Open Access Research article

“Features of two proteins of Leptospira interrogans with potential role in host-pathogen interactions”

Renan F Domingos12, Monica L Vieira12, Eliete C Romero3, Amane Paldes Gonçales4, Zenaide M de Morais4, Silvio A Vasconcellos4 and Ana L T O Nascimento12*

Author Affiliations

1 Centro de Biotecnologia, Instituto Butantan, Avenida Vital Brazil, 1500, 05503-900, São Paulo, SP, Brazil

2 Pós-Graduação Interunidades em Biotecnologia, Instituto de Ciências Biomédicas, USP, Avenida Prof. Lineu Prestes, 1730, 05508-900, São Paulo, SP, Brazil

3 Centro de Bacteriologia, Instituto Adolfo Lutz, Avenida Dr. Arnaldo, 355, CEP 01246-902, Sao Paulo, Brazil

4 Laboratório de Zoonoses Bacterianas do VPS, Faculdade de Medicina Veterinária e Zootecnia, USP, Avenida Prof. Dr. Orlando Marques de Paiva, 87, 05508-270, São Paulo, SP, Brazil

For all author emails, please log on.

BMC Microbiology 2012, 12:50  doi:10.1186/1471-2180-12-50

Published: 30 March 2012



Leptospirosis is considered a re-emerging infectious disease caused by pathogenic spirochaetes of the genus Leptospira. Pathogenic leptospires have the ability to survive and disseminate to multiple organs after penetrating the host. Leptospires were shown to express surface proteins that interact with the extracellular matrix (ECM) and to plasminogen (PLG). This study examined the interaction of two putative leptospiral proteins with laminin, collagen Type I, collagen Type IV, cellular fibronectin, plasma fibronectin, PLG, factor H and C4bp.


We show that two leptospiral proteins encoded by LIC11834 and LIC12253 genes interact with laminin in a dose - dependent and saturable mode, with dissociation equilibrium constants (KD) of 367.5 and 415.4 nM, respectively. These proteins were named Lsa33 and Lsa25 (Leptospiral surface adhesin) for LIC11834 and LIC12253, respectively. Metaperiodate - treated laminin reduced Lsa25 - laminin interaction, suggesting that sugar moieties of this ligand participate in this interaction. The Lsa33 is also PLG - binding receptor, with a KD of 23.53 nM, capable of generating plasmin in the presence of an activator. Although in a weak manner, both proteins interact with C4bp, a regulator of complement classical route. In silico analysis together with proteinase K and immunoflorescence data suggest that these proteins might be surface exposed. Moreover, the recombinant proteins partially inhibited leptospiral adherence to immobilized laminin and PLG.


We believe that these multifunctional proteins have the potential to participate in the interaction of leptospires to hosts by mediating adhesion and by helping the bacteria to escape the immune system and to overcome tissue barriers. To our knowledge, Lsa33 is the first leptospiral protein described to date with the capability of binding laminin, PLG and C4bp in vitro.