[Home ] [Archive]   [ فارسی ]  
:: Main :: About :: Current Issue :: Archive :: Search :: Submit :: Contact ::
Main Menu
Home::
Journal Information::
Editorial Board::
Executive Members::
Instruction to Authors::
Peer Review::
Articles Archive::
Indexing Databases::
Contact Us::
Site Facilities::
::
Search in website

Advanced Search
Receive site information
Enter your Email in the following box to receive the site news and information.
:: Volume 12, Issue 2 (7-2010) ::
J Gorgan Univ Med Sci 2010, 12(2): 33-41 Back to browse issues page
First report on the shortest CPB peptide chain in the Leishmania donovani complex and bioinformatical interpretations in relation with this mutation
Maleki Ravasan N (MSc) , Hide M (PhD) , Javadian E (PhD) , Oshaghi MA (PhD) * 1, Sadraei J (PhD)
Abstract:   (22279 Views)
Background and Objective: Visceral Leishmaniasis or Kala-azar is an important infectious disease in northwestern Iran. Members of the Leishmania donovani complex, L. donovani and L.infantum, are the two main parasites causing the disease in the world. In this study immunophenotype characters such as N-glycosylation, and T-cell and B-Cell epitopes of CPB gene was evaluated in the Leishmania parasites isolated from sandflies of the region. Materials and Methods: Partial of the CPB (702-741 bp) of Leishmania parasites was amplified and sequenced and used for bioinformatics analysis such as test three dimensional (3D) protein structure, N-glycosylation, and T-cell and B-Cell epitopes. Results: In 7 out of 3477 sand flies there was a positive PCR test for systeine protease B, gene. Also according to findings of this study, both agents of kala-azar L. donovani and L. infantum were bing transfered by sand flies of Phlbtomus perfiliewi transcaucasicus in North West Iran. DNA analysis of the CPB gene showed a cytosine insertion at 5’ end of the proofreading frame of the gene resulted in a stop codon (TGA) seven AA further down and hence translation is halted. This caused a short amino acid chain with only 76 AA much shorter than normal CPB peptide with 234-247 AA. This mutation has not been found in the L.infantum strain resulted in a normal CPB peptide. AA analysis showed no N-glycosylation site, T-cell and B-Cell epitopes on the short peptide of the L. donovani strain. Conclusion: This is the shortest CPB peptide chain reported for the L. donovani complex in the literature. This short peptide could have an effect on host-parasite and vector-parasite interactions. Since the CPBs genes have important implication on host–parasite and play key roles in infection and expression of the disease, further studies on the L. donovani parasite and its diminutive peptide necessitate to improve our understanding about the epidemiology of visceral leishmaniasis in Iran.
Keywords: CPBs, Host–Parasite Interactions, Kala-azar, Leishmania donovani complex, Iran
Full-Text [PDF 860 kb] [English Abstract]   (19073 Downloads) |   |   Abstract (HTML)  (943 Views)  
Type of Study: Original Articles | Subject: Parasitology
* Corresponding Author Address: Associate Professor, Department of Medical Entomology and Vector Control, School of Public Health and Institute of Health Research, Tehran University of Medical Sciences, Tehran, Iran. moshaghi@sina.tums.ac.ir


XML   Persian Abstract   Print


Download citation:
BibTeX | RIS | EndNote | Medlars | ProCite | Reference Manager | RefWorks
Send citation to:

Maleki Ravasan N (MSc), Hide M (PhD), Javadian E (PhD), Oshaghi MA (PhD), Sadraei J (PhD). First report on the shortest CPB peptide chain in the Leishmania donovani complex and bioinformatical interpretations in relation with this mutation. J Gorgan Univ Med Sci 2010; 12 (2) :33-41
URL: http://goums.ac.ir/journal/article-1-730-en.html


Rights and permissions
Creative Commons License This work is licensed under a Creative Commons Attribution-NonCommercial 4.0 International License.
Volume 12, Issue 2 (7-2010) Back to browse issues page
مجله دانشگاه علوم پزشکی گرگان Journal of Gorgan University of Medical Sciences
Persian site map - English site map - Created in 0.04 seconds with 35 queries by YEKTAWEB 4660
Creative Commons License
This work is licensed under a Creative Commons — Attribution-NonCommercial 4.0 International (CC BY-NC 4.0)