A proteomic approach to study the acid response inListeria monocytogenes

Phan‐Thanh, Luu; Mahouin, François

doi:10.1002/(sici)1522-2683(19990801)20:11<2214::aid-elps2214>3.0.co;2-g

Cited by 70 publications

(44 citation statements)

References 33 publications

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“…lactis strain IL 403 (112). DnaK and GroEL are also induced following acid adaptation of Lactobacillus delbrueckii (145), while GroEL is induced in response to acid stress in Clostridium perfringens (238), S. mutans (249), and Listeria monocytogenes (178,179).…”

Section: Protection or Repair Of Macromoleculesmentioning

confidence: 99%

“…In addition, six proteins were identified following HCl adaptation which were not visible on other gels (171). The proteins induced in response to acid induction and acid stress caused by the addition of HCl to minimal medium have also been examined (178,179). It was found that 47 and 37 proteins were induced by pH 3.5 and 5.5, respectively, and that 23 of these were common (Table 1).…”

Section: Listeria Monocytogenesmentioning

confidence: 99%

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Surviving the Acid Test: Responses of Gram-Positive Bacteria to Low pH

Cotter

Hill

2003

Microbiol Mol Biol Rev

1,042

828

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Gram-positive bacteria possess a myriad of acid resistance systems that can help them to overcome the challenge posed by different acidic environments. In this review the most common mechanisms are described: i.e., the use of proton pumps, the protection or repair of macromolecules, cell membrane changes, production of alkali, induction of pathways by transcriptional regulators, alteration of metabolism, and the role of cell density and cell signaling. We also discuss the reponses of Listeria monocytogenes, Rhodococcus, Mycobacterium, Clostridium perfringens, Staphylococcus aureus, Bacillus cereus, oral streptococci, and lactic acid bacteria to acidic environments and outline ways in which this knowledge has been or may be used to either aid or prevent bacterial survival in low-pH environments

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Section: Protection or Repair Of Macromoleculesmentioning

confidence: 99%

Section: Listeria Monocytogenesmentioning

confidence: 99%

Surviving the Acid Test: Responses of Gram-Positive Bacteria to Low pH

Cotter

Hill

2003

Microbiol Mol Biol Rev

1,042

828

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“…The procedure for in-gel tryptic digestion was performed according to the method previously described [28] except for a slight modification. In brief, Coomassie blue stained protein spots excised from distilled water-washed gel were cut into small pieces in microfuge tubes.…”

Section: Esi-q-tof Mass Spectrometry Analysismentioning

confidence: 99%

Comparison of Tir from enterohemorrahgic and enteropathogenic Escherichia coli strains: two homologues with distinct intracellular properties

Chuang¹,

Chiu²,

Hsu³

et al. 2005

J Biomed Sci

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SummaryTir of enteropathogenic Escherichia coli (EPEC) or enterohemorrahgic E. coil (EHEC) is translocated by a type III secretion system to the host cell membranes where it serves as a receptor for the binding of a second bacterial membrane protein. In response to the binding, EPEC Tir is phosphorylated at Tyr 474 , and this phosphorylation is necessary for the signaling of pedestal formation. Tir of EHEC has no equivalent phosphorylation site but it is similarly needed for cytoskeleton rearrangement. How these two Tir molecules achieve their function by apparently different mechanisms is not completely clear. To examine their intrinsic differences, the two Tirs were expressed in HeLa cells and compared. Actin in complexes could be pelleted down from the lysate of cells expressing EHEC Tir but not EPEC Tir. By immunostaining, neither Tir molecule was found in phosphorylated state. In the cytoplasm, EHEC Tir was frequently found in fibrous structures whereas EPEC Tir was observed completely in a diffusive form. The determinant critical for the EHEC Tir fibrous formation was mapped to the C-terminal region of the molecule that deviates from the EPEC counterpart. This region may play a role in taking an alternative route different from Tyr 474 phosphorylation to transduce signals.

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“…Q-TOF mass spectroscopy. In-gel tryptic digestion was performed as previously described (30), except for a slight modification. In brief, Coomassie blue dye-stained protein spots excised from a distilled-water-washed gel were cut into small pieces.…”

mentioning

confidence: 99%

Expression Analysis of Up-Regulated Genes Responding to Plumbagin inEscherichia coli

et al. 2006

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Plumbagin is found in many medicinal plants and has been reported to have antimicrobial activities. We examined the molecular responses of Escherichia coli to plumbagin by using a proteomic approach to search for bacterial genes up-regulated by the drug. The protein profile obtained was compared with that of E. coli without the plumbagin treatment. Subsequent analyses of the induced proteins by mass spectroscopy identified several up-regulated genes, including ygfZ, whose function has not been defined. Analyses of the 5-flanking sequences indicate that most of these genes contain a marbox-like stretch, and several of them are categorized as members of the mar/sox regulon. Representatives of these genes were cloned into plasmids, and the marbox-like sequences were modified by site-directed mutagenesis. It was proven that mutations in these regions substantially repressed the level of proteins encoded by the downstream genes. Furthermore, plumbagin's early effect was demonstrated to robustly induce SoxS rather than MarA, an observation distinctly different from that seen with sodium salicylate.Plumbagin (5-hydroxy-2-methyl-1,4-naphthoquinone) is a naphthoquinone having antibacterial (6), antifungal (5), anticancer (22), and antimutagenic activities (7). Like other redoxcycling chemicals such as paraquat and menadione, plumbagin has been used as an agent to generate superoxide or reactive oxygen species in order to study oxidative stress (14). Plumbagin has been suggested to activate SoxS by oxidizing the SoxR molecule (10, 21) or inhibiting the repression of MarR (2), the effect of which is exerted on marA, resulting in activation of the mar/sox regulon. In addition, it has been observed that the expression of some members of the mar/sox regulon in Escherichia coli, such as sodA (8), nfo (3), ribA (20), and pqi (21), is up-regulated by treatment with plumbagin.Although plumbagin could induce excessive expression of superoxide dismutase and catalase, overexpression of sodA failed to protect E. coli (17). The toxic effect of plumbagin may not simply result from the production of reactive oxygen species. It has been reported that plumbagin inhibits NADH dehydrogenase, as well as causing respiratory arrest (17). Plumbagin has also been shown to modify the lactose carrier and inhibit its binding with galactoside; the modified carrier then becomes completely inactive (29). The above effects appeared more or less to result directly from the chemical nature of plumbagin. In this report, we focus on the responses of the bacteria to the chemical, in which multiple proteins were simultaneously induced by plumbagin treatment. We report the evaluation of the bacterial regulatory systems after treating E. coli with plumbagin. MATERIALS AND METHODSBacterial strains, plasmids, and growth conditions. E. coli JM109 was used as the major experimental strain for the chemical treatments and the cloning host. Plasmids pGEM-T-easy (Promega, Madison, WI), pBluescript II SKϩ (Stratagene, La Jolla, CA), and pQE60 (QIAGEN, Valencia, CA) wer...

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A proteomic approach to study the acid response inListeria monocytogenes

Cited by 70 publications

References 33 publications

Surviving the Acid Test: Responses of Gram-Positive Bacteria to Low pH

Surviving the Acid Test: Responses of Gram-Positive Bacteria to Low pH

Comparison of Tir from enterohemorrahgic and enteropathogenic Escherichia coli strains: two homologues with distinct intracellular properties

Expression Analysis of Up-Regulated Genes Responding to Plumbagin inEscherichia coli

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