Artículos de revistas
A novel identified protein of Leptospira interrogans mediates binding to laminin
Fecha
2009Registro en:
Journal of Medical Microbiology, Edinburgh, v. 58, n. 10, p. 1275-1282, 2009
0022-2615
Autor
LONGHI, M. T
OLIVEIRA, Tatiane Rodrigues de
ROMERO, Eliete Caló
GONÇALVES, Amane Paldês
MORAIS, Zenaide Maria de
VASCONCELLOS, Silvio Arruda
NASCIMENTO, Ana Lúcia Tabet Oller do
Institución
Resumen
Pathogenic Leptospira is the etiological agent of leptospirosis, a life-threatening disease that affects populations worldwide. The search for novel antigens that could be relevant in host-pathogen interactions is been pursued. These antigens have the potential to elicit several activities, including adhesion. This study focuses on a hypothetical, predicted to be lipoprotein of Leptospira, encoded by the gene LIC12895 to mediate attachment to extracellular matrix (ECM) components. The gene was cloned and expressed in Escherichia coli BL21 Star (DE3) pLys strain by using the expression vector pAE. The recombinant protein tagged with N-terminal hexahistidine was purified by metal-charged chromatography and characterized by circular dichroism spectroscopy. The capacity of the protein to mediate attachment to ECM components was evaluated by binding assays. The leptospiral protein encoded by LIC12895, named Lsa27 (Leptospiral surface adhesin, 27 kDa), binds strongly to laminin in a dose-dependent and saturable fashion. Moreover, the Lsa27 was recognized by antibodies of serum samples of confirmed leptospirosis specimens in both initial and convalescent phases of the disease. The Lsa27 is most likely a new surface protein of Leptospira as revealed in liquid-phase immunofluorescence assays with living organisms. Taken together our date indicated that this novel identified membrane protein is expressed during natural infection and may play a role in mediating adhesion of L. interrogans to the hosts