Reversible redox regulation of specificity of Arg-gingipain B in Porphyromonas gingivalis.
FEBS Lett
; 587(9): 1275-80, 2013 May 02.
Article
en En
| MEDLINE
| ID: mdl-23499434
Arg-gingipain B (RgpB), a major virulence factor secreted by the periodontal pathogen Porphyromonas gingivalis is an Arg-specific cysteine proteinase. By monitoring proteolytic cleavage of a human salivary peptide histatin 5 using MALDI-TOF MS, RgpB purified from P. gingivalis HG66 was found to shift from a dominant Arg-X to dominant Lys-X activity, both in vitro and in vivo, upon reversible cysteine oxidation. Native PAGE analysis revealed the association of novel Lys-X activity with a reversible state change of the oxidized enzyme. The redox-regulated Lys-X activity of RgpB may provide a survival advantage to P. gingivalis against the oxidative host defence.
Texto completo:
1
Colección:
01-internacional
Base de datos:
MEDLINE
Asunto principal:
Cisteína Endopeptidasas
/
Porphyromonas gingivalis
/
Adhesinas Bacterianas
Tipo de estudio:
Prognostic_studies
Límite:
Humans
Idioma:
En
Revista:
FEBS Lett
Año:
2013
Tipo del documento:
Article
País de afiliación:
Australia
Pais de publicación:
Reino Unido