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A proteogenomic approach to map the proteome of an unsequenced pathogen – Leishmania donovani

Publication Type : Journal Article

Publisher : Proteomics

Source : Proteomics, Volume 12, Number 6, p.832-844 (2012)

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Keywords : amastigote, amino acid sequence, amino terminal sequence, article, bacterial enzyme, bacterial gene, bacterial genome, carboxy terminal sequence, Databases, Gene expression profiling, gene identification, genome analysis, Hexapoda, Kinetoplastida, Leishmania braziliensis, Leishmania donovani, Leishmania infantum, Leishmania major, Leishmaniasis, membrane protein, Molecular Sequence Data, Naso hexacanthus, nonhuman, priority journal, promastigote, protein, protein determination, protein expression, protein secretion, proteome, proteomics, Protozoa, protozoal protein, Protozoan Proteins, sequence homology, structural bioinformatics, structural proteomics, tandem mass spectrometry, virulence factor, Virulence Factors, Visceral

Campus : Amritapuri

School : School of Biotechnology

Year : 2012

Abstract : Visceral leishmaniasis or kala azar is the most severe form of leishmaniasis and is caused by the protozoan parasite Leishmania donovani. There is no published report on L. donovani genome sequence available till date, although the genome sequences of three related Leishmania species are already available. Thus, we took a proteogenomic approach to identify proteins from two different life stages of L. donovani. From our analysis of the promastigote (insect) and amastigote (human) stages of L. donovani, we identified a total of 22322 unique peptides from a homology-based search against proteins from three Leishmania species. These peptides were assigned to 3711 proteins in L. infantum, 3287 proteins in L. major, and 2433 proteins in L. braziliensis. Of the 3711 L. donovani proteins that were identified, the expression of 1387 proteins was detectable in both life stages of the parasite, while 901 and 1423 proteins were identified only in promastigotes and amastigotes life stages, respectively. In addition, we also identified 13 N-terminally and one C-terminally extended proteins based on the proteomic data search against the six-frame translated genome of the three related Leishmania species. Here, we report results from proteomic profiling of L. donovani, an organism with an unsequenced genome. © 2012 WILEY-VCH Verlag GmbH Co. KGaA, Weinheim.

Cite this Research Publication : Hab Pawar, Sahasrabuddhe, N. Aac d e, Renuse, Sad e f, Keerthikumar, Sak, Sharma, Jac, Kumar, G. S. Sag, Venugopal, Aag, Sekhar, N. Rah, Kelkar, D. Saf, Nemade, Hi, Khobragade, S. Ni, Muthusamy, Bah, Kandasamy, Kal, H. C. Harsha, Chaerkady, Rad e, Patole, M. Si, and Pandey, Ade j k, “A proteogenomic approach to map the proteome of an unsequenced pathogen - Leishmania donovani”, Proteomics, vol. 12, pp. 832-844, 2012.

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