title: The roles of RgpB and Kgp in late onset gingipain activity in the vimA-defective mutant of Porphyromonas gingivalis W83.
abstract: Previous studies have shown that VimA, an acetyltransferase, can modulate gingipain biogenesis in Porphyromonas gingivalis. Inactivation of the vimA gene resulted in isogenic mutants that showed a late onset of gingipain activity that only occurred during the stationary growth phase. To further elucidate the role and contribution of the gingipains in this VimA-dependent process, isogenic mutants defective in the gingipain genes in the vimA-deficient genetic background were evaluated. In contrast with the wild-type strain, RgpB and Kgp gingipain activities were absent in exponential phase in the ∆rgpA::tetQ-vimA::ermF mutant. However, these activities increased to 31 and 53%, respectively, of that of the wild-type during stationary phase. In the ∆rgpA::cat-∆kgp::tetQ-vimA::ermF mutant, the RgpB protein was observed in the extracellular fraction but no activity was present even at the stationary growth phase. There was no gingipain activity observed in the ∆rgpB::cat-∆kgp::tetQ-vimA::ermF mutant whereas Kgp activity in ∆rgpA::cat-∆rgpB::tetQ-vimA::ermF mutant was 24% of the wild-type at late stationary phase. In contrast to RgpA, the glycosylation profile of the RgpB catalytic domain from both W83 and P. gingivalis FLL92 (vimA::ermF) showed similarity. Taken together, the results suggest multiple gingipain activation pathways in P. gingivalis. Whereas the maturation pathways for RgpA and RgpB are different, the late-onset gingipain activity in the vimA-defective mutant was due to activation/maturation of RgpB and Kgp. Moreover, unlike RgpA, which is VimA-dependent, the maturation/activation pathways for RgpB and Kgp are interdependent in the absence VimA.
authors: Division of Microbiology and Molecular Genetics, School of Medicine, Loma Linda University, Loma Linda, CA, USA.
authors: Y
authors: Y
authors: Dou
authors: Division of Microbiology and Molecular Genetics, School of Medicine, Loma Linda University, Loma Linda, CA, USA.
authors: A
authors: A
authors: Robles
authors: Division of Microbiology and Molecular Genetics, School of Medicine, Loma Linda University, Loma Linda, CA, USA.
authors: F
authors: F
authors: Roy
authors: Division of Microbiology and Molecular Genetics, School of Medicine, Loma Linda University, Loma Linda, CA, USA.
authors: A W
authors: AW
authors: Aruni
authors: Division of Microbiology and Molecular Genetics, School of Medicine, Loma Linda University, Loma Linda, CA, USA.
authors: L
authors: L
authors: Sandberg
authors: Botany and Plant Sciences, University of California, Riverside, CA, USA.
authors: E
authors: E
authors: Nothnagel
authors: Division of Microbiology and Molecular Genetics, School of Medicine, Loma Linda University, Loma Linda, CA, USA.|Institute of Oral Biology, Kyung Hee University, Seoul, Korea.
authors: H M
authors: HM
authors: Fletcher
mesh_terms: D000123:Acetyltransferases / Q000235:genetics* / Q000378:metabolism; D018829:Adhesins, Bacterial / Q000302:isolation & purification / Q000378:metabolism*; D000818:Animals; D002415:Cats; D003546:Cysteine Endopeptidases / Q000302:isolation & purification / Q000378:metabolism*; D005798:Genes, Bacterial; D000080867:Gingipain Cysteine Endopeptidases; D006031:Glycosylation; D006388:Hemagglutinins / Q000378:metabolism; D009154:Mutation; D016966:Porphyromonas gingivalis / Q000235:genetics* / Q000254:growth & development / Q000378:metabolism*
chemical_list: D018829:Adhesins, Bacterial; D000080867:Gingipain Cysteine Endopeptidases; D006388:Hemagglutinins; D000123:Acetyltransferases; D003546:Cysteine Endopeptidases
keywords: VimA; acetylation; gingipain; glycosylation; periodontal disease