The
 vimE
 Gene Downstream of
 vimA
 Is Independently Expressed and Is Involved in Modulating Proteolytic Activity in
 Porphyromonas gingivalis
 W83

Vanterpool, Elaine; Roy, Frans van; Fletcher, HM

doi:10.1128/iai.72.12.7380.2004

Cited by 20 publications

(51 citation statements)

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“…While a reduction in Arg-X-and Lys-X-specific proteolytic activities was observed in P. gingivalis FLL92, transcription of the gingipain genes was unaltered in these mutants compared to that of the wild-type strain (Abaibou et al, 2001). A similar phenotype of the gingipain genes was also seen in P. gingivalis FLL32, a recA-and vimE-defective isogenic mutant that had reduced Arg-X-and Lys-X-specific proteolytic activities (Abaibou et al, 2000;Vanterpool et al, 2004). While there was a unique late onset of Arg-X-and Lys-X-specific proteolytic activity in P. gingivalis FLL92, there was little or no observed change of proteolytic activity in stationary-phase in P. gingivalis FLL93, a vimE-defective mutant (Vanterpool et al, 2004).…”

Section: Introductionmentioning

confidence: 49%

“…A similar phenotype of the gingipain genes was also seen in P. gingivalis FLL32, a recA-and vimE-defective isogenic mutant that had reduced Arg-X-and Lys-X-specific proteolytic activities (Abaibou et al, 2000;Vanterpool et al, 2004). While there was a unique late onset of Arg-X-and Lys-X-specific proteolytic activity in P. gingivalis FLL92, there was little or no observed change of proteolytic activity in stationary-phase in P. gingivalis FLL93, a vimE-defective mutant (Vanterpool et al, 2004). Collectively, these observations have raised the question whether the regulation of proteolytic activity in P. gingivalis may occur by multiple mechanisms.…”

Section: Introductionmentioning

confidence: 75%

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VimA is part of the maturation pathway for the major gingipains of Porphyromonas gingivalis W83

et al. 2006

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The authors have shown previously that the vimA gene, which is part of the bcp-recA-vimA operon, plays an important role in protease activation in Porphyromonas gingivalis. The gingipain RgpB proenzyme is secreted in the vimA-defective mutant P. gingivalis FLL92. An important question that is raised is whether the vimA gene product could directly interact with the proteases for their activation or regulate a pathway responsible for protease activation. To further study the mechanism(s) of VimA-dependent protease activation, the vimA gene product was further characterized. A 39 kDa protein consistent with the size of the predicted VimA protein was purified. In protein–protein interaction studies, the VimA protein was shown to interact with gingipains RgpA, RgpB and Kgp. Immune sera from mice immunized with P. gingivalis immunoreacted with the purified VimA protein. Taken together, these data suggest an interaction of VimA with the gingipains and further confirm the role of this protein in their regulation or maturation.

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Section: Introductionmentioning

confidence: 49%

Section: Introductionmentioning

confidence: 75%

VimA is part of the maturation pathway for the major gingipains of Porphyromonas gingivalis W83

et al. 2006

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“…Plasmid and P. gingivalis chromosomal DNA preparations and analyses were performed as previously described (Vanterpool et al, 2004). For large-scale preparation, plasmids were purified using a Qiagen plasmid maxi kit.…”

Section: Methodsmentioning

confidence: 99%

Role of the Porphyromonas gingivalis iron-binding protein PG1777 in oxidative stress resistance

et al. 2016

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Whole genome sequencing of the response of Porphyromonas gingivalis W83 to hydrogen peroxide revealed an upregulation of several uncharacterized, novel genes. Under conditions of prolonged oxidative stress in P. gingivalis, increased expression of a unique transcriptional unit carrying the grpE, dnaJ and three other hypothetical genes (PG1777, PG1778 and PG1779) was observed. The transcriptional start site of this operon appears to be located 91 bp upstream of the translational start, with a potential 210 region at 23 nt and a 235 region at 239 nt. Isogenic P. gingivalis mutants FLL273 (PG1777 : : ermF-ermAM) and FLL293 (PG1779 : : ermF-ermAM) showed increased sensitivity to and decreased survival after treatment with hydrogen peroxide. P. gingivalis FLL273 showed a fivefold increase in the formation of spontaneous mutants when compared with the parent strain after exposure to hydrogen peroxide. The recombinant PG1777 protein displayed iron-binding properties when incubated with FeSO 4 and Fe(NH 4 ) 2 (SO 4 ).6H 2 O. The rPG1777 protein protected DNA from degradation when exposed to hydrogen peroxide in the presence of iron. Taken together, the data suggest that the grpE-dnaJ-PG1777-PG1778-PG1779 transcriptional unit may play an important role in oxidative stress resistance in P. gingivalis via its ability to protect against DNA damage.

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“…The amplified fragment was inserted into the MscI restriction site of the htrA gene. The resultant recombinant plasmid, pFLL202, was used as a donor in electroporation of P. gingivalis W83 as previously reported (Vanterpool et al, 2004).…”

Section: Introductionmentioning

confidence: 99%

“…P. gingivalis chromosomal DNA was isolated as previously reported (Vanterpool et al, 2004). For plasmid DNA analysis, DNA extraction was performed by the alkaline lysis procedure as previously described (Johnson et al, 2004).…”

Section: Introductionmentioning

confidence: 99%

HtrA in Porphyromonas gingivalis can regulate growth and gingipain activity under stressful environmental conditions

2006

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In several micro-organisms, HtrA, a serine periplasmic protease, is considered an important virulence factor that plays a regulatory role in oxidative and temperature stress. The authors have previously shown that the vimA gene product is an important virulence regulator in Porphyromonas gingivalis. Further, purified recombinant VimA physically interacted with the major gingipains and the HtrA from P. gingivalis. To further evaluate a role for HtrA in the pathogenicity of this organism, a 1.5 kb fragment containing the htrA gene was PCR-amplified from the chromosomal DNA of P. gingivalis W83. This gene was insertionally inactivated using the ermF-ermAM antibiotic-resistance cassette and used to create an htrA-deficient mutant by allelic exchange. In one randomly chosen isogenic mutant designated P. gingivalis FLL203, there was increased sensitivity to hydrogen peroxide. Growth of this mutant at an elevated temperature was more inhibited compared to the wild-type. Further, in contrast to the wild-type, there was a significant decrease in Arg-gingipain activity after heat shock in FLL203. However, the gingipain activity in the mutant returned to normal levels after a further 30 min incubation at room temperature. Collectively, these data suggest that HtrA may play a similar role in oxidative and temperature stress in P. gingivalis as observed in other organisms.

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The vimE Gene Downstream of vimA Is Independently Expressed and Is Involved in Modulating Proteolytic Activity in Porphyromonas gingivalis W83

Cited by 20 publications

References 0 publications

VimA is part of the maturation pathway for the major gingipains of Porphyromonas gingivalis W83

VimA is part of the maturation pathway for the major gingipains of Porphyromonas gingivalis W83

Role of the Porphyromonas gingivalis iron-binding protein PG1777 in oxidative stress resistance

HtrA in Porphyromonas gingivalis can regulate growth and gingipain activity under stressful environmental conditions

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