Novel Leptospira interrogans protein Lsa32 is expressed during infection and binds laminin and plasminogen.
Microbiology (Reading)
; 161(Pt 4): 851-64, 2015 Apr.
Article
en En
| MEDLINE
| ID: mdl-25627443
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.
Texto completo:
1
Banco de datos:
MEDLINE
Asunto principal:
Plasminógeno
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Proteínas Bacterianas
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Regulación Bacteriana de la Expresión Génica
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Laminina
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Leptospira interrogans
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Leptospirosis
Idioma:
En
Revista:
Microbiology (Reading)
Asunto de la revista:
MICROBIOLOGIA
Año:
2015
Tipo del documento:
Article
País de afiliación:
Brasil