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(Reference retrieved automatically from Web of Science through information on FAPESP grant and its corresponding number as mentioned in the publication by the authors.)

Features of Two New Proteins with OmpA-Like Domains Identified in the Genome Sequences of Leptospira interrogans

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Author(s):
Teixeira, Aline F. [1, 2] ; de Morais, Zenaide M. [3] ; Kirchgatter, Karin [4] ; Romero, Eliete C. [5] ; Vasconcellos, Silvio A. [3] ; Nascimento, Ana Lucia T. O. [1, 2]
Total Authors: 6
Affiliation:
[1] Inst Butantan, Ctr Biotechnol, Sao Paulo, SP - Brazil
[2] Univ Sao Paulo, Inst Ciencias Biomed, Programa Posgrad Interunidades Biotecnol, Sao Paulo, SP - Brazil
[3] Univ Sao Paulo, Fac Med Vet & Zootecnia, Lab Zoonoses Bacterianas, Sao Paulo, SP - Brazil
[4] Univ Sao Paulo, Superintendencia Controle Endemias Inst Med, Nucl Estudos Malaria, Sao Paulo, SP - Brazil
[5] Adolfo Lutz Inst, Ctr Bacteriol, Sao Paulo - Brazil
Total Affiliations: 5
Document type: Journal article
Source: PLoS One; v. 10, n. 4 APR 7 2015.
Web of Science Citations: 13
Abstract

Leptospirosis is an acute febrile disease caused by pathogenic spirochetes of the genus Leptospira. It is considered an important re-emerging infectious disease that affects humans worldwide. The knowledge about the mechanisms by which pathogenic leptospires invade and colonize the host remains limited since very few virulence factors contributing to the pathogenesis of the disease have been identified. Here, we report the identification and characterization of two new leptospiral proteins with OmpA-like domains. The recombinant proteins, which exhibit extracellular matrix-binding properties, are called Lsa46 -LIC13479 and Lsa77 -LIC10050 (Leptospiral surface adhesins of 46 and 77 kDa, respectively). Attachment of Lsa46 and Lsa77 to laminin was specific, dose dependent and saturable, with K-D values of 24.3 +/- 17.0 and 53.0 +/- 17.5 nM, respectively. Lsa46 and Lsa77 also bind plasma fibronectin, and both adhesins are plasminogen (PLG)-interacting proteins, capable of generating plasmin (PLA) and as such, increase the proteolytic ability of leptospires. The proteins corresponding to Lsa46 and Lsa77 are present in virulent L. interrogans L1-130 and in saprophyte L. biflexa Patoc 1 strains, as detected by immunofluorescence. The adhesins are recognized by human leptospirosis serum samples at the onset and convalescent phases of the disease, suggesting that they are expressed during infection. Taken together, our data could offer valuable information to the understanding of leptospiral pathogenesis. (AU)

FAPESP's process: 12/23913-9 - Indentification and characterization of proteins of Leptospira interrogans involved in host-pathogen interactions
Grantee:Ana Lucia Tabet Oller Do Nascimento
Support type: Regular Research Grants