Role for HtrA in stress induction and virulence potential in Listeria monocytogenes.

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TY  - JOUR
  - Stack HM, Sleator RD, Bowers M, Hill C, Gahan CG
  - 2005
  - August
  - Applied and Environmental Microbiology
  - Role for HtrA in stress induction and virulence potential in Listeria monocytogenes.
  - Validated
  - Altmetric: 1 ()
  - 71
  - 8
  - 4241
  - 4247
  - In silico analysis of the Listeria monocytogenes genome revealed lmo0292, a gene predicted to encode a HtrA-like serine protease. A stable insertion mutant was constructed, revealing a requirement for htrA in the listerial response to heat, acid, and penicillin stress. Transcriptional analysis revealed that htrA is not induced in response to heat shock but is induced in response to low pH and penicillin G stress. Furthermore, htrA expression was shown to be dependent upon the LisRK two-component sensor-kinase, a system known to respond to changes in integrity of the cell envelope. In addition, we demonstrated that a second in-frame start codon, upstream of that previously annotated for L. monocytogenes htrA, incorporating a putative signal sequence appears to influence virulence potential. Finally, a significant virulence defect was observed for the htrA mutant, indicating that this gene is required for full virulence in mice. Our findings suggest that L. monocytogenes lmo0292 encodes an HtrA-like serine protease that is not part of the classical heat shock response but is involved in stress responses and virulence.
  - 10.1128/AEM.71.8.4241-4247.2005
DA  - 2005/08
ER  - 
@article{V14901061,
   = {Stack HM,  Sleator RD and  Bowers M,  Hill C and  Gahan CG },
   = {2005},
   = {August},
   = {Applied and Environmental Microbiology},
   = {Role for HtrA in stress induction and virulence potential in Listeria monocytogenes.},
   = {Validated},
   = {Altmetric: 1 ()},
   = {71},
   = {8},
  pages = {4241--4247},
   = {{In silico analysis of the Listeria monocytogenes genome revealed lmo0292, a gene predicted to encode a HtrA-like serine protease. A stable insertion mutant was constructed, revealing a requirement for htrA in the listerial response to heat, acid, and penicillin stress. Transcriptional analysis revealed that htrA is not induced in response to heat shock but is induced in response to low pH and penicillin G stress. Furthermore, htrA expression was shown to be dependent upon the LisRK two-component sensor-kinase, a system known to respond to changes in integrity of the cell envelope. In addition, we demonstrated that a second in-frame start codon, upstream of that previously annotated for L. monocytogenes htrA, incorporating a putative signal sequence appears to influence virulence potential. Finally, a significant virulence defect was observed for the htrA mutant, indicating that this gene is required for full virulence in mice. Our findings suggest that L. monocytogenes lmo0292 encodes an HtrA-like serine protease that is not part of the classical heat shock response but is involved in stress responses and virulence.}},
   = {10.1128/AEM.71.8.4241-4247.2005},
  source = {IRIS}
}
AUTHORSStack HM, Sleator RD, Bowers M, Hill C, Gahan CG
YEAR2005
MONTHAugust
JOURNAL_CODEApplied and Environmental Microbiology
TITLERole for HtrA in stress induction and virulence potential in Listeria monocytogenes.
STATUSValidated
TIMES_CITEDAltmetric: 1 ()
SEARCH_KEYWORD
VOLUME71
ISSUE8
START_PAGE4241
END_PAGE4247
ABSTRACTIn silico analysis of the Listeria monocytogenes genome revealed lmo0292, a gene predicted to encode a HtrA-like serine protease. A stable insertion mutant was constructed, revealing a requirement for htrA in the listerial response to heat, acid, and penicillin stress. Transcriptional analysis revealed that htrA is not induced in response to heat shock but is induced in response to low pH and penicillin G stress. Furthermore, htrA expression was shown to be dependent upon the LisRK two-component sensor-kinase, a system known to respond to changes in integrity of the cell envelope. In addition, we demonstrated that a second in-frame start codon, upstream of that previously annotated for L. monocytogenes htrA, incorporating a putative signal sequence appears to influence virulence potential. Finally, a significant virulence defect was observed for the htrA mutant, indicating that this gene is required for full virulence in mice. Our findings suggest that L. monocytogenes lmo0292 encodes an HtrA-like serine protease that is not part of the classical heat shock response but is involved in stress responses and virulence.
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URL
DOI_LINK10.1128/AEM.71.8.4241-4247.2005
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