RESEARCH ARTICLE


Proteome Analysis of Leptospira interrogans Virulent Strain



Monica L Vieira1, 2, Daniel C Pimenta3, Zenaide M de Morais4, Silvio A Vasconcellos4, Ana L.T.O Nascimento1, 2, *
1 Centro de Biotecnologia, Instituto Butantan, Avenida Vital Brazil, 1500, 05503-900, São Paulo, SP, Brazil
2 Interunidades em Biotecnologia, Instituto de Ciências Biomédicas, USP, São Paulo, Brazil
3 Laboratório de Bioquímica e Biofísica, Instituto Butantan, Avenida Vital Brazil, 1500, 05503-900, São Paulo, SP, Brazil
4 Laboratorio de Zoonoses Bacterianas do VPS, Faculdade de Medicina Veterinária e Zootecnia da Universidade de São Paulo, Brazil


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© Vieira et al.; Licensee Bentham Open.

open-access license: This is an open access article licensed under the terms of the Creative Commons Attribution Non-Commercial License (http://creativecommons.org/licenses/by-nc/3.0/) which permits unrestricted, non-commercial use, distribution and reproduction in any medium, provided the work is properly cited.

* Address correspondence to this author at the Centro de Biotecnologia, Instituto Butantan, Avenida Vital Brazil, 1500, 05503-900, Säo Paulo, SP, Brazil; Tel: (5511) 37220019; Fax: (5511) 37261505; E-mail: tabet@butantan.gov.br


Abstract

Leptospirosis is a worldwide zoonotic infection of human and veterinary concern. Caused by pathogenic spirochetes of the genus Leptospira, the disease presents greater incidence in tropical and subtropical regions. The identification of proteins that could be involved in the bacteria host interactions may facilitate the search for immune protective antigens. We report the proteomic analysis of Leptospira interrogans serovar Pomona virulent strain LPF cultured from kidney and liver of infected hamsters. Total protein extracts were separated by two-dimensional gel electrophoresis (2-DE), 895 spots were analyzed by MALDI-TOF mass spectrometry (MS), and 286 were identified as leptospiral proteins, corresponding to 108 distinct proteins. These proteins are allocated in all the bacterial cell compartments and are distributed in every functional category. Furthermore, the previously described, known outer membrane proteins, OmpL1, LipL21, LipL31, LipL32/Hap-1, LipL41, LipL45, LipL46, LruA/LipL71, and OmpA-like protein Loa22 were all recognized. Most importantly, this research work identified 27 novel leptospiral proteins annotated as hypothetical open reading frames (ORFs). We report for the first time an array of proteins of the Leptospira expressed by virulent, low-passage strain. We believe that our studies, together with the genome data will enlighten our understanding of the disease.

Key Words: Leptospira interrogans, leptospirosis, proteomics.