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FAZOLO, D. L. Study of the interaction of probable outer membrane lipoprotein of Leptospira with host proteins. 2014. 79 p. Masters thesis (Biotechnology) – Instituto de Ciências Biomédicas, Universidade de São Paulo, São Paulo, 2014. Leptospirosis is a worldwide zoonosis caused by pathogenic spirochetes of the genus Leptospira that colonize the renal tubules of wild and domestic animals and are excreted in the environment by their urine. The transmission occurs through contact with water, food and soil contaminated with urine, mainly from rodents. The mechanisms by which leptospires colonize the host and cause the disease are not fully understood. The identification of proteins that mediate interactions with the host during infection is essential for the understanding of the pathogenesis of leptospirosis and the development of efficient diagnostic tests and vaccines. The aim of this work was to study the interaction of six leptospiral probable outermembrane lipoproteins with host proteins: collagen I, collagen IV, elastin, fibrinogen, cellular fibronectin, plasma fibronectin, laminin, and plasminogen. The recombinant proteins were expressed in the soluble fraction (Lp25, Lp21 and Lp22) and insoluble fraction (Lp11, Lsa30 and Lp35) obtained from total lysates of induced E. coli, they were purified by nickel affinity chromatography, and subsequently analyzed by SDS-PAGE. The binding assay and doseresponse curves with recombinant and host proteins were performed by ELISA. Genomic DNA from some species of pathogenic and non-pathogenic Leptospira were isolated and digested with the restriction enzyme EcoRV, and the gene conservation study were performed by southern blot. Each purified recombinant protein showed a majority band with expected molecular weight. The high titers of polyclonal antibodies against recombinant proteins were produced in Balb/c mice. The binding experiments demonstrated that the recombinant proteins showed interaction with host components in a dose-dependent manner were Lp21, Lsa30 and Lp22. These proteins adhered to plasma fibronectin and laminin, in addition to these components, Lp21 and Lp22 interacted with plasminogen, Lp22 and Lsa30 interacted with collagen IV. The Lp22 also adhered to elastin and fibrinogen. The genes encoding the probable lipoproteins were found only in pathogenic Leptospira. These results demonstrated that these proteins may contribute in the adhesion to host tissues, which constitutes the essential initial event in the pathogenesis of Leptospira. Moreover, these proteins may also be candidates for vaccine antigens since they are present in the L. interrogans serovars, which are the most prevalent cause of human leptospirosis.

Estudo da interação de prováveis lipoproteínas de membrana externa de Leptospira com proteínas do hospedeiro.