology
Received: 2014/06/21 | Accepted: 2014/06/21 | Published: 2014/06/21
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Tabatabaee A, Siadat S D, Mousavi S F, Aghasadeghi M R. Determination of antigenic determinants in the C-terminal 311 amino acids of Haps adhesion from Nontypeable Haemophilus influenza. MEDICAL SCIENCES 2014; 24 (2) :95-102
URL: http://tmuj.iautmu.ac.ir/article-1-811-en.html


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Volume 24, Issue 2 (summer 2014) Back to browse issues page
فصلنامه علوم پزشکی دانشگاه آزاد اسلامی واحد پزشکی تهران Medical Science Journal of Islamic Azad Univesity - Tehran Medical Branch
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