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

Leptospiral Immunoglobulin-like Proteins Interact With Human Complement Regulators Factor H, FHL-1, FHR-1, and C4BP

Full text
Author(s):
Castiblanco-Valencia, Monica Marcela [1] ; Fraga, Tatiana Rodrigues [1] ; da Silva, Ludmila Bezerra [2] ; Monaris, Denize [2] ; Estima Abreu, Patricia Antonia [2] ; Strobel, Stefanie [3] ; Jozsi, Mihaly [3] ; Isaac, Lourdes [1] ; Barbosa, Angela Silva [2]
Total Authors: 9
Affiliation:
[1] Univ Sao Paulo, Dept Imunol, Inst Ciencias Biomed, BR-05508900 Sao Paulo - Brazil
[2] Butantan Inst, Bacteriol Lab, Sao Paulo - Brazil
[3] Hans Knoell Inst, Leibniz Inst Nat Prod Res & Infect Biol, Jr Res Grp Cellular Immunobiol, Jena - Germany
Total Affiliations: 3
Document type: Journal article
Source: Journal of Infectious Diseases; v. 205, n. 6, p. 995-1004, MAR 15 2012.
Web of Science Citations: 68
Abstract

Leptospira, the causative agent of leptospirosis, interacts with several host molecules, including extracellular matrix components, coagulation cascade proteins, and human complement regulators. Here we demonstrate that acquisition of factor H (FH) on the Leptospira surface is crucial for bacterial survival in the serum and that these spirochetes, besides interacting with FH, FH related-1, and C4b binding protein (C4BP), also acquire FH like-1 from human serum. We also demonstrate that binding to these complement regulators is mediated by leptospiral immunoglobulin-like (Lig) proteins, previously shown to interact with fibronectin, laminin, collagen, elastin, tropoelastin, and fibrinogen. Factor H binds to Lig proteins via short consensus repeat domains 5 and 20. Competition assays suggest that FH and C4BP have distinct binding sites on Lig proteins. Moreover, FH and C4BP bound to immobilized Ligs display cofactor activity, mediating C3b and C4b degradation by factor I. In conclusion, Lig proteins are multifunctional molecules, contributing to leptospiral adhesion and immune evasion. (AU)

FAPESP's process: 10/50043-0 - Complement system and pathogenicity of Leptospires: mechanisms of activation and evasion, identification of bacterial ligands, characterization of proteases and establishment of an in vivo murine model
Grantee:Lourdes Isaac
Support Opportunities: Research Projects - Thematic Grants