TY - JOUR
T1 - regT can modulate gingipain activity and response to oxidative stress in Porphyromonas gingivalis
AU - Vanterpool, E.
AU - Wilson Aruni, A.
AU - Roy, F.
AU - Fletcher, H. M.
N1 - Recombinant VimA protein can interact with the gingipains and several other proteins that may play a role in its biogenesis in Porphyromonas gingivalis. In silico analysis of PG2096, a hypothetical protein that was shown to interact with VimA, suggests ...
PY - 2010/10
Y1 - 2010/10
N2 - Recombinant VimA protein can interact with the gingipains and several other proteins that may play a role in its biogenesis in Porphyromonas gingivalis. In silico analysis of PG2096, a hypothetical protein that was shown to interact with VimA, suggests that it may have environmental stress resistance properties. To further evaluate the role(s) of PG2096, the predicted open reading frame was PCR amplified from P. gingivalis W83 and insertionally inactivated using the ermF-ermAM antibiotic-resistance cassette. One randomly chosen PG2096-defective mutant created by allelic exchange and designated FLL205 was further characterized. Under normal growth conditions at 37°C, Arg-X and Lys-X gingipain activities in FLL205 were reduced by approximately 35% and 21 %, respectively, compared to the wild-type strain. However, during prolonged growth at an elevated temperature of 42°C, Arg-X activity was increased by more than 40% in FLL205 in comparison to the wild-type strain. In addition, the PG2096-defective mutant was more resistant to oxidative stress when treated with 0.25 mM hydrogen peroxide. Taken together these results suggest that the PG2096 gene, designated regT (regulator of gingipain activity at elevated temperatures), may be involved in regulating gingipain activity at elevated temperatures and be important in oxidative stress resistance in P. gingivalis. © 2010 SGM.
AB - Recombinant VimA protein can interact with the gingipains and several other proteins that may play a role in its biogenesis in Porphyromonas gingivalis. In silico analysis of PG2096, a hypothetical protein that was shown to interact with VimA, suggests that it may have environmental stress resistance properties. To further evaluate the role(s) of PG2096, the predicted open reading frame was PCR amplified from P. gingivalis W83 and insertionally inactivated using the ermF-ermAM antibiotic-resistance cassette. One randomly chosen PG2096-defective mutant created by allelic exchange and designated FLL205 was further characterized. Under normal growth conditions at 37°C, Arg-X and Lys-X gingipain activities in FLL205 were reduced by approximately 35% and 21 %, respectively, compared to the wild-type strain. However, during prolonged growth at an elevated temperature of 42°C, Arg-X activity was increased by more than 40% in FLL205 in comparison to the wild-type strain. In addition, the PG2096-defective mutant was more resistant to oxidative stress when treated with 0.25 mM hydrogen peroxide. Taken together these results suggest that the PG2096 gene, designated regT (regulator of gingipain activity at elevated temperatures), may be involved in regulating gingipain activity at elevated temperatures and be important in oxidative stress resistance in P. gingivalis. © 2010 SGM.
KW - Gingipain Cysteine Endopeptidases
KW - Amino Acid Sequence
KW - Sequence Alignment
KW - Oxidative Stress
KW - Molecular Sequence Data
KW - Adhesins, Bacterial/genetics
KW - Mutagenesis, Insertional
KW - Hot Temperature
KW - Mutation
KW - Peptide Hydrolases/metabolism
KW - Cysteine Endopeptidases/genetics
KW - Porphyromonas gingivalis/genetics
UR - https://www.scopus.com/pages/publications/77957870729
UR - https://www.scopus.com/pages/publications/77957870729#tab=citedBy
UR - https://www.mendeley.com/catalogue/ce47a2ad-490f-3e35-b64d-fecd3270d2bb/
U2 - 10.1099/mic.0.038315-0
DO - 10.1099/mic.0.038315-0
M3 - Article
C2 - 20595264
SN - 1350-0872
VL - 156
SP - 3065
EP - 3072
JO - Microbiology
JF - Microbiology
IS - 10
ER -