PmtA functions as a ferrous iron and cobalt efflux pump in Streptococcus suis

References

• Turner AG, Ong CY, Walker MJ, et al. Transition metal homeostasis in Streptococcus pyogenes and Streptococcus pneumoniae. Adv Microb Physiol. 2017;70:123–191. doi: 10.1016/bs.ampbs.2017.01.002
   PubMed Web of Science ®Google Scholar
• Andreini C, Bertini I, Cavallaro G, et al. Metal ions in biological catalysis: from enzyme databases to general principles. J Biol Inorg Chem. 2008;13(8):1205–1218. doi: 10.1007/s00775-008-0404-5
   PubMed Web of Science ®Google Scholar
• Guilhen C, Taha MK, Veyrier FJ. Role of transition metal exporters in virulence: the example of Neisseria meningitidis. Front Cell Infect Microbiol. 2013;3:102. doi: 10.3389/fcimb.2013.00102
   PubMed Web of Science ®Google Scholar
• Honsa ES, Johnson MD, Rosch JW. The roles of transition metals in the physiology and pathogenesis of Streptococcus pneumoniae. Front Cell Infect Microbiol. 2013;3:92. doi: 10.3389/fcimb.2013.00092
   PubMed Web of Science ®Google Scholar
• Ong CL, Gillen CM, Barnett TC, et al. An antimicrobial role for zinc in innate immune defense against group A Streptococcus. J Infect Dis. 2014;209(10):1500–1508. doi: 10.1093/infdis/jiu053
   PubMed Web of Science ®Google Scholar
• Turner AG, Ong CLY, Gillen CM, et al. Manganese homeostasis in group A Streptococcus is critical for resistance to oxidative stress and virulence. mBio. 2015;6(2):e00278–15. doi: 10.1128/mBio.00278-15
   Web of Science ®Google Scholar
• Guan G, Pinochet-Barros A, Gaballa A, et al. Pfet, a P1B4-type ATPase, effluxes ferrous iron and protects Bacillus subtilis against iron intoxication. Mol Microbiol. 2015;98(4):787–803. doi: 10.1111/mmi.13158
   PubMed Web of Science ®Google Scholar
• Pi H, Patel SJ, Arguello JM, et al. The Listeria monocytogenes Fur-regulated virulence protein FrvA is an Fe(II) efflux P1B4-type ATPase. Mol Microbiol. 2016;100(6):1066–1079. doi: 10.1111/mmi.13368
   PubMed Web of Science ®Google Scholar
• Brenot A, Weston BF, Caparon MG. A PerR-regulated metal transporter (PmtA) is an interface between oxidative stress and metal homeostasis in Streptococcus pyogenes. Mol Microbiol. 2007;63(4):1185–1196. doi: 10.1111/j.1365-2958.2006.05577.x
   PubMed Web of Science ®Google Scholar
• VanderWal AR, Makthal N, Pinochet-Barros A, et al. Iron efflux by PmtA is critical for oxidative stress resistance and contributes significantly to group A Streptococcus virulence. Infect Immun. 2017;85(6):e00091–17. doi: 10.1128/IAI.00091-17
   PubMed Web of Science ®Google Scholar
• Turner AG, Ong CY, Djoko KY, et al. The PerR-regulated P1B-4-type ATPase (PmtA) acts as a ferrous iron efflux pump in Streptococcus pyogenes. Infect Immun. 2017;85(6):e00140–17. doi: 10.1128/IAI.00140-17
   PubMed Web of Science ®Google Scholar
• Lun ZR, Wang QP, Chen XG, et al. Streptococcus suis: an emerging zoonotic pathogen. Lancet Infect Dis. 2007;7(3):201–209. doi: 10.1016/S1473-3099(07)70001-4
   PubMed Web of Science ®Google Scholar
• Wertheim HFL, Nghia HDT, Taylor W, et al. Streptococcus suis: an emerging human pathogen. Clin Infect Dis. 2009;48(5):617–625. doi: 10.1086/596763
   PubMed Web of Science ®Google Scholar
• Goyette-Desjardins G, Auger JP, Xu J, et al. Streptococcus suis, an important pig pathogen and emerging zoonotic agent-an update on the worldwide distribution based on serotyping and sequence typing. Emerg Microbes Infect. 2014;3(6):e45.
   PubMed Web of Science ®Google Scholar
• Tohya M, Arai S, Tomida J, et al. Defining the taxonomic status of Streptococcus suis serotype 33: the proposal for Streptococcus ruminantium sp nov. Int J Syst Evol Micr. 2017;67(9):3660–3665. doi: 10.1099/ijsem.0.002204
   PubMed Web of Science ®Google Scholar
• Tang JQ, Wang CJ, Feng YJ, et al. Streptococcal toxic shock syndrome caused by Streptococcus suis serotype 2. Plos Med. 2006;3(5):668–676. doi: 10.1371/journal.pmed.0030151
   Web of Science ®Google Scholar
• Yu HJ, Jing HQ, Chen ZH, et al. Human Streptococcus suis outbreak, Sichuan, China. Emerg Infect Dis. 2006;12(6):914–920. doi: 10.3201/eid1206.051194
   PubMed Web of Science ®Google Scholar
• Anita N, Marta K, Peter S. Special case of purulent meningitis caused by Streptococcus suis. case report. Orv Hetil. 2019;160(1):30–34. doi: 10.1556/650.2019.31243
   PubMed Web of Science ®Google Scholar
• Yanase T, Morii D, Kamio S, et al. The first report of human meningitis and pyogenic ventriculitis caused by Streptococcus suis: a case report. J Infect Chemother. 2018;24(8):669–673. doi: 10.1016/j.jiac.2018.01.009
   PubMed Web of Science ®Google Scholar
• Raberahona M, Rasoanandrasana S, Rahajamanana VL, et al. Novel Streptococcus suis sequence type 834 among humans, Madagascar. Emerg Infect Dis. 2018;24(2):391–392. doi: 10.3201/eid2402.171138
   PubMed Web of Science ®Google Scholar
• Gomez-Torres J, Nimir A, Cluett J, et al. Human case of Streptococcus suis disease, Ontario, Canada. Emerg Infect Dis. 2017;23(12):2107–2109. doi: 10.3201/eid2312.171005
   PubMed Web of Science ®Google Scholar
• Rajahram GS, Hameed AA, Menon J, et al. Case report: two human Streptococcus suis infections in Borneo, Sabah, Malaysia. BMC Infect Dis. 2017;17(1):188. doi: 10.1186/s12879-017-2294-z
   PubMed Web of Science ®Google Scholar
• Xu J, Zheng C, Cao M, et al. The manganese efflux system MntE contributes to the virulence of Streptococcus suis serotype 2. Microb Pathog. 2017;110:23–30. doi: 10.1016/j.micpath.2017.06.022
   PubMed Web of Science ®Google Scholar
• Niven DF, Ekins A. Iron content of Streptococcus suis and evidence for a dpr homologue. Can J Microbiol. 2001;47(5):412–416. doi: 10.1139/w01-027
   PubMed Web of Science ®Google Scholar
• Pulliainen AT, Kauko A, Haataja S, et al. Dps/Dpr ferritin-like protein: insights into the mechanism of iron incorporation and evidence for a central role in cellular iron homeostasis in Streptococcus suis. Mol Microbiol. 2005;57(4):1086–1100. doi: 10.1111/j.1365-2958.2005.04756.x
   PubMed Web of Science ®Google Scholar
• Teng L, Dong X, Zhou Y, et al. Draft genome sequence of hypervirulent and vaccine candidate Streptococcus suis strain SC19. Genome Announc. 2017;5(3):e01484–16. doi: 10.1128/genomeA.01484-16
   Google Scholar
• Bustin SA, Benes V, Garson JA, et al. The MIQE guidelines: minimum information for publication of quantitative real-time PCR experiments. Clin Chem. 2009;55(4):611–622. doi: 10.1373/clinchem.2008.112797
   PubMed Web of Science ®Google Scholar
• Livak KJ, Schmittgen TD. Analysis of relative gene expression data using real-time quantitative PCR and the 2(-Delta Delta C(T)) method. Methods. 2001;25(4):402–408. doi: 10.1006/meth.2001.1262
   PubMed Web of Science ®Google Scholar
• Takamatsu D, Osaki M, Sekizaki T. Thermosensitive suicide vectors for gene replacement in Streptococcus suis. Plasmid. 2001;46(2):140–148. doi: 10.1006/plas.2001.1532
   PubMed Web of Science ®Google Scholar
• Takamatsu D, Osaki M, Sekizaki T. Construction and characterization of Streptococcus suis-Escherichia coli shuttle cloning vectors. Plasmid. 2001;45(2):101–113. doi: 10.1006/plas.2000.1510
   PubMed Web of Science ®Google Scholar
• Arguello JM. Identification of ion-selectivity determinants in heavy-metal transport P1B-type ATPases. J Membr Biol. 2003;195(2):93–108. doi: 10.1007/s00232-003-2048-2
   PubMed Web of Science ®Google Scholar
• Arguello JM, Gonzalez-Guerrero M, Raimunda D. Bacterial transition metal P1B-ATPases: transport mechanism and roles in virulence. Biochem. 2011;50(46):9940–9949. doi: 10.1021/bi201418k
   PubMed Web of Science ®Google Scholar
• Zhang T, Ding Y, Li T, et al. A Fur-like protein PerR regulates two oxidative stress response related operons dpr and metQIN in Streptococcus suis. BMC Microbiol. 2012;12:85. doi: 10.1186/1471-2180-12-85
   PubMed Web of Science ®Google Scholar
• Feng YJ, Li M, Zhang HM, et al. Functional definition and global regulation of Zur, a zinc uptake regulator in a Streptococcus suis serotype 2 strain causing streptococcal toxic shock syndrome. J Bacteriol. 2008;190(22):7567–7578. doi: 10.1128/JB.01532-07
   PubMed Web of Science ®Google Scholar
• Aranda J, Garrido ME, Fittipaldi N, et al. The cation-uptake regulators AdcR and Fur are necessary for full virulence of Streptococcus suis. Vet Microbiol. 2010;144(1–2):246–249. doi: 10.1016/j.vetmic.2009.12.037
   PubMed Web of Science ®Google Scholar
• Yeowell HN, White JR. Iron requirement in the bactericidal mechanism of streptonigrin. Antimicrob Agents Ch. 1982;22(6):961–968. doi: 10.1128/AAC.22.6.961
   PubMed Web of Science ®Google Scholar
• Aranda J, Cortes P, Garrido ME, et al. Contribution of the FeoB transporter to Streptococcus suis virulence. Int Microbiol. 2009;12(2):137–143.
   PubMed Web of Science ®Google Scholar
• Schreur PJW, Rebel JMJ, Smits MA, et al. Troa of Streptococcus suis is required for manganese acquisition and full virulence. J Bacteriol. 2011;193(19):5073–5080. doi: 10.1128/JB.05305-11
   PubMed Web of Science ®Google Scholar
• Aranda J, Garrido ME, Fittipaldi N, et al. Protective capacities of cell surface-associated proteins of Streptococcus suis mutants deficient in divalent cation-uptake regulators. Microbiol. 2009;155(Pt 5):1580–1587. doi: 10.1099/mic.0.026278-0
   PubMed Web of Science ®Google Scholar
• Aranda J, Garrido ME, Cortes P, et al. Analysis of the protective capacity of three Streptococcus suis proteins induced under divalent-cation-limited conditions. Infect Immun. 2008;76(4):1590–1598. doi: 10.1128/IAI.00987-07
   PubMed Web of Science ®Google Scholar
• Manzoor I, Shafeeq S, Afzal M, et al. The regulation of the AdcR regulon in Streptococcus pneumoniae depends both on Zn2+- and Ni2+-availability. Front Cell Infect Microbiol. 2015;5:91. doi: 10.3389/fcimb.2015.00091
   PubMed Web of Science ®Google Scholar
• Barras F, Fontecave M. Cobalt stress in Escherichia coli and Salmonella enterica: molecular bases for toxicity and resistance. Metallomics. 2011;3(11):1130–1134. doi: 10.1039/c1mt00099c
   PubMed Web of Science ®Google Scholar
• Pi H, Helmann JD. Ferrous iron efflux systems in bacteria. Metallomics. 2017;9(7):840–851. doi: 10.1039/C7MT00112F
   PubMed Web of Science ®Google Scholar
• Frawley ER, Crouch ML, Bingham-Ramos LK, et al. Iron and citrate export by a major facilitator superfamily pump regulates metabolism and stress resistance in Salmonella Typhimurium. Proc Natl Acad Sci U S A. 2013;110(29):12054–12059. doi: 10.1073/pnas.1218274110
   PubMed Web of Science ®Google Scholar
• Arenas J, Bossers-de Vries R, Harders-Westerveen J, et al. In vivo transcriptomes of Streptococcus suis reveal genes required for niche-specific adaptation and pathogenesis. Virulence. 2019;10(1):334–351. doi: 10.1080/21505594.2019.1599669
   PubMed Web of Science ®Google Scholar