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. 1995 Apr;63(4):1603–1607. doi: 10.1128/iai.63.4.1603-1607.1995

Isolation and identification of a glutathione peroxidase homolog gene, gpxA, present in Neisseria meningitidis but absent in Neisseria gonorrhoeae.

T D Moore 1, P F Sparling 1
PMCID: PMC173197  PMID: 7890429

Abstract

Antioxidant enzymes are thought to be important for the survival of pathogenic Neisseria species. We isolated a glutathione peroxidase-related gene (gpxA) from Neisseria meningitidis FAM20. The N. meningitidis glutathione peroxidase homolog was 49 to 57% identical to seven other glutathione peroxidase family members over a 49-amino-acid region which is conserved among various species. The gpxA sequence was present in all 7 meningococcal strains tested but absent in 10 gonococcal strains and 6 nonpathogenic neisserial strains as determined by Southern hybridization. The homology of gpxA to mammalian glutathione peroxidases and the presence of this gene specifically in the meningococcus suggest that it is important in the cellular metabolism or defense processes particular to this pathogen.

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Selected References

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  1. Alcorn T. M., Zheng H. Y., Gunther M. R., Hassett D. J., Cohen M. S. Variation in hydrogen peroxide sensitivity between different strains of Neisseria gonorrhoeae is dependent on factors in addition to catalase activity. Infect Immun. 1994 May;62(5):2138–2140. doi: 10.1128/iai.62.5.2138-2140.1994. [DOI] [PMC free article] [PubMed] [Google Scholar]
  2. Altschul S. F., Gish W., Miller W., Myers E. W., Lipman D. J. Basic local alignment search tool. J Mol Biol. 1990 Oct 5;215(3):403–410. doi: 10.1016/S0022-2836(05)80360-2. [DOI] [PubMed] [Google Scholar]
  3. Archibald F. S., Duong M. N. Superoxide dismutase and oxygen toxicity defenses in the genus Neisseria. Infect Immun. 1986 Feb;51(2):631–641. doi: 10.1128/iai.51.2.631-641.1986. [DOI] [PMC free article] [PubMed] [Google Scholar]
  4. Black J. R., Black W. J., Cannon J. G. Neisserial antigen H.8 is immunogenic in patients with disseminated gonococcal and meningococcal infections. J Infect Dis. 1985 Apr;151(4):650–657. doi: 10.1093/infdis/151.4.650. [DOI] [PubMed] [Google Scholar]
  5. Brigelius-Flohé R., Aumann K. D., Blöcker H., Gross G., Kiess M., Klöppel K. D., Maiorino M., Roveri A., Schuckelt R., Usani F. Phospholipid-hydroperoxide glutathione peroxidase. Genomic DNA, cDNA, and deduced amino acid sequence. J Biol Chem. 1994 Mar 11;269(10):7342–7348. [PubMed] [Google Scholar]
  6. Callahan H. L., Crouch R. K., James E. R. Helminth anti-oxidant enzymes: a protective mechanism against host oxidants? Parasitol Today. 1988 Aug;4(8):218–225. doi: 10.1016/0169-4758(88)90162-7. [DOI] [PubMed] [Google Scholar]
  7. Clark V. L., Campbell L. A., Palermo D. A., Evans T. M., Klimpel K. W. Induction and repression of outer membrane proteins by anaerobic growth of Neisseria gonorrhoeae. Infect Immun. 1987 Jun;55(6):1359–1364. doi: 10.1128/iai.55.6.1359-1364.1987. [DOI] [PMC free article] [PubMed] [Google Scholar]
  8. Cookson E., Blaxter M. L., Selkirk M. E. Identification of the major soluble cuticular glycoprotein of lymphatic filarial nematode parasites (gp29) as a secretory homolog of glutathione peroxidase. Proc Natl Acad Sci U S A. 1992 Jul 1;89(13):5837–5841. doi: 10.1073/pnas.89.13.5837. [DOI] [PMC free article] [PubMed] [Google Scholar]
  9. Criqui M. C., Jamet E., Parmentier Y., Marbach J., Durr A., Fleck J. Isolation and characterization of a plant cDNA showing homology to animal glutathione peroxidases. Plant Mol Biol. 1992 Feb;18(3):623–627. doi: 10.1007/BF00040684. [DOI] [PubMed] [Google Scholar]
  10. Dower W. J., Miller J. F., Ragsdale C. W. High efficiency transformation of E. coli by high voltage electroporation. Nucleic Acids Res. 1988 Jul 11;16(13):6127–6145. doi: 10.1093/nar/16.13.6127. [DOI] [PMC free article] [PubMed] [Google Scholar]
  11. Dyer D. W., McKenna W., Woods J. P., Sparling P. F. Isolation by streptonigrin enrichment and characterization of a transferrin-specific iron uptake mutant of Neisseria meningitidis. Microb Pathog. 1987 Nov;3(5):351–363. doi: 10.1016/0882-4010(87)90005-2. [DOI] [PubMed] [Google Scholar]
  12. Elkins C., Thomas C. E., Seifert H. S., Sparling P. F. Species-specific uptake of DNA by gonococci is mediated by a 10-base-pair sequence. J Bacteriol. 1991 Jun;173(12):3911–3913. doi: 10.1128/jb.173.12.3911-3913.1991. [DOI] [PMC free article] [PubMed] [Google Scholar]
  13. Epp O., Ladenstein R., Wendel A. The refined structure of the selenoenzyme glutathione peroxidase at 0.2-nm resolution. Eur J Biochem. 1983 Jun 1;133(1):51–69. doi: 10.1111/j.1432-1033.1983.tb07429.x. [DOI] [PubMed] [Google Scholar]
  14. Fahey R. C., Sundquist A. R. Evolution of glutathione metabolism. Adv Enzymol Relat Areas Mol Biol. 1991;64:1–53. doi: 10.1002/9780470123102.ch1. [DOI] [PubMed] [Google Scholar]
  15. Forestier C., Welch R. A. Nonreciprocal complementation of the hlyC and lktC genes of the Escherichia coli hemolysin and Pasteurella haemolytica leukotoxin determinants. Infect Immun. 1990 Mar;58(3):828–832. doi: 10.1128/iai.58.3.828-832.1990. [DOI] [PMC free article] [PubMed] [Google Scholar]
  16. Friedrich M. J., de Veaux L. C., Kadner R. J. Nucleotide sequence of the btuCED genes involved in vitamin B12 transport in Escherichia coli and homology with components of periplasmic-binding-protein-dependent transport systems. J Bacteriol. 1986 Sep;167(3):928–934. doi: 10.1128/jb.167.3.928-934.1986. [DOI] [PMC free article] [PubMed] [Google Scholar]
  17. Goodman S. D., Scocca J. J. Identification and arrangement of the DNA sequence recognized in specific transformation of Neisseria gonorrhoeae. Proc Natl Acad Sci U S A. 1988 Sep;85(18):6982–6986. doi: 10.1073/pnas.85.18.6982. [DOI] [PMC free article] [PubMed] [Google Scholar]
  18. Ho Y. S., Howard A. J., Crapo J. D. Nucleotide sequence of a rat glutathione peroxidase cDNA. Nucleic Acids Res. 1988 Jun 10;16(11):5207–5207. doi: 10.1093/nar/16.11.5207. [DOI] [PMC free article] [PubMed] [Google Scholar]
  19. Holland D., Ben-Hayyim G., Faltin Z., Camoin L., Strosberg A. D., Eshdat Y. Molecular characterization of salt-stress-associated protein in citrus: protein and cDNA sequence homology to mammalian glutathione peroxidases. Plant Mol Biol. 1993 Mar;21(5):923–927. doi: 10.1007/BF00027124. [DOI] [PubMed] [Google Scholar]
  20. Issartel J. P., Koronakis V., Hughes C. Activation of Escherichia coli prohaemolysin to the mature toxin by acyl carrier protein-dependent fatty acylation. Nature. 1991 Jun 27;351(6329):759–761. doi: 10.1038/351759a0. [DOI] [PubMed] [Google Scholar]
  21. Johnson S. R., Steiner B. M., Cruce D. D., Perkins G. H., Arko R. J. Characterization of a catalase-deficient strain of Neisseria gonorrhoeae: evidence for the significance of catalase in the biology of N. gonorrhoeae. Infect Immun. 1993 Apr;61(4):1232–1238. doi: 10.1128/iai.61.4.1232-1238.1993. [DOI] [PMC free article] [PubMed] [Google Scholar]
  22. KELLOGG D. S., Jr, PEACOCK W. L., Jr, DEACON W. E., BROWN L., PIRKLE D. I. NEISSERIA GONORRHOEAE. I. VIRULENCE GENETICALLY LINKED TO CLONAL VARIATION. J Bacteriol. 1963 Jun;85:1274–1279. doi: 10.1128/jb.85.6.1274-1279.1963. [DOI] [PMC free article] [PubMed] [Google Scholar]
  23. Meyer T. F., Mlawer N., So M. Pilus expression in Neisseria gonorrhoeae involves chromosomal rearrangement. Cell. 1982 Aug;30(1):45–52. doi: 10.1016/0092-8674(82)90010-1. [DOI] [PubMed] [Google Scholar]
  24. Mickelsen P. A., Sparling P. F. Ability of Neisseria gonorrhoeae, Neisseria meningitidis, and commensal Neisseria species to obtain iron from transferrin and iron compounds. Infect Immun. 1981 Aug;33(2):555–564. doi: 10.1128/iai.33.2.555-564.1981. [DOI] [PMC free article] [PubMed] [Google Scholar]
  25. Nachamkin I., Cannon J. G., Mittler R. S. Monoclonal antibodies against Neisseria gonorrhoeae: production of antibodies directed against a strain-specific cell surface antigen. Infect Immun. 1981 May;32(2):641–648. doi: 10.1128/iai.32.2.641-648.1981. [DOI] [PMC free article] [PubMed] [Google Scholar]
  26. Norrod P., Morse S. A. Absence of superoxide dismutase in some strains of Neisseria gonorrhoeae. Biochem Biophys Res Commun. 1979 Oct 29;90(4):1287–1294. doi: 10.1016/0006-291x(79)91176-8. [DOI] [PubMed] [Google Scholar]
  27. Roche C., Williams D. L., Khalife J., LePresle T., Capron A., Pierce R. J. Cloning and characterization of the gene encoding Schistosoma mansoni glutathione peroxidase. Gene. 1994 Jan 28;138(1-2):149–152. doi: 10.1016/0378-1119(94)90798-6. [DOI] [PubMed] [Google Scholar]
  28. Roveri A., Casasco A., Maiorino M., Dalan P., Calligaro A., Ursini F. Phospholipid hydroperoxide glutathione peroxidase of rat testis. Gonadotropin dependence and immunocytochemical identification. J Biol Chem. 1992 Mar 25;267(9):6142–6146. [PubMed] [Google Scholar]
  29. Takahashi K., Akasaka M., Yamamoto Y., Kobayashi C., Mizoguchi J., Koyama J. Primary structure of human plasma glutathione peroxidase deduced from cDNA sequences. J Biochem. 1990 Aug;108(2):145–148. doi: 10.1093/oxfordjournals.jbchem.a123172. [DOI] [PubMed] [Google Scholar]
  30. Thompson S. A., Sparling P. F. The RTX cytotoxin-related FrpA protein of Neisseria meningitidis is secreted extracellularly by meningococci and by HlyBD+ Escherichia coli. Infect Immun. 1993 Jul;61(7):2906–2911. doi: 10.1128/iai.61.7.2906-2911.1993. [DOI] [PMC free article] [PubMed] [Google Scholar]
  31. Thompson S. A., Wang L. L., Sparling P. F. Cloning and nucleotide sequence of frpC, a second gene from Neisseria meningitidis encoding a protein similar to RTX cytotoxins. Mol Microbiol. 1993 Jul;9(1):85–96. doi: 10.1111/j.1365-2958.1993.tb01671.x. [DOI] [PubMed] [Google Scholar]
  32. Thompson S. A., Wang L. L., West A., Sparling P. F. Neisseria meningitidis produces iron-regulated proteins related to the RTX family of exoproteins. J Bacteriol. 1993 Feb;175(3):811–818. doi: 10.1128/jb.175.3.811-818.1993. [DOI] [PMC free article] [PubMed] [Google Scholar]
  33. Welch R. A., Hull R., Falkow S. Molecular cloning and physical characterization of a chromosomal hemolysin from Escherichia coli. Infect Immun. 1983 Oct;42(1):178–186. doi: 10.1128/iai.42.1.178-186.1983. [DOI] [PMC free article] [PubMed] [Google Scholar]
  34. West S. E., Clark V. L. Genetic loci and linkage associations in Neisseria gonorrhoeae and Neisseria meningitidis. Clin Microbiol Rev. 1989 Apr;2 (Suppl):S92–103. doi: 10.1128/cmr.2.suppl.s92. [DOI] [PMC free article] [PubMed] [Google Scholar]
  35. de Veaux L. C., Clevenson D. S., Bradbeer C., Kadner R. J. Identification of the btuCED polypeptides and evidence for their role in vitamin B12 transport in Escherichia coli. J Bacteriol. 1986 Sep;167(3):920–927. doi: 10.1128/jb.167.3.920-927.1986. [DOI] [PMC free article] [PubMed] [Google Scholar]

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