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Alterations induced by penicillin in the protein profile and cell structure of Group GStreptococcus

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We investigated the effect of a subminimal concentration of penicillin on the ultrastructure and protein profile of Group G streptococci. In cells treated with penicillin (1/3 MIC), the protein content increased by 50%, and several protein bands with a molecular mass of 14–70 kDa were detected. In the hydrophilic phase, carbohydrate-containing proteins were detected by PAS staining, and in the hydrophobic phase, a group of proteins that reacted strongly with homologous antisera were observed. In terms of cell structure, Triton X-114 extraction was found to induce alterations in the cross wall of untreated cells. In bacteria treated with penicillin but not extracted with Triton X-114, the cell wall was observed to detach itself, and regions with reduced amounts of cellular material appeared in the cytoplasm. After Triton-X114 extraction, these penicillin-treated cells exhibited profound morphological changes, leading in some cases to lysis.

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Literature Cited

  1. Atkinson BA, Amaral L (1982) Sublethal concentrations of antibiotics effects on bacteria and the immune system. Crit Rev Microbiol 9:101–138

    PubMed  Google Scholar 

  2. Barnhan M (1983) The gut as a source of the haemolytic streptococci causing infection in surgery of the intestinal and biliary tracts. J Infect6:129–139

    PubMed  Google Scholar 

  3. Beachey EH, Eisenstein BI, Ofek I (1982) Prevention of the adhesion of bacteria to mucosal surfaces: influence of antimicrobial agents. In: Eickenberg HU, Hahn H, Opfurkuch W (eds) The influence of antibiotics on the host-parasite relationship. New York: Springer-Verlag, pp 171–182

    Google Scholar 

  4. Bordier C (1981) Phase separation of integral membrane proteins in Triton X-114 solution. J Biol Chem 256:1604–1607

    PubMed  Google Scholar 

  5. Castro ACD, Benchetrit LC, Barrucand L (1985) Eteito de concentracões submínimas inibitórias de penicilina sobre a morfologia de estreptococos do grupo G. Rev Bras Pat Clin 21:123–129

    Google Scholar 

  6. Castro ACD, Ferreira BT, Benchetrit LC (1990) Correlation between growth in antibiotic—medium and hemolytic activity of group C and G Streptococci. Zentralbl Bakt 272:283–290

    Google Scholar 

  7. Christensen KK, Christensen P, Flamholc L, Ripa T (1974) Frequencies of streptococci of group A, B, C, D and G in urethra and cervix swab specimens from patients with suspected gonococcal infection. Acta Pathol Microbiol Scand B 82:470–474

    Google Scholar 

  8. Doerner AC, White BA (1990) Detection of glycoproteins separated by nondenaturing polyacrylamide gel electrophoresis using the periodic acid—Schiffstain. Anal Biochem 187:147–150

    PubMed  Google Scholar 

  9. Efstratiou A (1989) Outbreaks of human infection caused by pyogenic streptococci to Lancefield group C and G. J Med Microbiol 29:207–219

    PubMed  Google Scholar 

  10. Forrer OB, Ellner PD (1979) Distribution of haemolytic streptococci in respiratory specimens. J Clin Microbiol 10: 69–71

    PubMed  Google Scholar 

  11. Gaunt PN, Seal DV (1987) Group G streptococcal infections. J Infect 15:5–20

    PubMed  Google Scholar 

  12. Giovanini de Simone S, Bonaldo MC, Pinho RP, Pontes de Carvalho LC, Galvão Castro B, Goldenberg S (1988) A study on the amphilic proteins of threeTrypanosoma cruzi populations. Braz J Med Res 21:435–443

    Google Scholar 

  13. Hallander HO, Lawrell G, Lofstrom G (1966) Stimulation of staphylococcal hemolysin production by low concentrations of penicillin. Acta Pathol Microbiol Scand 68:142

    PubMed  Google Scholar 

  14. Jaffe CL, Bennett E, Grimaldi Jr G, McMahon-Pratt D (1984) Production and characterization of species—specific monoclonal antibodies againstLeishmania donovani for immunodiagnosis. J Immunol 133:440–447

    PubMed  Google Scholar 

  15. James R (1975) Identification of an outer membrane protein ofEscherichia coli with a role in the coordination of deoxyribonucleic acid replication and cell elongation. J Bacteriol 124:918

    PubMed  Google Scholar 

  16. Jones RN, Barry AL, Gavan TL, Washington JA (1985) Susceptibility tests microdilution and macrodilution broth procedures. In: Lennette EH, Balows A, Hausler Jr WJ, Shadomy HJ (eds) Manual of clinical microbiology. Washington DC: American Society for Microbiology, pp 972–977

    Google Scholar 

  17. Laemmli VK (1970) Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature 227:680–685

    PubMed  Google Scholar 

  18. Lancefield RC (1933) A serological differentiation of human and other groups of haemolytic streptococci. J Exp Med 57:571–595

    Google Scholar 

  19. Lorian V (1975) Some effects of subinhibitory concentrations of penicillin on the structure and division of staphylococci Antimicrob Agents Chemother 7:864–870

    PubMed  Google Scholar 

  20. Lorian V (1986) Effect of antibiotic concentrations on bacteria: effects on ultrastructure, their virulence, and susceptibility to immunodefenses. In: Lorian V (ed) Antibiotics in laboratory medicine. Baltimore: Williams & Wilkins, pp 596–668

    Google Scholar 

  21. Lorian V, Sabath LD, Simonescu M (1975) Decrease in ribosomal density ofProteus mirabilis exposed to subinhibitory concentration of ampicillin or cephalothin. Proc Soc Exp Biol Med 149:731–735

    PubMed  Google Scholar 

  22. Lowry OH, Rosebrough NJ, Farr AL, Randall RJ (1951) Protein measurement with the Folin phenol reagent. J Biol Chem 193:265–275

    PubMed  Google Scholar 

  23. McDowell TD, Lemanski CL (1988) Absence of autolytic activity (peptidoglycan nicking) in penicillin-induced nonlytic death in a group A Streptococcus. J Bacteriol 170:1783–1788

    PubMed  Google Scholar 

  24. Meirelles MNL, Araujo Jorge TC, Miranda CF, De Souza W (1986) Interaction ofTrypanosoma cruzi with heart muscle cells: ultrastructural and cytochemical analysis of endocytic vacuole formation and effect upon myogenesis in vitro. Eur J Cell Biol 41:198–206

    PubMed  Google Scholar 

  25. Michel J, Ferne M, Borinski R, Kornberg Z, Berger-Rabinowitz S, Ginsburg I (1982) Effects of subminimal inhibitory concentrations of chloramphenicol, erythromycin and penicillin on group A Streptococci. Eur J Clin Microbiol 1:375–380

    PubMed  Google Scholar 

  26. Murray PJ, Spithill TW, Handman E (1989) Characterization of integral membrane proteins ofLeishmania major by Triton X-114 fraction and analysis of vaccination effects in mice. Infect Immun 57:2203–2209

    PubMed  Google Scholar 

  27. Shockman GD, Daneo-Moore L, McDowell TD, Wong W (1981) Function and structure of the cell wall-its importance in the life and death of bacteria. In: Salton MJ, Shockman GD (eds) β-Lactam antibiotics: mode of action, new developments and future prospects. New York: Academic Press, Inc. pp 65–76

    Google Scholar 

  28. Vermelho AB, Barreto Bergter E, Pereira MC, Meirelles MNL (1992) Glycolipid and protein profiles of normal andTrypanosoma cruzi infected heat muscle cells. Acta Trop (Basel) 52:17–25

    Google Scholar 

  29. Vieira VV, Barrucand L, Castro ACD (1993) The effects of subminimal inhibitory concentrations of penicillin on growth rate and haemolysin activity of group G Streptococcus. Mem Inst Osvaldo Cruz 88, in press

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de Castro, A.C.D., Meirelles, M.N.L., Hampshire de Carvalho Santos, A. et al. Alterations induced by penicillin in the protein profile and cell structure of Group GStreptococcus . Current Microbiology 28, 269–273 (1994). https://doi.org/10.1007/BF01573204

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