Journal article

Reversible redox regulation of specificityof Arg-gingipain B in Porphyromonas gingivalis

Yu-Yen Chen, Christine A Seers, Nada Slakeski, Caroline Moore, Lianyi Zhang, Eric C Reynolds

FEBS LETTERS | ELSEVIER SCIENCE BV | Published : 2013

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.