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

Leptospira interrogans Secreted Proteases Degrade Extracellular Matrix and Plasma Proteins From the Host

Full text
Show less -
da Silva, Ludmila B. [1] ; Menezes, Milene C. [2] ; Kitano, Eduardo S. [2] ; Oliveira, Ana K. [3] ; Abreu, Afonso G. [4, 5] ; Souza, Gisele O. [6] ; Heinemann, Marcos B. [6] ; Isaac, Lourdes [7] ; Fraga, Tatiana R. [7] ; Serrano, Solange M. T. [2] ; Barbosa, Angela S. [1]
Total Authors: 11
[1] Butantan Inst, Lab Bacteriol, Sao Paulo - Brazil
[2] Butantan Inst, Ctr Toxins Immune Response & Cell Signaling, Special Lab Appl Toxinol, Sao Paulo - Brazil
[3] Brazilian Ctr Res Energy & Mat, Brazilian Biosci Natl Lab, Campinas, SP - Brazil
[4] CEUMA Univ, Postgrad Program Parasit Biol, Sao Luis - Brazil
[5] Univ Fed Maranhao, Postgrad Program Hlth Sci, Sao Luis - Brazil
[6] Univ Sao Paulo, Sch Vet Med & Anim Sci, Dept Prevent Vet Med & Anim Hlth, Sao Paulo - Brazil
[7] Univ Sao Paulo, Inst Biomed Sci, Dept Immunol, Sao Paulo - Brazil
Total Affiliations: 7
Document type: Journal article
Web of Science Citations: 1

Leptospires are highly motile spirochetes equipped with strategies for efficient invasion and dissemination within the host. Our group previously demonstrated that pathogenic leptospires secrete proteases capable of cleaving and inactivating key molecules of the complement system, allowing these bacteria to circumvent host's innate immune defense mechanisms. Given the successful dissemination of leptospires during infection, we wondered if such proteases would target a broader range of host molecules. In the present study, the proteolytic activity of secreted leptospiral proteases against a panel of extracellular matrix (ECM) and plasma proteins was assessed. The culture supernatant of the virulent L. interrogans serovar Kennewicki strain Fromm (LPF) degraded human fibrinogen, plasma fibronectin, gelatin, and the proteoglycans decorin, biglycan, and lumican. Interestingly, human plasminogen was not cleaved by proteases present in the supernatants. Proteolytic activity was inhibited by 1,10-phenanthroline, suggesting the participation of metalloproteases. Moreover, production of proteases might be an important virulence determinant since culture-attenuated or saprophytic Leptospira did not display proteolytic activity against ECM or plasma components. Exoproteomic analysis allowed the identification of three metalloproteases that could be involved in the degradation of host components. The ability to cleave conjunctive tissue molecules and coagulation cascade proteins may certainly contribute to invasion and tissue destruction observed upon infection with Leptospira. (AU)

FAPESP's process: 13/17419-4 - Identification of Leptospira proteases involved in the degradation of extracellular matrix proteins
Grantee:Ludmila Bezerra da Silva
Support type: Scholarships in Brazil - Doctorate
FAPESP's process: 14/00926-3 - Leptospira-host interaction: aspects related to tissue invasion and innate immune system evasion
Grantee:Angela Silva Barbosa
Support type: Regular Research Grants