scholarly journals Role of ςB in Adaptation ofListeria monocytogenes to Growth at Low Temperature

2000 ◽  
Vol 182 (24) ◽  
pp. 7083-7087 ◽  
Author(s):  
Lynne A. Becker ◽  
Stefanie N. Evans ◽  
Robert W. Hutkins ◽  
Andrew K. Benson

ABSTRACT The activity of ςB in Listeria monocytogenes is stimulated by high osmolarity and is necessary for efficient uptake of osmoprotectants. Here we demonstrate that, during cold shock, ςB contributes to adaptation in a growth phase-dependent manner and is necessary for efficient accumulation of betaine and carnitine as cryoprotectants.

1998 ◽  
Vol 180 (1) ◽  
pp. 90-95 ◽  
Author(s):  
Li Fang ◽  
Yan Hou ◽  
Masayori Inouye

ABSTRACT Upon temperature downshift, a group of proteins called cold shock proteins, such as CspA, CspB, and CsdA, are transiently induced inEscherichia coli. However, when the 5′ untranslated region (5′ UTR) of cspA mRNA is overproduced at low temperature, the expression of cold shock genes is prolonged or derepressed. It has been proposed that this effect is due to highly conserved 11-base sequences designated the “cold box” existing in the 5′ UTRs ofcspA, cspB, and csdA. Here, we demonstrate that the overproduction of the 5′ UTR of not onlycspA but also cspB and csdA mRNAs causes derepression of all three genes at the same time. Conversely, when the cold-box region was deleted from the cspA 5′ UTR its derepression function was abolished. The amount of mRNA from the chromosomal cspA gene was much higher in cells overproducing the wild-type 5′ UTR by means of a plasmid than it was in cells overproducing the cold-box-deleted 5′ UTR. The stability of the chromosomal cspA mRNA in cells overproducing the wild-type 5′ UTR was almost identical to that in cells overproducing the cold-box-deleted 5′ UTR. Therefore, the derepression ofcspA caused by overproduction of 5′ UTR at the end of the acclimation phase occurs at the level of transcription but not by mRNA stabilization, indicating that the cold-box region plays a negative role in cspA transcription in cold shock-adapted cells. The role of the cold-box region was further confirmed with acspA mutant strain containing a cold-box-deletedcspA gene integrated into the chromosome, which showed a high level of constitutive production of CspA but not CspB during exponential growth at low temperature.


2005 ◽  
Vol 245 (2) ◽  
pp. 329-336 ◽  
Author(s):  
Ute Schwab ◽  
Barbara Bowen ◽  
Celine Nadon ◽  
Martin Wiedmann ◽  
Kathryn J. Boor

2000 ◽  
Vol 182 (22) ◽  
pp. 6391-6400 ◽  
Author(s):  
Christine A. White-Ziegler ◽  
Anuradha Villapakkam ◽  
Karla Ronaszeki ◽  
Sarah Young

ABSTRACT A comparative study was completed to determine the influence of various environmental stimuli on the transcription of three different fimbrial operons in Escherichia coli and to determine the role of the histone-like protein H-NS in this environmental regulation. The fimbrial operons studied included the pap operon, which encodes pyelonephritis-associated pili (P pili), the daaoperon, which encodes F1845 fimbriae, and the fan operon, which encodes K99 fimbriae. Using lacZYA transcriptional fusions within each of the fimbrial operons, we tested temperature, osmolarity, carbon source, rich medium, oxygen levels, pH, amino acids, solid medium, and iron concentration for their effects on fimbrial gene expression. Low temperature, high osmolarity, glucose as a carbon source, and rich medium repressed transcription of all three operons. High iron did not alter transcription of any of the operons tested, whereas the remaining stimuli had effects on individual operons. For the pap and daa operons, introduction of thehns651 mutation relieved the repression, either fully or partially, due to low temperature, glucose as a carbon source, rich medium, and high osmolarity. Taken together, these data indicate that there are common environmental cues that regulate fimbrial transcription in E. coli and that H-NS is an important environmental regulator for fimbrial transcription in response to several stimuli.


2000 ◽  
Vol 68 (12) ◽  
pp. 7069-7077 ◽  
Author(s):  
Elise Borezee ◽  
Elisabeth Pellegrini ◽  
Patrick Berche

ABSTRACT We identified a new oligopeptide permease operon in the pathogenListeria monocytogenes. This opp operon consists of five genes (oppA, oppB, oppC, oppD, andoppF) and displays the same genetic organization as those of several bacterial species. The first gene of this operon,oppA, encodes a 62-kDa protein sharing 33% identity with OppA of Bacillus subtilis and is expressed predominantly during exponential growth. The function of oppA was studied by constructing an oppA deletion mutant. The phenotype analysis of this mutant revealed that OppA mediates the transport of oligopeptides and is required for bacterial growth at low temperature. The wild-type phenotype was restored by complementing the mutant withoppA. We also found that OppA is involved in intracellular survival in macrophages and in bacterial growth in organs of mice infected with L. monocytogenes, although the level of virulence was not altered in the mutant. These results show the major role of OppA in the uptake of oligopeptides and the pleiotropic effects of this oligopeptide-binding protein on the behavior of this pathogen in the environment and in its host.


2003 ◽  
Vol 219 (2) ◽  
pp. 233-239 ◽  
Author(s):  
Lone Brøndsted ◽  
Birgitte H Kallipolitis ◽  
Hanne Ingmer ◽  
Susanne Knöchel

2000 ◽  
Vol 23 (2) ◽  
pp. 165-173 ◽  
Author(s):  
Jeroen A. Wouters ◽  
Frank M. Rombouts ◽  
Oscar P. Kuipers ◽  
Willem M. de Vos ◽  
T. Abee

2008 ◽  
Vol 190 (10) ◽  
pp. 3467-3474 ◽  
Author(s):  
Tatiana E. Erova ◽  
Valeri G. Kosykh ◽  
Amin A. Fadl ◽  
Jian Sha ◽  
Amy J. Horneman ◽  
...  

ABSTRACT In this study, we cloned and sequenced a virulence-associated gene (vacB) from a clinical isolate SSU of Aeromonas hydrophila. We identified this gene based on our recently annotated genome sequence of the environmental isolate ATCC 7966T of A. hydrophila and the vacB gene of Shigella flexneri. The A. hydrophila VacB protein contained 798 amino acid residues, had a molecular mass of 90.5 kDa, and exhibited an exoribonuclease (RNase R) activity. The RNase R of A. hydrophila was a cold-shock protein and was required for bacterial growth at low temperature. The vacB isogenic mutant, which we developed by homologous recombination using marker exchange mutagenesis, was unable to grow at 4°C. In contrast, the wild-type (WT) A. hydrophila exhibited significant growth at this low temperature. Importantly, the vacB mutant was not defective in growth at 37°C. The vacB mutant also exhibited reduced motility, and these growth and motility phenotype defects were restored after complementation of the vacB mutant. The A. hydrophila RNase R-lacking strain was found to be less virulent in a mouse lethality model (70% survival) when given by the intraperitoneal route at as two 50% lethal doses (LD50). On the other hand, the WT and complemented strains of A. hydrophila caused 80 to 90% of the mice to succumb to infection at the same LD50 dose. Overall, this is the first report demonstrating the role of RNase R in modulating the expression of A. hydrophila virulence.


Microbiology ◽  
1995 ◽  
Vol 141 (1) ◽  
pp. 41-49 ◽  
Author(s):  
A. Maria-Rosario ◽  
I. Davidson ◽  
M. Debra ◽  
A. Verheul ◽  
T. Abee ◽  
...  

2002 ◽  
Vol 68 (2) ◽  
pp. 456-463 ◽  
Author(s):  
Henrike H. Wemekamp-Kamphuis ◽  
Andreas K. Karatzas ◽  
Jeroen A. Wouters ◽  
Tjakko Abee

ABSTRACT Listeria monocytogenes is a psychrotrophic food-borne pathogen that is problematic for the food industry because of its ubiquitous distribution in nature and its ability to grow at low temperatures and in the presence of high salt concentrations. Here we demonstrate that the process of adaptation to low temperature after cold shock includes elevated levels of cold shock proteins (CSPs) and that the levels of CSPs are also elevated after treatment with high hydrostatic pressure (HHP). Two-dimensional gel electrophoresis combined with Western blotting performed with anti-CspB of Bacillus subtilis was used to identify four 7-kDa proteins, designated Csp1, Csp2, Csp3, and Csp4. In addition, Southern blotting revealed four chromosomal DNA fragments that reacted with a csp probe, which also indicated that a CSP family is present in L. monocytogenes LO28. After a cold shock in which the temperature was decreased from 37�C to 10�C the levels of Csp1 and Csp3 increased 10- and 3.5-fold, respectively, but the levels of Csp2 and Csp4 were not elevated. Pressurization of L. monocytogenes LO28 cells resulted in 3.5- and 2-fold increases in the levels of Csp1 and Csp2, respectively. Strikingly, the level of survival after pressurization of cold-shocked cells was 100-fold higher than that of cells growing exponentially at 37�C. These findings imply that cold-shocked cells are protected from HHP treatment, which may affect the efficiency of combined preservation techniques.


2015 ◽  
Vol 81 (12) ◽  
pp. 3994-4004 ◽  
Author(s):  
Anna Pöntinen ◽  
Annukka Markkula ◽  
Miia Lindström ◽  
Hannu Korkeala

ABSTRACTTwo-component systems (TCSs) aid bacteria in adapting to a wide variety of stress conditions. While the role of TCS response regulators in the cold tolerance of the psychrotrophic foodborne pathogenListeria monocytogeneshas been demonstrated previously, no comprehensive studies showing the role of TCS histidine kinases ofL. monocytogenesat low temperature have been performed. We compared the expression levels of each histidine kinase-encoding gene ofL. monocytogenesEGD-e in logarithmic growth phase at 3°C and 37°C, as well as the expression levels 30 min, 3 h, and 7 h after cold shock at 5°C and preceding cold shock (at 37°C). We constructed a deletion mutation in each TCS histidine kinase gene, monitored the growth of the EGD-e wild-type and mutant strains at 3°C and 37°C, and measured the minimum growth temperature of each strain. Two genes,yycGandlisK, proved significant in regard to induced relative expression levels under cold conditions and cold-sensitive mutant phenotypes. Moreover, the ΔresEmutant showed a lower growth rate than that of wild-type EGD-e at 3°C. Eleven other genes showed upregulated gene expression but revealed no cold-sensitive phenotypes. The results show that the histidine kinases encoded byyycGandlisKare important for the growth and adaptation ofL. monocytogenesEGD-e at low temperature.


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