Journal article

Propeptide-Mediated Inhibition of Cognate Gingipain Proteinases

N Laila Huq, Christine A Seers, Elena CY Toh, Stuart G Dashper, Nada Slakeski, Lianyi Zhang, Brent R Ward, Vincent Meuric, Dina Chen, Keith J Cross, Eric C Reynolds

PLOS ONE | PUBLIC LIBRARY SCIENCE | Published : 2013

Abstract

Porphyromonas gingivalis is a major pathogen associated with chronic periodontitis. The organism's cell-surface cysteine proteinases, the Arg-specific proteinases (RgpA, RgpB) and the Lys-specific proteinase (Kgp), which are known as gingipains have been implicated as major virulence factors. All three gingipain precursors contain a propeptide of around 200 amino acids in length that is removed during maturation. The aim of this study was to characterize the inhibitory potential of the Kgp and RgpB propeptides against the mature cognate enzymes. Mature Kgp was obtained from P. gingivalis mutant ECR368, which produces a recombinant Kgp with an ABM1 motif deleted from the catalytic domain (rKg..

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