Pathogenic leptospires have the ability to survive and disseminate to multiple organs after penetrating the host. Several pathogens, including spirochetes, have been shown to express surface proteins that interact with the extracellular matrix (ECM). This adhesin-mediated binding process seems to be a crucial step in the colonization of host tissues. This study examined the interaction of leptospiral outer membrane proteins with laminin, collagen Type I, collagen Type IV, cellular fibronectin and plasma fibronectin. Six predicted coding sequences selected from the L. interrogans serovar Copenhageni genome were cloned, proteins expressed, purified by metal affinity chromatography and characterized by circular dichroism spectroscopy. Their capacity to mediate attachment to ECM components was evaluated by binding assays. We have identified a leptospiral surface protein encoded by LIC12906 that binds strongly to laminin. Attachment of LIC12906 encoded protein to laminin was specific, dose-dependent and saturable. Laminin oxidation by sodium metaperiodate reduced protein-laminin interaction in a concentration-dependent manner, indicating that laminin sugar moieties are crucial for this interaction. This newly identified surface protein may play a role in mediating adhesion of L. interrogans to the hosts. To our knowledge, this is the first leptospiral adhesin with laminin-binding properties reported to date.