Novel Leptospira interrogans protein Lsa32 is expressed during infection and binds laminin and plasminogen.

Autor:	Domingos RF; Centro de Biotecnologia, Instituto Butantan, Avenida Vital Brazil, 1500, 05503-900, São Paulo, SP, Brazil Programa Interunidades em Biotecnologia, Instituto de Ciências Biomédicas, USP, Avenida Professor Lineu Prestes, 1730, 05508-900, São Paulo, SP, Brazil., Fernandes LG; Centro de Biotecnologia, Instituto Butantan, Avenida Vital Brazil, 1500, 05503-900, São Paulo, SP, Brazil Programa Interunidades em Biotecnologia, Instituto de Ciências Biomédicas, USP, Avenida Professor Lineu Prestes, 1730, 05508-900, São Paulo, SP, Brazil., Romero EC; Divisão de Biologia Medica, Instituto Adolfo Lutz, São Paulo, SP, Brazil., de Morais ZM; Laboratório de Zoonoses Bacterianas do VPS, Faculdade de Medicina Veterinária e Zootecnia, USP, Avenida Professor Dr Orlando Marques de Paiva, 87, 05508-270, São Paulo, SP, Brazil., Vasconcellos SA; Laboratório de Zoonoses Bacterianas do VPS, Faculdade de Medicina Veterinária e Zootecnia, USP, Avenida Professor Dr Orlando Marques de Paiva, 87, 05508-270, São Paulo, SP, Brazil., Nascimento AL; Centro de Biotecnologia, Instituto Butantan, Avenida Vital Brazil, 1500, 05503-900, São Paulo, SP, Brazil Programa Interunidades em Biotecnologia, Instituto de Ciências Biomédicas, USP, Avenida Professor Lineu Prestes, 1730, 05508-900, São Paulo, SP, Brazil ana.nascimento@butantan.gov.br.
Jazyk:	angličtina
Zdroj:	Microbiology (Reading, England) [Microbiology (Reading)] 2015 Apr; Vol. 161 (Pt 4), pp. 851-64. Date of Electronic Publication: 2015 Jan 27.
DOI:	10.1099/mic.0.000041
Abstrakt:	Pathogenic Leptospira is the aetiological agent of leptospirosis, a life-threatening disease of human and veterinary concern. The quest for novel antigens that could mediate host-pathogen interactions is being pursued. Owing to their location, these antigens have the potential to elicit numerous activities, including immune response and adhesion. This study focuses on a hypothetical protein of Leptospira, encoded by the gene LIC11089, and its three derived fragments: the N-terminal, intermediate and C terminus regions. The gene coding for the full-length protein and fragments was cloned and expressed in Escherichia coli BL21(SI) strain by using the expression vector pAE. The recombinant protein and fragments tagged with hexahistidine at the N terminus were purified by metal affinity chromatography. The leptospiral full-length protein, named Lsa32 (leptospiral surface adhesin, 32 kDa), adheres to laminin, with the C terminus region being responsible for this interaction. Lsa32 binds to plasminogen in a dose-dependent fashion, generating plasmin when an activator is provided. Moreover, antibodies present in leptospirosis serum samples were able to recognize Lsa32. Lsa32 is most likely a new surface protein of Leptospira, as revealed by proteinase K susceptibility. Altogether, our data suggest that this multifaceted protein is expressed during infection and may play a role in host-L. interrogans interactions. (© 2015 The Authors.)
Databáze:	MEDLINE
Externí odkaz:	Zobrazit plný text záznamu