Reversible redox regulation of specificity of Arg-gingipain B in Porphyromonas gingivalis.
FEBS Lett
; 587(9): 1275-80, 2013 May 02.
Article
em En
| MEDLINE
| ID: mdl-23499434
ABSTRACT
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.
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Base de dados:
MEDLINE
Assunto principal:
Cisteína Endopeptidases
/
Porphyromonas gingivalis
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Adesinas Bacterianas
Idioma:
En
Ano de publicação:
2013
Tipo de documento:
Article