Abstract
The term “stress” refers to any extracellular influence that threatens the ability of microorganisms to perform their living functions. In nature, microorganisms are constantly exposed to diverse changes in temperature, oxygen, moisture, light, pH, and chemical composition. Thanks to their wide array of molecular responses that make them survive by providing cellular protection against stresses. This protection from such inevitable stresses in microbial systems is ensured by sophisticated genetic regulatory systems and molecular stress responses specific to individual chemical or physical threats. This chapter will summarize and discuss current knowledge about the oxidative stress response evolved in food pathogens following the oxidative stress encountered in food and food processing environments (including acid, osmotic and oxidative stress, starvation, detergents and disinfectants, chilling, heat, and other nonthermal technologies) and from the food preservation technologies designed to rapidly inactivate microbial cells including thermal processes such as low-temperature storage (refrigeration and freezing), irradiation, high-pressure processing, use of strong oxidant compounds, reduction of moisture content (concentration and drying), control of redox potential (use of controlled atmospheres and vacuum packaging), and acidification (fermentation and addition of organic acids) certainly with special emphasis on virulence and growth fitness.
Access this chapter
Tax calculation will be finalised at checkout
Purchases are for personal use only
Similar content being viewed by others
References
Abram F, Starr E, Karatzas KAG et al (2008) Identification of components of the sigma B regulon in Listeria monocytogenes that contribute to acid and salt tolerance. Appl Environ Microbiol 74(22):6848–6858. https://doi.org/10.1128/AEM.00442-08
Alamuri P, Maier RJ (2004) Methionine sulphoxide reductase is an important antioxidant enzyme in the gastric pathogen Helicobacter pylori. Mol Microbiol 53(5):1397–1406. https://doi.org/10.1111/j.1365-2958.2004.04190.x
Allen KJ, Lepp D, McKellar RC, Griffiths MW (2008) Examination of stress and virulence gene expression in Escherichia coli O157:H7 using targeted microarray analysis. Foodborne Pathog Dis 5(4):437–447. https://doi.org/10.1089/fpd.2008.0100
Alonso JC, Stiege AC, Lüder G (1993) Genetic recombination in Bacillus subtilis 168: effect of recN, recF, recH and addAB mutations on DNA repair and recombination. MGG Mol Gen Genet 239:129–136. https://doi.org/10.1007/BF00281611
Ambur OH, Davidsen T, Frye SA et al (2009) Genome dynamics in major bacterial pathogens. FEMS Microbiol Rev 33(3):453–470
Andersen JB, Roldgaard BB, Christensen BB, Licht TR (2007) Oxygen restriction increases the infective potential of Listeria monocytogenes in vitro in Caco-2 cells and in vivo in Guinea pigs. BMC Microbiol 7:1–7
Antelmann H, Hecker M, Zuber P (2008) Proteomic signatures uncover thiol-specific electrophile resistance mechanisms in Bacillus subtilis. Expert Rev Proteomics 5(1):77–90
Arnér ESJ, Holmgren A (2000) Physiological functions of thioredoxin and thioredoxin reductase. Eur J Biochem 267(20):6102–6109
Atack JM, Kelly DJ (2008) Contribution of the stereospecific methionine sulphoxide reductases MsrA and MsrB to oxidative and nitrosative stress resistance in the food-borne pathogen Campylobacter jejuni. Microbiology. https://doi.org/10.1099/mic.0.2008/019711-0
Atack JM, Harvey P, Jones MA, Kelly DJ (2008) The Campylobacter jejuni thiol peroxidases Tpx and Bcp both contribute to aerotolerance and peroxide-mediated stress resistance but have distinct substrate specificities. J Bacteriol. https://doi.org/10.1128/JB.00100-08
Baichoo N, Helmann JD (2002) Recognition of DNA by fur: a reinterpretation of the fur box consensus sequence. J Bacteriol 184:5826–5832. https://doi.org/10.1128/JB.184.21.5826-5832
Baillon MLA, Van Vliet AHM, Ketley JM et al (1999) An iron-regulated alkyl hydroperoxide reductase (AhpC) confers aerotolerance and oxidative stress resistance to the microaerophilic pathogen Campylobacter jejuni. J Bacteriol. https://doi.org/10.1128/jb.181.16.4798-4804.1999
Baker J, Sitthisak S, Sengupta M et al (2010) Copper stress induces a global stress response in Staphylococcus aureus and represses sae and agr expression and biofilm formations. Appl Environ Microbiol 76:150–160. https://doi.org/10.1128/AEM.02268-09
Ballal A, Manna AC (2009) Regulation of superoxide dismutase (sod) genes by sarA in Staphylococcus aureus. J Bacteriol 191(10):3301–3310. https://doi.org/10.1128/JB.01496-08
Barrière C, Brückner R, Talon R (2001) Characterization of the single superoxide dismutase of Staphylococcus xylosus. Appl Environ Microbiol. https://doi.org/10.1128/AEM.67.9.4096-4104.2001
Beales N (2004) Adaptation of microorganisms to cold temperatures, weak acid preservatives, low pH, and osmotic stress: a review. Compr Rev Food Sci Food Saf. https://doi.org/10.1111/j.1541-4337.2004.tb00057.x
Becker LA, Çetin MS, Hutkins RW, Benson AK (1998) Identification of the gene encoding the alternative sigma factor σ(B) from Listera monocytogenes and its role in osmotolerance. J Bacteriol. https://doi.org/10.1128/jb.180.17.4547-4554.1998
Beckman JS, Koppenol WH (1996) Nitric oxide, superoxide, and peroxynitrite: the good, the bad, and the ugly. Am J Physiol Cell Physiol 271(5 Pt 1):C1424–C1437
Beggs GA, Brennan RG, Arshad M (2020) MarR family proteins are important regulators of clinically relevant antibiotic resistance. Protein Sci 29(3):647–653
Begley M, Hill C (2015) Stress adaptation in foodborne pathogens. Annu Rev Food Sci Technol 6:191–210
Begley M, Hill C, Ross RP (2006) Tolerance of Listeria monocytogenes to cell envelope-acting antimicrobial agents is dependent on SigB. Appl Environ Microbiol. https://doi.org/10.1128/AEM.72.3.2231-2234.2006
Blaiotta G, Fusco V, Ercolini D et al (2010) Diversity of Staphylococcus species strains based on partial kat (catalase) gene sequences and design of a PCR-restriction fragment length polymorphism assay for identification and differentiation of coagulase-positive species (S. aureus, S. delphini, S. hyicus, S. intermedius, S. pseudintermedius, and S. schleiferi subsp. coagulans). J Clin Microbiol 48:192–201. https://doi.org/10.1128/JCM.00542-09
Bonamore A, Boffi A (2008) Flavohemoglobin: structure and reactivity. IUBMB Life 60:19–28
Brot N, Weissbach H (2000) Peptide methionine sulfoxide reductase: biochemistry and physiological role. Biopolymers 55(4):288–296
Browne N, Dowds BCA (2001) Heat and salt stress in the food pathogen Bacillus cereus. J Appl Microbiol. https://doi.org/10.1046/j.1365-2672.2001.01478.x
Bsat N, Herbig A, Casillas-Martinez L et al (1998) Bacillus subtilis contains multiple fur homologues: identification of the iron uptake (fur) and peroxide regulon (PerR) repressors. Mol Microbiol. https://doi.org/10.1046/j.1365-2958.1998.00921.x
Caleb OJ, Mahajan PV, Al-Said FA-J, Opara UL (2013) Modified atmosphere packaging technology of fresh and fresh-cut produce and the microbial consequences-a review. Food Bioprocess Technol 6:303–329
Cao M, Moore CM, Helmann JD (2005) Bacillus subtilis paraquat resistance is directed by σM, an extracytoplasmic function sigma factor, and is conferred by YqjL and BcrC. J Bacteriol 187:2948–2956. https://doi.org/10.1128/JB.187.9.2948-2956.2005
Capozzi V, Fiocco D, Amodio ML et al (2009) Bacterial stressors in minimally processed food. Int J Mol Sci 10(7):3076–3105
Cebrián G, Sagarzazu N, Aertsen A et al (2009) Role of the alternative sigma factor σb on Staphylococcus aureus resistance to stresses of relevance to food preservation. J Appl Microbiol. https://doi.org/10.1111/j.1365-2672.2009.04194.x
Ceragioli M, Mols M, Moezelaar R et al (2010) Comparative transcriptomic and phenotypic analysis of the responses of Bacillus cereus to various disinfectant treatments. Appl Environ Microbiol. https://doi.org/10.1128/AEM.03003-09
Chang W, Small DA, Toghrol F, Bentley WE (2006) Global transcriptome analysis of Staphylococcus aureus response to hydrogen peroxide. J Bacteriol. https://doi.org/10.1128/jb.188.4.1648-1659.2006
Chelikani P, Fita I, Loewen PC (2004) Diversity of structures and properties among catalases. Cell Mol Life Sci C. 61(2):192–208
Chiang SM, Schellhorn HE (2012) Regulators of oxidative stress response genes in Escherichia coli and their functional conservation in bacteria. Arch Biochem Biophys 525(2):161–169
Chouchani ET, James AM, Fearnley IM et al (2011) Proteomic approaches to the characterization of protein thiol modification. Curr Opin Chem Biol 15(1):120–128
Chowdhury R, Sahu GK, Das J (1996) Stress response in pathogenic bacteria. J Biosci. https://doi.org/10.1007/BF02703105
Clements MO, Watson SP, Foster SJ (1999) Characterization of the major superoxide dismutase of Staphylococcus aureus and its role in starvation survival, stress resistance, and pathogenicity. J Bacteriol. https://doi.org/10.1128/jb.181.13.3898-3903.1999
Corbett D, Goldrick M, Fernandes VE, et al (2017) Listeria monocytogenes has both a bd-type and an aa3-type terminal oxidase which allow growth in different oxygen levels and both are important in infection. Infect Immun 85(11):e00354–e00317
Coulter SN, Schwan WR, Ng EYW, et al (1998) Staphylococcus aureus genetic loci impacting growth and survival in multiple infection environments. Mol Microbiol. https://doi.org/10.1046/j.1365-2958.1998.01075.x
Dame RT (2005) The role of nucleoid-associated proteins in the organization and compaction of bacterial chromatin. Mol Microbiol 56:858–870
Davì V, Minc N (2015) Mechanics and morphogenesis of fission yeast cells. Curr Opin Microbiol 28:36–45
Dean RT, Fu S, Stocker R, Davies MJ (1997) Biochemistry and pathology of radical-mediated protein oxidation. Biochem J 324(Pt 1):1–18
Demple B, Harrison L (1994) Repair of oxidative damage to DNA: enzymology and biology. Annu Rev Biochem 63:915–948
Demple B, Linn S (1982) 5,6-saturated thymine lesions in DNA: production by ultraviolet light or hydrogen peroxide. Nucleic Acids Res 10:3781–3789
Den Besten HMW, Mols M, Moezelaar R et al (2009) Phenotypic and transcriptomic analyses of mildly and severely salt-stressed Bacillus cereus ATCC 14579 cells. Appl Environ Microbiol. https://doi.org/10.1128/AEM.02891-08
Di Simplicio P, Franconi F, Frosalí S, Di Giuseppe D (2003) Thiolation and nitrosation of cysteines in biological fluids and cells. Amino Acids 25(3–4):323–339
Dukan S, Belkin S, Touati D (1999) Reactive oxygen species are partially involved in the bacteriocidal action of hypochlorous acid. Arch Biochem Biophys. https://doi.org/10.1006/abbi.1999.1265
Eisen JA, Hanawalt PC (1999) A phylogenomic study of DNA repair genes, proteins, and processes. Mutat Res 435(3):171–213
Elvers KT, Park SF (2002) Quorum sensing in Campylobacter jejuni: detection of a luxS encoded signalling molecule. Microbiology 148(5):1475–1481. https://doi.org/10.1099/00221287-148-5-1475
Ermler U, Siddiqui RA, Cramm R, Friedrich B (1995) Crystal structure of the flavohemoglobin from Alcaligenes eutrophus at 1.75 Å resolution. EMBO J. https://doi.org/10.1002/j.1460-2075.1995.tb00297.x
Esbelin J, Santos T, Hébraud M (2018) Desiccation: an environmental and food industry stress that bacteria commonly face. Food Microbiol 69:82–88
Ezraty B, Gennaris A, Barras F, Collet JF (2017) Oxidative stress, protein damage and repair in bacteria. Nat Rev Microbiol 15(7):385–396
Fahey RC (2001) Novel thiols of prokaryotes. Annu Rev Microbiol 55:333–356
Farr SB, Kogoma T (1991) Oxidative stress responses in Escherichia coli and Salmonella Typhimurium. Microbiol Rev 55:561–585
Flint DH, Tuminello JF, Emptage MH (1993) The inactivation of Fe-S cluster containing hydro-lyases by superoxide. J Biol Chem. https://doi.org/10.1016/s0021-9258(18)41538-4
Flint A, Sun YQ, Stintzi A (2012) Cj1386 is an ankyrin-containing protein involved in heme trafficking to catalase in Campylobacter jejuni. J Bacteriol. https://doi.org/10.1128/JB.05740-11
Flint A, Sun YQ, Butcher J et al (2014) Phenotypic screening of a targeted mutant library reveals Campylobacter jejuni defenses against oxidative stress. Infect Immun. https://doi.org/10.1128/IAI.01528-13
Freedman JC, Shrestha A, McClane BA (2016) Clostridium perfringens enterotoxin: action, genetics, and translational applications. Toxins (Basel) 8(3):73
Fridavich I (1995) Superoxide radical and superoxide dismutases. Annu Rev Biochem 64:97–112
Fuangthong M, Herbig AF, Bsat N, Helmann JD (2002) Regulation of the Bacillus subtilis fur and perR genes by PerR: not all members of the PerR regulon are peroxide inducible. J Bacteriol 184(12):3276–3286. https://doi.org/10.1128/JB.184.12.3276-3286.2002
Gaballa A, Helmann JD (2002) A peroxide-induced zinc uptake system plays an important role in protection against oxidative stress in Bacillus subtilis. Mol Microbiol. https://doi.org/10.1046/j.1365-2958.2002.03068.x
Gaballa A, Newton GL, Antelmann H et al (2010) Biosynthesis and functions of bacillithiol, a major low-molecular-weight thiol in bacilli. Proc Natl Acad Sci U S A. https://doi.org/10.1073/pnas.1000928107
Gardner PR, Gardner AM, Martin LA, Salzman AL (1998) Nitric oxide dioxygenase: an enzymic function for flavohemoglobin. Proc Natl Acad Sci U S A. https://doi.org/10.1073/pnas.95.18.10378
Garénaux A, Guillou S, Ermel G et al (2008) Role of the Cj1371 periplasmic protein and the Cj0355c two-component regulator in the Campylobacter jejuni NCTC 11168 response to oxidative stress caused by paraquat. Res Microbiol. https://doi.org/10.1016/j.resmic.2008.08.001
Gaupp R, Ledala N, Somerville GA (2012) Staphylococcal response to oxidative stress. Front Cell Infect Microbiol. https://doi.org/10.3389/fcimb.2012.00033
Gonçalves VL, Nobre LS, Vicente JB et al (2006) Flavohemoglobin requires microaerophilic conditions for nitrosative protection of Staphylococcus aureus. FEBS Lett. https://doi.org/10.1016/j.febslet.2006.02.039
Gort AS, Imlay JA (1998) Balance between endogenous superoxide stress and antioxidant defenses. J Bacteriol. https://doi.org/10.1128/jb.180.6.1402-1410.1998
Götz F, Bannerman T, Schleifer K-H (2006) The genera Staphylococcus and Macrococcus. Prokaryotes 2006:5–75
Grant KA, Park SF (1995) Molecular characterization of katA from Campylobacter jejuni and generation of a catalase-deficient mutant of Campylobacter coli by interspecific allelic exchange. Microbiology. https://doi.org/10.1099/13500872-141-6-1369
Greenberg JT, Monach P, Chou JH et al (1990) Positive control of a global antioxidant defense regulon activated by superoxide-generating agents in Escherichia coli. Proc Natl Acad Sci U S A. https://doi.org/10.1073/pnas.87.16.6181
Gu M, Imlay JA (2011) The SoxRS response of Escherichia coli is directly activated by redox-cycling drugs rather than by superoxide. Mol Microbiol. https://doi.org/10.1111/j.1365-2958.2010.07520.x
Gundogdu O, Mills DC, Elmi A et al (2011) The Campylobacter jejuni transcriptional regulator Cj1556 plays a role in the oxidative and aerobic stress response and is important for bacterial survival in vivo. J Bacteriol. https://doi.org/10.1128/JB.05189-11
Guo MS, Gross CA (2014) Stress-induced remodeling of the bacterial proteome. Curr Biol 24(10):R424–R434
Gutteridge JMC, Rowley DA, Halliwell B (1982) Superoxide-dependent formation of hydroxyl radicals and lipid peroxidation in the presence of iron salts. Detection of ‘catalytic’ iron and anti-oxidant activity in extracellular fluids. Biochem J. https://doi.org/10.1042/bj2060605
Hall-Stoodley L, Stoodley P (2005) Biofilm formation and dispersal and the transmission of human pathogens. Trends Microbiol. https://doi.org/10.1016/j.tim.2004.11.004
Hazeleger WC, Wouters JA, Rombouts FM, Abee T (1998) Physiological activity of Campylobacter jejuni far below the minimal growth temperature. Appl Environ Microbiol. https://doi.org/10.1128/aem.64.10.3917-3922.1998
Hendrixson DR, Akerley BJ, DiRita VJ (2001) Transposon mutagenesis of Campylobacter jejuni identifies a bipartite energy taxis system required for motility. Mol Microbiol. https://doi.org/10.1046/j.1365-2958.2001.02376.x
Hengge R (2008) The two-component network and the general stress sigma factor RpoS (σS) in Escherichia coli. Adv Exp Med Biol 631:40–53
Hill C, O’Driscoll B, Booth I (1995) Acid adaptation and food poisoning microorganisms. Int J Food Microbiol. https://doi.org/10.1016/0168-1605(95)00060-7
Hochgräfe F, Mostertz J, Pöther DC et al (2007) S-cysteinylation is a general mechanism for thiol protection of Bacillus subtilis proteins after oxidative stress. J Biol Chem. https://doi.org/10.1074/jbc.C700105200
Horsburgh MJ, Clements MO, Crossley H et al (2001a) PerR controls oxidative stress resistance and iron storage proteins and is required for virulence in Staphylococcus aureus. Infect Immun. https://doi.org/10.1128/IAI.69.6.3744-3754.2001
Horsburgh MJ, Ingham E, Foster SJ (2001b) In Staphylococcus aureus, fur is an interactive regulator with PerR, contributes to virulence, and is necessary for oxidative stress resistance through positive regulation of catalase and iron homeostasis. J Bacteriol. https://doi.org/10.1128/JB.183.2.468-475.2001
Huie RE, Padmaja S (1993) The reaction of no with superoxide. Free Radic Res. https://doi.org/10.3109/10715769309145868
Humphries KM, Szweda LI (1998) Selective inactivation of α-ketoglutarate dehydrogenase and pyruvate dehydrogenase: reaction of lipoic acid with 4-hydroxy-2-nonenal. Biochemistry. https://doi.org/10.1021/bi981512h
Huyen NTT, Eiamphungporn W, Mäder U et al (2009) Genome-wide responses to carbonyl electrophiles in Bacillus subtilis: control of the thiol-dependent formaldehyde dehydrogenase AdhA and cysteine proteinase YraA by the MerR-family regulator YraB (AdhR). Mol Microbiol. https://doi.org/10.1111/j.1365-2958.2008.06568.x
Hwang S, Jeon B, Yun J, Ryu S (2011a) Roles of RpoN in the resistance of Campylobacter jejuni under various stress conditions. BMC Microbiol. https://doi.org/10.1186/1471-2180-11-207
Hwang S, Kim M, Ryu S, Jeon B (2011b) Regulation of oxidative stress response by CosR, an essential response regulator in Campylobacter jejuni. PLoS One. https://doi.org/10.1371/journal.pone.0022300
Hwang S, Ryu S, Jeon B (2013) Roles of the superoxide dismutase SodB and the catalase KatA in the antibiotic resistance of Campylobacter jejuni. J Antibiot (Tokyo). https://doi.org/10.1038/ja.2013.20
Imlay JA (2003) Pathways of oxidative damage. Annu Rev Microbiol 57:395–418
Imlay JA (2008) Cellular defenses against superoxide and hydrogen peroxide. Annu Rev Biochem 77:755–776
Imlay JA (2015) Diagnosing oxidative stress in bacteria: not as easy as you might think. Curr Opin Microbiol 24:124–131
Ingavale SS, Van Wamel W, Cheung AL (2003) Characterization of RAT, an autolysis regulator in Staphylococcus aureus. Mol Microbiol. https://doi.org/10.1046/j.1365-2958.2003.03503.x
Jahan S (2012) Epidemiology of foodborne illness. Sci Heal Soc Asp Food Ind 1:321–342
Jang S, Imlay JA (2007) Micromolar intracellular hydrogen peroxide disrupts metabolism by damaging iron-sulfur enzymes. J Biol Chem. https://doi.org/10.1074/jbc.M607646200
Jenkins DE, Schultz JE, Matin A (1988) Starvation-induced cross protection against heat or H2 O2 challenge in Escherichia coli. J Bacteriol 170(9):3910–3914. https://doi.org/10.1128/jb.170.9.3910-3914.1988
Jenkins DE, Chaisson SA, Matin A (1990) Starvation-induced cross protection against osmotic challenge in Escherichia coli. J Bacteriol. https://doi.org/10.1128/jb.172.5.2779-2781.1990
Johansson J, Freitag NE (2019) Regulation of Listeria monocytogenes virulence. Microbiol Spectr:836–850
Johnson M, Sengupta M, Purves J et al (2011) Fur is required for the activation of virulence gene expression through the induction of the sae regulatory system in Staphylococcus aureus. Int J Med Microbiol. https://doi.org/10.1016/j.ijmm.2010.05.003
Justino MC, Almeida CC, Gonçalves VL et al (2006) Escherichia coli YtfE is a di-iron protein with an important function in assembly of iron-sulphur clusters. FEMS Microbiol Lett. https://doi.org/10.1111/j.1574-6968.2006.00179.x
Kaakoush NO, Baar C, MacKichan J et al (2009) Insights into the molecular basis of the microaerophily of three Campylobacterales: a comparative study. Antonie van Leeuwenhoek. https://doi.org/10.1007/s10482-009-9370-3
Kalmokoff M, Lanthier P, Tremblay TL et al (2006) Proteomic analysis of Campylobacter jejuni 11168 biofilms reveals a role for the motility complex in biofilm formation. J Bacteriol. https://doi.org/10.1128/JB.01975-05
Karavolos MH, Horsburgh M, Ingham E, Foster SJ (2003) Role and regulation of the superoxide dismutases of Staphylococcus aureus. Microbiology. https://doi.org/10.1099/mic.0.26353-0
Kehres DG, Maguire ME (2003) Emerging themes in manganese transport, biochemistry and pathogenesis in bacteria. FEMS Microbiol Rev 27(2–3):263–290
Keyer K, Imlay JA (1996) Superoxide accelerates DNA damage by elevating free-iron levels. Proc Natl Acad Sci USA 93(24):13635–13640. https://doi.org/10.1073/pnas.93.24.13635
Kim J, Yoshimura SH, Hizume K et al (2004) Fundamental structural units of the Escherichia coli nucleoid revealed by atomic force microscopy. Nucleic Acids Res 32(6):1982–1992. https://doi.org/10.1093/nar/gkh512
Kim YH, Lee Y, Kim S et al (2006) The role of periplasmic antioxidant enzymes (superoxide dismutase and thiol peroxidase) of the Shiga toxin-producing Escherichia coli O157:H7 in the formation of biofilms. Proteomics. https://doi.org/10.1002/pmic.200600320
Kim M, Hwang S, Ryu S, Jeon B (2011) Regulation of perr expression by iron and perr in Campylobacter jejuni. J Bacteriol. https://doi.org/10.1128/JB.05493-11
Kim JC, Oh E, Kim J, Jeon B (2015) Regulation of oxidative stress resistance in Campylobacter jejuni, a microaerophilic foodborne pathogen. Front Microbiol 6:751
Klebanoff SJ (2005) Myeloperoxidase: friend and foe. J Leukoc Biol. https://doi.org/10.1189/jlb.1204697
Kohanski MA, Dwyer DJ, Hayete B et al (2007) A common mechanism of cellular death induced by bactericidal antibiotics. Cell. https://doi.org/10.1016/j.cell.2007.06.049
Kong IS, Bates TC, Hülsmann A et al (2004) Role of catalase and oxyR in the viable but nonculturable state of Vibrio vulnificus. FEMS Microbiol Ecol. https://doi.org/10.1016/j.femsec.2004.06.004
Korshunov S, Imlay JA (2010) Two sources of endogenous hydrogen peroxide in Escherichia coli. Mol Microbiol. https://doi.org/10.1111/j.1365-2958.2010.07059.x
Larsson JT, Rogstam A, Von Wachenfeldt C (2007) YjbH is a novel negative effector of the disulphide stress regulator, Spx, in Bacillus subtilis. Mol Microbiol. https://doi.org/10.1111/j.1365-2958.2007.05949.x
Lee JW, Helmann JD (2006) The PerR transcription factor senses H2O2 by metal-catalysed histidine oxidation. Nature 440(7082):363–367. https://doi.org/10.1038/nature04537
Lee H, Ma R, Grimm MC et al (2014) Examination of the anaerobic growth of Campylobacter concisus strains. Int J Microbiol 2014:476047
Lindahl T (1979) DNA glycosylases, endonucleases for Apurinic/Apyrimidinic sites, and base excision-repair. Prog Nucleic Acid Res Mol Biol. https://doi.org/10.1016/S0079-6603(08)60800-4
Lindsay JA (1997) Chronic sequelae of foodborne disease. Emerg Infect Dis 3:443
Liu GY, Essex A, Buchanan JT, et al (2005) Staphylococcus aureus golden pigment impairs neutrophil killing and promotes virulence through its antioxidant activity. J Exp Med. https://doi.org/10.1084/jem.20050846
Liu Z, Yang M, Peterfreund GL, et al (2011) Vibrio cholerae anaerobic induction of virulence gene expression is controlled by thiol-based switches of virulence regulator AphB. Proc Natl Acad Sci 108:810–815
Lu J, Holmgren A (2014) The thioredoxin superfamily in oxidative protein folding. Antioxidants Redox Signals 21(3):457–470
Lushchak VI (2011) Adaptive response to oxidative stress: bacteria, fungi, plants and animals. Comp Biochem Physiol C Toxicol Pharmacol 153(2):175–190
Mack A, Hutton R, Olsen L et al (2012) Improving food safety through a one health approach: workshop summary. National Academies Press, New York
Macomber L, Imlay JA (2009) The iron-sulfur clusters of dehydratases are primary intracellular targets of copper toxicity. Proc Natl Acad Sci U S A. https://doi.org/10.1073/pnas.0812808106
Mandelker L (2011) Oxidative stress, free radicals, and cellular damage. In: Studies on veterinary medicine. Springer, New York, pp 1–17
Messner KR, Imlay JA (1999) The identification of primary sites of superoxide and hydrogen peroxide formation in the aerobic respiratory chain and sulfite reductase complex of Escherichia coli. J Biol Chem. https://doi.org/10.1074/jbc.274.15.10119
Mizunoe Y, Wai SN, Takade A, Yoshida SI (1999) Restoration of culturability of starvation-stressed and low-temperature-stressed Escherichia coli O157 cells by using H2O2-degrading compounds. Arch Microbiol 172(1):63–67. https://doi.org/10.1007/s002030050741
Mols M, Abee T (2011) Primary and secondary oxidative stress in Bacillus. Environ Microbiol. https://doi.org/10.1111/j.1462-2920.2011.02433.x
Mols M, Pier I, Zwietering MH, Abee T (2009) The impact of oxygen availability on stress survival and radical formation of Bacillus cereus. Int J Food Microbiol. https://doi.org/10.1016/j.ijfoodmicro.2009.09.002
Moskovitz J, Weissbach H, Brot N (1996) Cloning and expression of a mammalian gene involved in the reduction of methionine sulfoxide residues in proteins. Proc Natl Acad Sci U S A. https://doi.org/10.1073/pnas.93.5.2095
Mostertz J, Scharf C, Hecker M, Homuth G (2004) Transcriptome and proteome analysis of Bacillus subtilis gene expression in response to superoxide and peroxide stress. Microbiology. https://doi.org/10.1099/mic.0.26665-0
Müller-Herbst S, Wüstner S, Mühlig A et al (2014) Identification of genes essential for anaerobic growth of Listeria monocytogenes. Microbiology 160:752–765
Nachin L, Loiseau L, Expert D, Barras F (2003) SufC: an unorthodox cytoplasmic ABC/ATPase required for [Fe-S] biogenesis under oxidative stress. EMBO J 22:427–437
Nauseef WM (2004) Assembly of the phagocyte NADPH oxidase. Histochem Cell Biol 22(3):427–437
Newell DG, Koopmans M, Verhoef L et al (2010) Food-borne diseases—the challenges of 20 years ago still persist while new ones continue to emerge. Int J Food Microbiol 139:S3–S15
Niga T, Yoshida H, Hattori H et al (1997) Cloning and sequencing of a novel gene (recG) that affects the quinolone susceptibility of Staphylococcus aureus. Antimicrob Agents Chemother 41(8):1770–1774. https://doi.org/10.1128/aac.41.8.1770
Ole Leichert LI, Scharf C, Hecker M (2003) Global characterization of disulfide stress in Bacillus subtilis. J Bacteriol. https://doi.org/10.1128/JB.185.6.1967-1975.2003
Oliver HF, Orsi RH, Wiedmann M, Boor KJ (2010) Listeria monocytogenes σB has a small core regulon and a conserved role in virulence but makes differential contributions to stress tolerance across a diverse collection of strains. Appl Environ Microbiol 76(13):4216–4232. https://doi.org/10.1128/AEM.00031-10
Palyada K, Sun YQ, Flint A et al (2009) Characterization of the oxidative stress stimulon and PerR regulon of Campylobacter jejuni. BMC Genomics. https://doi.org/10.1186/1471-2164-10-481
Pané-Farré J, Jonas B, Förstner K et al (2006) The σB regulon in Staphylococcus aureus and its regulation. Int J Med Microbiol. https://doi.org/10.1016/j.ijmm.2005.11.011
Park S, Imlay JA (2003) High levels of intracellular cysteine promote oxidative DNA damage by driving the Fenton reaction. J Bacteriol. https://doi.org/10.1128/JB.185.6.1942-1950.2003
Park S, You X, Imlay JA (2005) Substantial DNA damage from submicromolar intracellular hydrogen peroxide detected in Hpx- mutants of Escherichia coli. Proc Natl Acad Sci U S A. https://doi.org/10.1073/pnas.0502051102
Parkhill J, Wren BW, Mungall K et al (2000) The genome sequence of the food-borne pathogen Campylobacter jejuni reveals hypervariable sequences. Nature. https://doi.org/10.1038/35001088
Parsek MR, Singh PK (2003) Bacterial biofilms: an emerging link to disease pathogenesis. Annu Rev Microbiol 57:677–701
Passalacqua KD, Bergman NH, Jung YL et al (2007) The global transcriptional responses of Bacillus anthracis sterne (34F2) and a ΔsodA1 mutant to paraquat reveal metal ion homeostasis imbalances during endogenous superoxide stress. J Bacteriol 189:3996–4013. https://doi.org/10.1128/JB.00185-07
Pesci EC, Cottle DL, Pickett CL (1994) Genetic, enzymatic, and pathogenic studies of the iron superoxide dismutase of Campylobacter jejuni. Infect Immun. https://doi.org/10.1128/iai.62.7.2687-2694.1994
Pomposiello PJ, Bennik MHJ, Demple B (2001) Genome-wide transcriptional profiling of the Escherichia coli responses to superoxide stress and sodium salicylate. J Bacteriol. https://doi.org/10.1128/JB.183.13.3890-3902.2001
Poole LB (2005) Bacterial defenses against oxidants: mechanistic features of cysteine-based peroxidases and their flavoprotein reductases. Arch Biochem Biophys 433(1):240–254
Poole K (2012) Bacterial stress responses as determinants of antimicrobial resistance. J Antimicrob Chemother 67:2069–2089
Poole RK, Hughes MN (2000) New functions for the ancient globin family: bacterial responses to nitric oxide and nitrosative stress. Mol Microbiol 36:775–783
Poole LB, Reynolds CM, Wood ZA et al (2000) AhpF and other NADH: peroxiredoxin oxidoreductases, homologues of low Mr thioredoxin reductase. Eur J Biochem 267:6126–6133
Poyart C, Berche P, Trieu-cuot P (1995) Characterization of superoxide dismutase genes from gram-positive bacteria by polymerase chain reaction using degenerate primers. FEMS Microbiol Lett. https://doi.org/10.1016/0378-1097(95)00232-T
Puig S, Thiele DJ (2002) Molecular mechanisms of copper uptake and distribution. Curr Opin Chem Biol 6(2):171–180
Reuter M, Mallett A, Pearson BM, Van Vliet AHM (2010) Biofilm formation by Campylobacter jejuni is increased under aerobic conditions. Appl Environ Microbiol. https://doi.org/10.1128/AEM.01878-09
Richardson AR, Dunman PM, Fang FC (2006) The nitrosative stress response of Staphylococcus aureus is required for resistance to innate immunity. Mol Microbiol. https://doi.org/10.1111/j.1365-2958.2006.05290.x
Rossetto O, Pirazzini M, Montecucco C (2014) Botulinum neurotoxins: genetic, structural and mechanistic insights. Nat Rev Microbiol 12(8):535–549
Rukmana A, Morimoto T, Takahashi H et al (2009) Assessment of transcriptional responses of Bacillus subtilis cells to the antibiotic enduracidin, which interferes with cell wall synthesis, using a high-density tiling chip. Genes Genet Syst. https://doi.org/10.1266/ggs.84.253
Sanz R, Marín I, Ruiz-Santa-Quiteria JA et al (2000) Catalase deficiency in Staphylococcus aureus subsp. anaerobius is associated with natural loss-of-function mutations within the structural gene. Microbiology 146(2):465–475. https://doi.org/10.1099/00221287-146-2-465
Schellhorn HE (2014) Elucidating the function of the RpoS regulon. Future Microbiol 9(4):497–507
Sewell D, Allen SCH, Phillips CA (2015) Oxygen limitation induces acid tolerance and impacts simulated gastro-intestinal transit in Listeria monocytogenes J0161. Gut Pathog 7:1–5
Shatalin K, Gusarov I, Avetissova E et al (2008) Bacillus anthracis-derived nitric oxide is essential for pathogen virulence and survival in macrophages. Proc Natl Acad Sci USA 105(3):1009–1013. https://doi.org/10.1073/pnas.0710950105
Shaw MR, Zavaleta ES, Chiariello NR et al (2002) Grassland responses to global environmental changes suppressed by elevated CO2. Science. https://doi.org/10.1126/science.1075312
Sheikh MA, Taylor GL (2009) Crystal structure of the Vibrio cholerae ferric uptake regulator (fur) reveals insights into metal co-ordination. Mol Microbiol 72(5):1208–1220. https://doi.org/10.1111/j.1365-2958.2009.06718.x
Shibutani S, Takeshita M, Grollman AP (1991) Insertion of specific bases during DNA synthesis past the oxidation-damaged base 8-oxodG. Nature. https://doi.org/10.1038/349431a0
Sung JS, Mosbaugh DW (2003) Escherichia coli uracil- and ethenocytosine-initiated base excision DNA repair: rate-limiting step and patch size distribution. Biochemistry. https://doi.org/10.1021/bi027115v
Suzuki T, Murai T, Fukuda I et al (1994) Identification and characterization of a chromosomal virulence gene, vacJ, required for intercellular spreading of Shigella flexneri. Mol Microbiol 11(1):31–41. https://doi.org/10.1111/j.1365-2958.1994.tb00287.x
Suzuki H, Matsuzaki J, Hibi T (2010) Ghrelin and oxidative stress in gastrointestinal tract. J Clin Biochem Nutr 48(2):122–125
Suzuki H, Nishizawa T, Tsugawa H et al (2011) Roles of oxidative stress in stomach disorders. J Clin Biochem Nutr 50(1):35–39
Svensson SL, Davis LM, MacKichan JK et al (2009) The CprS sensor kinase of the zoonotic pathogen Campylobacter jejuni influences biofilm formation and is required for optimal chick colonization. Mol Microbiol. https://doi.org/10.1111/j.1365-2958.2008.06534.x
Tao K, Fujita N, Ishihama A (1993) Involvement of the RNA polymerase α subunit C-terminal region in co-operative interaction and transcriptional activation with OxyR protein. Mol Microbiol. https://doi.org/10.1111/j.1365-2958.1993.tb01176.x
Van Schaik W, Abee T (2005) The role of σB in the stress response of gram-positive bacteria - targets for food preservation and safety. Curr Opin Biotechnol 16(2):218–224
Van Vliet AHM, Wooldridge KG, Ketley JM (1998) Iron-responsive gene regulation in a Campylobacter jejuni fur mutant. J Bacteriol 180(20):5291–5298. https://doi.org/10.1128/jb.180.20.5291-5298.1998
Van Vliet AHM, Baillon MLA, Penn CW, Ketley JM (1999) Campylobacter jejuni contains two fur homologs: characterization of iron-responsive regulation of peroxide stress defense genes by the PerR repressor. J Bacteriol. https://doi.org/10.1128/jb.181.20.6371-6376.1999
Van Vliet AHM, Baillon MLA, Penn CW, Ketley JM (2001) The iron-induced ferredoxin FdxA of Campylobacter jejuni is involved in aerotolerance. FEMS Microbiol Lett. https://doi.org/10.1016/S0378-1097(01)00067-2
Van Vliet AHM, Ketley JM, Park SF, Penn CW (2002) The role of iron in Campylobacter gene regulation, metabolism and oxidative stress defense. FEMS Microbiol Rev. 26(2):173–186
Vasudevan SG, Armarego WLF, Shawl DC et al (1991) Isolation and nucleotide sequence of the hmp gene that encodes a haemoglobin-like protein in Escherichia coli K-12. MGG Mol Gen Genet. https://doi.org/10.1007/BF00273586
Vergara-Irigaray M, Fookes MC, Thomson NR, Tang CM (2014) RNA-seq analysis of the influence of anaerobiosis and FNR on Shigella flexneri. BMC Genomics 15:1–22
Verly WG, Paquette Y (1972) An endonuclease for depurinated DNA in Escherichia coli B. Can J Biochem 50:217–224
Vido K, Diemer H, Van Dorsselaer A et al (2005) Roles of thioredoxin reductase during the aerobic life of Lactococcus lactis. J Bacteriol. https://doi.org/10.1128/JB.187.2.601-610.2005
Vogt W (1995) Oxidation of methionyl residues in proteins: tools, targets, and reversal. Free Radic Biol Med 18(1):93–105
Wagner D, Maser J, Lai B et al (2005) Elemental analysis of Mycobacterium avium-, Mycobacterium tuberculosis-, and Mycobacterium smegmatis- containing phagosomes indicates pathogen-induced microenvironments within the host Cell’s endosomal system. J Immunol. https://doi.org/10.4049/jimmunol.174.3.1491
Wallace N, Newton E, Abrams E et al (2017) Metabolic determinants in Listeria monocytogenes anaerobic listeriolysin O production. Arch Microbiol 199:827–837
West NJ, Obernosterer I, Zemb O, Lebaron P (2008) Major differences of bacterial diversity and activity inside and outside of a natural iron-fertilized phytoplankton bloom in the Southern Ocean. Environ Microbiol 10:738–756
Whiteley AT, Ruhland BR, Edrozo MB, Reniere ML (2017) A redox-responsive transcription factor is critical for pathogenesis and aerobic growth of Listeria monocytogenes. Infect Immun:85, e00978-16
Winter SE, Thiennimitr P, Winter MG et al (2010) Gut inflammation provides a respiratory electron acceptor for Salmonella. Nature 467:426–429
Winterbourn CC, Hawkins RE, Brian M, Carrell RW (1975) The estimation of red cell superoxide dismutase activity. J Lab Clin Med. https://doi.org/10.5555/uri:pii:0022214375904394
Wolf C, Hochgräfe F, Kusch H et al (2008) Proteomic analysis of antioxidant strategies of Staphylococcus aureus: diverse responses to different oxidants. Proteomics. https://doi.org/10.1002/pmic.200701062
Woodmansee AN, Imlay JA (2003) A mechanism by which nitric oxide accelerates the rate of oxidative DNA damage in Escherichia coli. Mol Microbiol. https://doi.org/10.1046/j.1365-2958.2003.03530.x
Wouters JA, Rombouts FM, Kuipers OP et al (2000) The role of cold-shock proteins in low-temperature adaptation of food-related bacteria. Syst Appl Microbiol 23(2):165–173
Xiong A, Jayaswal RK (1998) Molecular characterization of a chromosomal determinant conferring resistance to zinc and cobalt ions in Staphylococcus aureus. J Bacteriol. https://doi.org/10.1128/jb.180.16.4024-4029.1998
Yeeles JTP, Dillingham MS (2010) The processing of double-stranded DNA breaks for recombinational repair by helicase-nuclease complexes. DNA Repair (Amst) 9(3):276–285
Zheng M, Åslund F, Storz G (1998) Activation of the OxyR transcription factor by reversible disulfide bond formation. Science. https://doi.org/10.1126/science.279.5357.1718
Zheng M, Wang X, Templeton LJ et al (2001) DNA microarray-mediated transcriptional profiling of the Escherichia coli response to hydrogen peroxide. J Bacteriol. https://doi.org/10.1128/JB.183.15.4562-4570.2001
Author information
Authors and Affiliations
Corresponding author
Editor information
Editors and Affiliations
Rights and permissions
Copyright information
© 2022 The Author(s), under exclusive license to Springer Nature Switzerland AG
About this chapter
Cite this chapter
Rakhi, N.N., Bari, L., Rahaman, M.M. (2022). Response of Foodborne Pathogens to Oxidative Stress. In: Ding, T., Liao, X., Feng, J. (eds) Stress Responses of Foodborne Pathogens. Springer, Cham. https://doi.org/10.1007/978-3-030-90578-1_6
Download citation
DOI: https://doi.org/10.1007/978-3-030-90578-1_6
Published:
Publisher Name: Springer, Cham
Print ISBN: 978-3-030-90577-4
Online ISBN: 978-3-030-90578-1
eBook Packages: Biomedical and Life SciencesBiomedical and Life Sciences (R0)