Leptospiral binding proteins to C4bp,

factor H and factor H – like have also been identified in Leptospira[9, 31, 32]. Interaction of C4bp and of factor H with other pathogens has been described, including the spirochetes Borrelia spp. [33, 37–41]. The capacity of the leptospires ISRIB manufacturer to adhere to extracellular matrix components has been reported and to date, several leptospiral adhesins have been identified. These include 36 – kDa fibronectin – binding protein [42], LfhA/Lsa24 [6, 31], LigA and LigB proteins [7, 8], Len-family proteins [9], Lsa21 [10], LipL32 [12, 43], Lsa27 [13], Lp95 [11], TlyC [14], selleck chemicals llc LipL53 [44], Lsa63 [15], OmpL37 [45], Lsa66 [17] and Lsa20 [18]. We have reported that Leptospira species were also capable to bind PLG and generating plasmin, in the presence of host activator, on the outer surface in vitro[19]. In addition, we have described that plasmin – coated virulent L.interrogans bacteria were capable to degrade purified extracellular matrix components fibronectin [19] and laminin (Vieira et al., unpublished data), a step that SAHA nmr may contribute for dissemination of the bacteria through the host tissues. More recently, we have shown that plasmin generation on the bacterial surface decreases the deposition of C3b and IgG and

hence, opsonization and phagocytosis, a process that could facilitate leptospires to evade the immune system [22]. Several PLG-receptor proteins in Leptospira have been identified [17, 18, 20, 21]. By data mining the genome sequences of L. interrogans, searching for surface

exposed proteins that could mediate host – pathogen interactions, we have identified two proteins annotated as Leptospira conserved hypothetical, one of them, predicted to be a novel lipoprotein, LIC11834, and the other, LIC12253, has recently been shown to be non-protective in leptospiral challenge assay [46]. Both selected Casein kinase 1 coding sequences were cloned and the recombinant proteins expressed in E. coli. We report that these proteins, Lsa33 and Lsa25, are laminin – binding adhesins and in the case of Lsa33, capable to bind PLG generating enzymatically active plasmin. Although weak, both proteins showed the ability to bind human purified C4bp, suggesting that these proteins have the potential to participate in leptospiral immune evasion by interfering with the complement classical pathway. Due to the high degree of antigenic variation among leptospires, we examined the gene/protein conservation among important species of Leptospira. The LIC11834 and LIC12253 genes are conserved in five serovars of L. interrogans and in other species tested but in the case of L. santarosai serovar Shermani the gene LIC11834 is absent. However, LIC11834 transcripts were detected only in serovars of L. interrogans, while LIC12253 appears to be expressed in all strains evaluated. None of the proteins seems to be expressed in the saprophytic strain, L. biflexa serovar Patoc.