BMC Microbiology | |
A ferritin-like protein with antioxidant activity in Ureaplasma urealyticum | |
Yimou Wu3  Xiaoxing You3  Chuanhao Jiang2  Hongliang Chen1  Ranhui Li3  Guozhi Dai1  | |
[1] Department of Clinical Laboratory, The First People’s Hospital of Chenzhou, Chenzhou 42300, Hunan, China;Institute of Pathogenic Biology, University of South China, Changsheng road 28, Hengyang 421001, Hunan, China;Hunan Province Cooperative Innovation Center for Molecular Target New Drug Study, Hengyang 421001, Hunan, China | |
关键词: Antioxidant activity; Reactive oxygen species; Ferritin; Ureaplasma urealyticum; | |
Others : 1227618 DOI : 10.1186/s12866-015-0485-6 |
|
received in 2014-12-22, accepted in 2015-07-13, 发布年份 2015 | |
【 摘 要 】
Background
Ureaplasma urealyticum is a major pathogen associated with many diseases. The ability of U. urealyticum to protect itself from oxidative stress is likely to be important for its pathogenesis and survival, but its oxidative stress tolerance mechanisms remain unclear. This study investigates the antioxidant activity of a ferritin-like protein from U. urealyticum.
Results
The uuferritin gene, which was up regulated when U. urealyticum was subjected to oxidative stress, was cloned from U. urealyticum and the corresponding recombinant protein uuferritin was purified. Uuferritin protein reduced the levels of hydroxyl radicals generated by the Fenton reaction as a consequence of its ferroxidase activity, and thus the protein protected DNA from oxidative damage. Furthermore, oxidation-sensitive Escherichia coli mutants transformed with pTrc99a-uuferritin showed significantly improved tolerance to oxidative stress compared to E. coli mutants transformed with an empty pTrc99a vector.
Conclusions
The present work shows that uuferritin protein confers resistance to oxidative stress in vitro and in E. coli. The protective role of uuferritin provides a foundation for understanding the mechanisms of oxidative stress tolerance in U. urealyticum.
【 授权许可】
2015 Dai et al.
【 预 览 】
Files | Size | Format | View |
---|---|---|---|
20150929022800374.pdf | 1199KB | download | |
Fig. 4. | 27KB | Image | download |
Fig. 3. | 24KB | Image | download |
Fig. 2. | 42KB | Image | download |
Fig. 1. | 27KB | Image | download |
【 图 表 】
Fig. 1.
Fig. 2.
Fig. 3.
Fig. 4.
【 参考文献 】
- [1]Glass JI, Lefkowitz EJ, Glass JS, Heiner CR, Chen EY, Cassell GH. The complete sequence of the mucosal pathogen Ureaplasma urealyticum. Nature. 2000; 407(6805):757-762.
- [2]Waites KB, Schelonka RL, Xiao L, Grigsby PL, Novy MJ. Congenital and opportunistic infections: ureaplasma species and mycoplasma hominis. Semin Fetal Neonatal Med. 2009; 14(4):190-199.
- [3]Deetjen P, Maurer C, Rank A, Berlis A, Schubert S, Hoffmann R. Brain abscess caused by Ureaplasma urealyticum in an adult patient. J Clin Microbiol. 2014; 52(2):695-698.
- [4]Shimada Y, Ito S, Mizutani K, Sugawara T, Seike K, Tsuchiya T et al.. Bacterial loads of Ureaplasma urealyticum contribute to development of urethritis in men. Int J STD AIDS. 2014; 25(4):294-298.
- [5]Radonić A, Kovačević V, Markotić A, Škerk V, Turčić P, Škerk V. The clinical significance of Ureaplasma urealyticum in chronic prostatitis. J Chemother. 2009; 21(4):465-466.
- [6]Larsen B, Hwang J. Mycoplasma, Ureaplasma, and adverse pregnancy outcomes: a fresh look. Infect Dis Obstet Gynecol. 2010; 2010:521921.
- [7]Capoccia R, Greub G, Baud D. Ureaplasma urealyticum, Mycoplasma hominis and adverse pregnancy outcomes. Curr Opin Infect Dis. 2013; 26(3):231-240.
- [8]Zhang Q, Xiao Y, Zhuang W, Cheng B, Zheng L, Cai Y et al.. Effects of biovar I and biovar II of Ureaplasma urealyticum on sperm parameters, lipid peroxidation, and deoxyribonucleic acid damage in male infertility. Urology. 2014; 84(1):87-92.
- [9]Potts JM, Sharma R, Pasqualotto F, Nelson D, Hall G, Agarwal A. Association of Ureaplasma urealyticum with abnormal reactive oxygen species levels and absence of leukocytospermia. J Urol. 2000; 163(6):1775-1778.
- [10]Wang Y, Liang CL, Wu JQ, Xu C, Qin SX, Gao ES. Do Ureaplasma urealyticum infections in the genital tract affect semen quality? Asian J Androl. 2006; 8(5):562-568.
- [11]Fraczek M, Szumala-Kakol A, Jedrzejczak P, Kamieniczna M, Kurpisz M. Bacteria trigger oxygen radical release and sperm lipid peroxidation in in vitro model of semen inflammation. Fertil Steril. 2007; 88(4 Suppl):1076-1085.
- [12]Zhang ZH, Zhang HG, Dong Y, Han RR, Dai RL, Liu RZ. Ureaplasma urealyticum in male infertility in Jilin Province, North-east China, and its relationship with sperm morphology. J Int Med Res. 2011; 39(1):33-40.
- [13]Padmini E, Uthra V. Role of Ureaplasma urealyticum in altering the endothelial metal concentration during preeclampsia. Placenta. 2012; 33(4):304-411.
- [14]Padmini E, Uthra V, Lavanya S. HSP70 overexpression in response to ureaplasma urealyticum-mediated oxidative stress in preeclamptic placenta. Hypertens Pregnancy. 2011; 30(2):133-143.
- [15]Haas A, Goebel W. Microbial strategies to prevent oxygen-dependent killing by phagocytes. Free Radic Res Commun. 1992; 16(3):137-157.
- [16]Jenkins C, Samudrala R, Geary SJ, Djordjevic SP. Structural and functional characterization of an organic hydroperoxide resistance protein from Mycoplasma gallisepticum. J Bacteriol. 2008; 190(6):2206-2216.
- [17]Lu J, Holmgren A. The thioredoxin antioxidant system. Free Radic Biol Med. 2014; 66:75-87.
- [18]Marinho HS, Real C, Cyrne L, Soares H, Antunes F. Hydrogen peroxide sensing, signaling and regulation of transcription factors. Redox Biol. 2014; 2:535-562.
- [19]Rocha ER, Smith CJ. Transcriptional regulation of the Bacteroides fragilis ferritin gene (ftnA) by redox stress. Microbiology. 2004; 150(Pt 7):2125-2134.
- [20]Imlay JA. Cellular defenses against superoxide and hydrogen peroxide. Annu Rev Biochem. 2008; 77:755-776.
- [21]Chiancone E, Ceci P, Ilari A, Ribacchi F, Stefanini S. Iron and proteins for iron storage and detoxification. Biometals. 2004; 17(3):197-202.
- [22]Ekman M, Sandh G, Nenninger A, Oliveira P, Stensjo K. Cellular and functional specificity among ferritin-like proteins in the multicellular cyanobacterium Nostoc punctiforme. Environ Microbiol. 2014; 16(3):829-844.
- [23]Pulliainen AT, Kauko A, Haataja S, Papageorgiou AC, Finne J. 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.
- [24]Rocha ER, Smith CJ. Ferritin-like family proteins in the anaerobe Bacteroides fragilis: when an oxygen storm is coming, take your iron to the shelter. Biometals. 2013; 26(4):577-591.
- [25]Calhoun LN, Kwon YM. The ferritin-like protein Dps protects Salmonella enterica serotype Enteritidis from the Fenton-mediated killing mechanism of bactericidal antibiotics. Int J Antimicrob Agents. 2011; 37(3):261-265.
- [26]Takatsuka M, Osada-Oka M, Satoh EF, Kitadokoro K, Nishiuchi Y, Niki M et al.. A histone-like protein of mycobacteria possesses ferritin superfamily protein-like activity and protects against DNA damage by Fenton reaction. PLoS One. 2011; 6(6):e20985.
- [27]Grant RA, Filman DJ, Finkel SE, Kolter R, Hogle JM. The crystal structure of Dps, a ferritin homolog that binds and protects DNA. Nat Struct Biol. 1998; 5(4):294-303.
- [28]Crouse DT, Cassell GH, Waites KB, Foster JM, Cassady G. Hyperoxia potentiates Ureaplasma urealyticum pneumonia in newborn mice. Infect Immun. 1990; 58(11):3487-3493.
- [29]Li YH, Yan ZQ, Jensen JS, Tullus K, Brauner A. Activation of nuclear factor kappaB and induction of inducible nitric oxide synthase by Ureaplasma urealyticum in macrophages. Infect Immun. 2000; 68(12):7087-7093.
- [30]Liu G, Xu H, Zhang L, Zheng Y. Fe binding properties of two soybean (Glycine max L.) LEA4 proteins associated with antioxidant activity. Plant Cell Physiol. 2011; 52(6):994-1002.
- [31]Ishikawa T, Mizunoe Y, Kawabata S, Takade A, Harada M, Wai SN et al.. The iron-binding protein Dps confers hydrogen peroxide stress resistance to Campylobacter jejuni. J Bacteriol. 2003; 185(3):1010-1017.
- [32]Ko SH, Choi SW, Ye SK, Yoo S, Kim HS, Chung MH. Comparison of anti-oxidant activities of seventy herbs that have been used in Korean traditional medicine. Nutr Res Pract. 2008; 2(3):143-151.
- [33]Baba T, Ara T, Hasegawa M, Takai Y, Okumura Y, Baba M et al.. Construction of Escherichia coli K-12 in-frame, single-gene knockout mutants: the Keio collection. Mol Syst Biol. 2006; 2:2006 0008.
- [34]Park M, Yun ST, Hwang SY, Chun CI, Ahn TI. The dps gene of symbiotic “Candidatus Legionella jeonii” in Amoeba proteus responds to hydrogen peroxide and phagocytosis. J Bacteriol. 2006; 188(21):7572-7580.
- [35]Huergo LF, Rahman H, Ibrahimovic A, Day CJ, Korolik V. Campylobacter jejuni Dps protein binds DNA in the presence of iron or hydrogen peroxide. J Bacteriol. 2013; 195(9):1970-1978.
- [36]Nair S, Finkel SE. Dps protects cells against multiple stresses during stationary phase. J Bacteriol. 2004; 186(13):4192-4198.
- [37]Paralanov V, Lu J, Duffy LB, Crabb DM, Shrivastava S, Methe BA et al.. Comparative genome analysis of 19 Ureaplasma urealyticum and Ureaplasma parvum strains. BMC Microbiol. 2012; 12:88. BioMed Central Full Text
- [38]Ben-Menachem G, Himmelreich R, Herrmann R, Aharonowitz Y, Rottem S. The thioredoxin reductase system of mycoplasmas. Microbiology. 1997; 143(Pt 6):1933-1940.
- [39]Dhandayuthapani S, Blaylock MW, Bebear CM, Rasmussen WG, Baseman JB. Peptide methionine sulfoxide reductase (MsrA) is a virulence determinant in Mycoplasma genitalium. J Bacteriol. 2001; 183(19):5645-5650.
- [40]Andrews SC, Robinson AK, Rodriguez-Quinones F. Bacterial iron homeostasis. FEMS Microbiol Rev. 2003; 27(2–3):215-237.
- [41]Williams SM, Chandran AV, Vijayabaskar MS, Roy S, Balaram H, Vishveshwara S et al.. A histidine aspartate ionic lock gates the iron passage in miniferritins from Mycobacterium smegmatis. J Biol Chem. 2014; 289(16):11042-11058.
- [42]Hua CZ, Howard A, Malley R, Lu YJ. Effect of nonheme iron-containing ferritin Dpr in the stress response and virulence of pneumococci. Infect Immun. 2014; 82(9):3939-3947.
- [43]Kreuzer KN. DNA damage responses in prokaryotes: regulating gene expression, modulating growth patterns, and manipulating replication forks. Cold Spring Harb Perspect Biol. 2013; 5(11):a012674.
- [44]George NP, Ngo KV, Chitteni-Pattu S, Norais CA, Battista JR, Cox MM et al.. Structure and cellular dynamics of Deinococcus radiodurans single-stranded DNA (ssDNA)-binding protein (SSB)-DNA complexes. J Biol Chem. 2012; 287(26):22123-22132.
- [45]Martinez A, Kolter R. Protection of DNA during oxidative stress by the nonspecific DNA-binding protein Dps. J Bacteriol. 1997; 179(16):5188-5194.
- [46]Reon BJ, Nguyen KH, Bhattacharyya G, Grove A. Functional comparison of Deinococcus radiodurans Dps proteins suggests distinct in vivo roles. J Biol Chem. 2012; 447(3):381-391.
- [47]Wang G, Hong Y, Olczak A, Maier SE, Maier RJ. Dual roles of Helicobacter pylori NapA in inducing and combating oxidative stress. Infect Immun. 2006; 74(12):6839-6846.
- [48]Ceci P, Ilari A, Falvo E, Chiancone E. The Dps protein of Agrobacterium tumefaciens does not bind to DNA but protects it toward oxidative cleavage: x-ray crystal structure, iron binding, and hydroxyl-radical scavenging properties. J Biol Chem. 2003; 278(22):20319-20326.
- [49]Ceci P, Forte E, Di Cecca G, Fornara M, Chiancone E. The characterization of Thermotoga maritima ferritin reveals an unusual subunit dissociation behavior and efficient DNA protection from iron-mediated oxidative stress. Extremophiles. 2011; 15(3):431-439.
- [50]Glass JI, Assad-Garcia N, Alperovich N, Yooseph S, Lewis MR, Maruf M et al.. Essential genes of a minimal bacterium. Proc Natl Acad Sci U S A. 2006; 103(2):425-430.