title: Characterization of three novel adhesins of Leptospira interrogans.
abstract: We report cloning, expression, purification, and characterization of three predicted leptospiral membrane proteins (LIC11360, LIC11009, and LIC11975). In silico analysis and proteinase K accessibility data suggest that these proteins might be surface exposed. We show that proteins encoded by LIC11360, LIC11009 and LIC11975 genes interact with laminin in a dose-dependent and saturable manner. The proteins are referred to as leptospiral surface adhesions 23, 26, and 36 (Lsa23, Lsa26, and Lsa36), respectively. These proteins also bind plasminogen and generate active plasmin. Attachment of Lsa23 and Lsa36 to fibronectin occurs through the involvement of the 30-kDa and 70-kDa heparin-binding domains of the ligand. Dose-dependent, specific-binding of Lsa23 to the complement regulator C4BP and to a lesser extent, to factor H, suggests that this protein may interfere with the complement cascade pathways. Leptospira spp. may use these interactions as possible mechanisms during the establishment of infection.
authors: Centro de Biotecnologia, Instituto Butantan, São Paulo, Brazil; Programa de Pós-Graduação Interunidades em Biotecnologia, Instituto de Ciências Biomédicas, e Laboratório de Zoonoses Bacterianas do Veterinária Preventiva e Saúde Animal, Faculdade de Medicina Veterinária e Zootecnia, Universidade de São Paulo, São Paulo, Brazil.
authors: Gabriela H
authors: GH
authors: Siqueira
authors: Marina V
authors: MV
authors: Atzingen
authors: Ivy J
authors: IJ
authors: Alves
authors: Zenaide M
authors: ZM
authors: de Morais
authors: Silvio A
authors: SA
authors: Vasconcellos
authors: Ana L T O
authors: AL
authors: Nascimento
mesh_terms: D018829:Adhesins, Bacterial / Q000235:genetics / Q000302:isolation & purification / Q000378:metabolism*; D000818:Animals; D003001:Cloning, Molecular; D050716:Complement C4b-Binding Protein / Q000378:metabolism; D019295:Computational Biology; D004305:Dose-Response Relationship, Drug; D005260:Female; D005341:Fibrinolysin / Q000378:metabolism; D005353:Fibronectins / Q000378:metabolism; D006801:Humans; D007797:Laminin / Q000378:metabolism; D007919:Leptospira / Q000235:genetics / Q000378:metabolism; D007921:Leptospira interrogans / Q000235:genetics / Q000378:metabolism*; D007922:Leptospirosis / Q000382:microbiology*; D008239:Lysine / Q000378:metabolism; D051379:Mice; D008807:Mice, Inbred BALB C; D010802:Phylogeny; D010958:Plasminogen / Q000378:metabolism; D011485:Protein Binding; D051381:Rats; D011994:Recombinant Proteins / Q000235:genetics / Q000378:metabolism; D016415:Sequence Alignment
chemical_list: D018829:Adhesins, Bacterial; C055609:C4BPA protein, human; D050716:Complement C4b-Binding Protein; D005353:Fibronectins; D007797:Laminin; D011994:Recombinant Proteins; D010958:Plasminogen; D005341:Fibrinolysin; D008239:Lysine
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