Leptospira interrogans shotgun phage display identified LigB as a heparin-binding protein.
Biochem Biophys Res Commun
; 427(4): 774-9, 2012 Nov 02.
Article
em En
| MEDLINE
| ID: mdl-23044419
LigB is an adhesin from pathogenic Leptospira that is able to bind to extracellular matrix and is considered a virulence factor. A shotgun phage display genomic library was constructed and used for panning against Heparan Sulfate Proteoglycan (HSPG). A phage clone encoding part of LigB protein was selected in panning experiments and showed specific binding to heparin. To validate the selected clone, fragments of LigB were produced as recombinant proteins and showed affinity to heparin and to mammalian cells. Heparin was also able to reduce the binding of rLB-Ct to mammalian cells. Our data suggests that the glycosaminoglycan moiety of the HSPG is responsible for its binding and could mediate the attachment of the recombinant protein rLB-Ct. Thus, heparin may act as a receptor for Leptospira to colonize and to invade the host tissue.
Texto completo:
1
Base de dados:
MEDLINE
Assunto principal:
Vacinas Bacterianas
/
Proteínas Sanguíneas
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Proteínas de Transporte
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Adesinas Bacterianas
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Peptídeos Catiônicos Antimicrobianos
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Leptospira interrogans
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Leptospirose
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Antígenos de Bactérias
Tipo de estudo:
Prognostic_studies
Limite:
Animals
Idioma:
En
Revista:
Biochem Biophys Res Commun
Ano de publicação:
2012
Tipo de documento:
Article
País de afiliação:
Brasil