PhoE porin of Escherichia coli and phosphate reversal of acid damage and killing and of acid induction of the CadA gene product

Rowbury, R. J.; Goodson, Margaret

doi:10.1111/j.1365-2672.1993.tb05199.x

Cited by 25 publications

(25 citation statements)

References 20 publications

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“…However, inhibition of ASP synthesis did not abolish ATR in all the studies. Protein neosynthesis inhibition by chloramphenicol reversed ATR in L. monocytogenes (4), in A. hydrophila (18), and in the enterobacteria S. enterica serovar Typhimurium and E. coli (7,36). In contrast, it showed no effect on acid adaptation in L. lactis subsp.…”

Section: Discussionmentioning

confidence: 82%

“…ATR has been well documented for a number of gastrointestinal or foodborne pathogenic bacteria, such as Escherichia coli (36), Salmonella enterica serovar Typhimurium (7), Aeromonas hydrophila (18), Vibrio parahaemolyticus (45), Helicobacter pylori (27), Listeria monocytogenes (4), and Enterococcus faecalis (6), as well as the oral cariogenic organism Streptococcus mutans (12). Indeed adaptation and survival at low pH might be important factors in the pathogenicity of gastrointestinal bacteria and are of great concern in food safety and health.…”

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confidence: 99%

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Changes in Protein Synthesis and Morphology during Acid Adaptation of Propionibacterium freudenreichii

Jan

Leverrier

Pichereau

et al. 2001

Appl Environ Microbiol

103

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Survival of bacteria in changing environments depends on their ability to adapt to abiotic stresses. Microorganisms used in food technology face acid stress during fermentation processes. Similarly, probiotic bacteria have to survive acid stress imposed within the stomach in order to reach the intestine and play a beneficial role. Propionibacteria are used both as cheese starters and as probiotics in human alimentation. Adaptation to low pH thus constitutes a limit to their efficacy. Acid stress adaptation in the probiotic SI41 strain of Propionibacterium freudenreichii was therefore investigated. The acid tolerance response (ATR) was evidenced in a chemically defined medium. Transient exposure to pH 5 afforded protection toward acid challenge at pH 2. Protein neosynthesis was shown to be required for optimal ATR, since chloramphenicol reduced the acquired acid tolerance. Important changes in genetic expression were observed with two-dimensional electrophoresis during adaptation. Among the up-regulated polypeptides, a biotin carboxyl carrier protein and enzymes involved in DNA synthesis and repair were identified during the early stress response, while the universal chaperonins GroEL and GroES corresponded to a later response. The beneficial effect of ATR was evident at both the physiological and morphological levels. This study constitutes a first step toward understanding the very efficient ATR described in P. freudenreichii.

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Section: Discussionmentioning

confidence: 82%

mentioning

confidence: 99%

Changes in Protein Synthesis and Morphology during Acid Adaptation of Propionibacterium freudenreichii

Jan

Leverrier

Pichereau

et al. 2001

Appl Environ Microbiol

103

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“…It is possible that this enzyme also plays a role in the survival of L. monoytugenes at low pH. Other possible mechanisms of acid resistance include acidinduced DNA repair systems, increased cytoplasmic buffering capacity and decreased proton permeability of the cell membrane (perhaps by removing 'leaky' membrane proteins; see for example Rowbury & Goodson, 1993).…”

Section: Discussionmentioning

confidence: 99%

Acid tolerance in Listeria monocytogenes: the adaptive acid tolerance response (ATR) and growth-phase-dependent acid resistance

Davis

Coote²,

O’Byrne³

1996

Microbiology

218

135

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Listeria monocytogenes acquired increased acid tolerance during exponential growth upon exposure to sublethal acid stress, a response designated the acid tolerance response (ATR). Maximal acid resistance was seen when the organism was exposed to pH 5.0 for 1 h prior to challenge at pH 3.0, although intermediate levels of protection were afforded by exposure to pH values ranging from 4.0 to 6.0. A 60 min adaptive period was required for the development of maximal acid tolerance; during this period the level of acid tolerance increased gradually. Full expression of the ATR required de now0 protein synthesis; chloramphenicol, a protein synthesis inhibitor, prevented full induction of acid tolerance. Analysis of protein expression during the adaptive period by two-dimensional gel electrophoresis revealed a change in the expression of at least 23 proteins compared to the non-adapted culture.Eleven proteins showed induced expression while 12 were repressed, implying that the ATR is a complex response involving a modulation in the expression of a large number of genes. In addition to the exponential phase ATR, L. monocytogenes also developed increased acid resistance upon entry into the stationary phase; this response appeared to be independent of the pHdependent ATR seen during exponential growth.

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“…The external pH was maintained within 0.2 pH unit during cell growth in these media throughout the course of the experiments. The cadaverine used was in the free-base form (C5H14N2) Antibiotics were used in plate and liquid media at the following concentrations: ampicillin sodium salt, kanamycin sulfate, and spectinomycin, 50 ,ug/ml; tetracycline, 10 ,ug/ml; streptomycin, 100 jig/ml; and chloramphenicol, 35 ,ug/ml. X-Gal (5-bromo-4-chloro-3-indolyl-,3-D-galactopyranoside) was used at 40 ,ug/ml in solid media.…”

Section: Methodsmentioning

confidence: 99%

“…An adaptation response occurs when Escherichia coli and Salmonella typhimurium are exposed to moderate acid conditions, which serves to protect them from a more severe drop in external pH (8-12, 33, 36). E. coli mutants defective in lysine decarboxylase carry out a normal adaptation response, suggesting that these systems for responding to low external pH are distinct (35).…”

mentioning

confidence: 99%

Roles of LysP and CadC in mediating the lysine requirement for acid induction of the Escherichia coli cad operon

Neely¹,

Dell²,

Olson³

1994

J Bacteriol

122

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Expression of the Escherichia col cadBA operon, Encoding functions required for the conversion of lysine to cadaverine and for cadaverine excretion, requires at least two extracellular signals: low pH and a high concentration of lysine. To better understand the nature of the lysine-dependent signal, mutants were isolated which expressed a cad4-lacZ transciription fusion in the absence of lysine while retaining pH regulation. The responsible mutation in one of these isolates (EP310) was in cadC, a gene encoding a function necessary for transcriptional activation of cadB4. This mutation (cadC310) is in a part of the gene encoding the periplasmic domain of CadC and results in an Arg-to-Cys chane at position 265, indicating that this part of the protein is involved in responding to the presence of lysine. Three other mutants had mutations mapping in or near lysP (cadR), a gene encoding a lysine transport protein that has previously been shown to regulate cad4 expression. One of these mutations is an insertion in the lysP coding regiw. Thus, in the absence of exogenous lysine, LysP is a negative regulator ofcadB4 expression. Negative regulation b$fysP was further demonstrated by showing that lysP expression from a hi-opy-number plasmid rendered cad4-lacZ uninducible. Expression of cad4-lacZ in a strain carrying the cadC310 allele, however, was not affected by the plasmid-expressed IsP. Cadaverine was shown to inhibit expression of the cad4-lacZ fusion in cadC' cells but not in a cadC310 background.Bacteria respond to changes in external pH by altering their pattern of gene expression as well as other physiological processes (1, 3, 9, 14, 15, 18-20, 28-30, 39, 41). In many cases the responsible pH change does not alter internal pH, suggesting that bacteria possess transmembrane signaling systems which ultimately influence the transcription and translation machineries. Despite the important role that this physicochemical parameter plays in cell physiology, the components and operation of these signaling systems are poorly understood. One of the first observations concerning the alteration of enzymatic functions in bacteria as a consequence of low external pH was of increased levels of amino acid decarboxylases (13). These decarboxylation reactions result in excretion of the decarboxylated amino acid, release of C02, and an increase in external pH. The exact physiological role of each of these reactants and products in growth and survival of the cell at low pH has not been thoroughly examined. An adaptation response occurs when Escherichia coli and Salmonella typhimurium are exposed to moderate acid conditions, which serves to protect them from a more severe drop in external pH (8-12, 33, 36). E. coli mutants defective in lysine decarboxylase carry out a normal adaptation response, suggesting that these systems for responding to low external pH are distinct (35).To better understand how bacteria sense and respond to changes in external pH, we have been studying the genetic elements involved in acid induction of the E. ...

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PhoE porin of Escherichia coli and phosphate reversal of acid damage and killing and of acid induction of the CadA gene product

Cited by 25 publications

References 20 publications

Changes in Protein Synthesis and Morphology during Acid Adaptation of Propionibacterium freudenreichii

Changes in Protein Synthesis and Morphology during Acid Adaptation of Propionibacterium freudenreichii

Acid tolerance in Listeria monocytogenes: the adaptive acid tolerance response (ATR) and growth-phase-dependent acid resistance

Roles of LysP and CadC in mediating the lysine requirement for acid induction of the Escherichia coli cad operon

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