Abstract
Chlamydia trachomatis LGV-434 was grown in HeLa 229 cells. Benzylpenicillin completely inhibited the formation of infectious elementary bodies (EBs) at a concentration of 19 pmol/ml or higher and produced abnormally large reticulate bodies (RBs) in the inclusions at 30 pmol/ml or higher. The possible targets for penicillin in C. trachomatis were three penicillin-binding proteins (PBPs) which were identified in the Sarkosyl-soluble fractions of both RBs and EBs. The apparent subunit molecular weights were 88,000 (PBP 1), 61,000 (BPB 2), and 36,000 (PBP 3). The 50% binding concentrations of [3H]penicillin for PBPs 1 to 3 in EBs and RBs were between 7 and 70 pmol/ml. Such high susceptibility to penicillin was shown by an organism that did not have detectable muramic acid (less than 0.02% by weight) in preparations of either whole cells or sodium dodecyl sulfate-insoluble residues.
Full text
PDF![420](https://cdn.ncbi.nlm.nih.gov/pmc/blobs/66d4/220254/68bfdab038b4/jbacter00254-0430.png)
![421](https://cdn.ncbi.nlm.nih.gov/pmc/blobs/66d4/220254/22e767fc12e5/jbacter00254-0431.png)
![422](https://cdn.ncbi.nlm.nih.gov/pmc/blobs/66d4/220254/c4b11ff0df13/jbacter00254-0432.png)
![423](https://cdn.ncbi.nlm.nih.gov/pmc/blobs/66d4/220254/0ab32311d1ff/jbacter00254-0433.png)
![424](https://cdn.ncbi.nlm.nih.gov/pmc/blobs/66d4/220254/b3ba0c765d58/jbacter00254-0434.png)
![425](https://cdn.ncbi.nlm.nih.gov/pmc/blobs/66d4/220254/f6eca2203ba0/jbacter00254-0435.png)
![426](https://cdn.ncbi.nlm.nih.gov/pmc/blobs/66d4/220254/345c46364852/jbacter00254-0436.png)
![427](https://cdn.ncbi.nlm.nih.gov/pmc/blobs/66d4/220254/cd202c81899b/jbacter00254-0437.png)
![428](https://cdn.ncbi.nlm.nih.gov/pmc/blobs/66d4/220254/097c640a220e/jbacter00254-0438.png)
Images in this article
Selected References
These references are in PubMed. This may not be the complete list of references from this article.
- Alexander J. J. Separation of protein synthesis in meningopneumonitisgent from that in L cells by differential susceptibility to cycloheximide. J Bacteriol. 1968 Feb;95(2):327–332. doi: 10.1128/jb.95.2.327-332.1968. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Barbour A. G. Properties of penicillin-binding proteins in Neisseria gonorrhoeae. Antimicrob Agents Chemother. 1981 Feb;19(2):316–322. doi: 10.1128/aac.19.2.316. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Blumberg P. M., Strominger J. L. Interaction of penicillin with the bacterial cell: penicillin-binding proteins and penicillin-sensitive enzymes. Bacteriol Rev. 1974 Sep;38(3):291–335. doi: 10.1128/br.38.3.291-335.1974. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Bradford M. M. A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Anal Biochem. 1976 May 7;72:248–254. doi: 10.1016/0003-2697(76)90527-3. [DOI] [PubMed] [Google Scholar]
- Braun V., Bosch V. Sequence of the murein-lipoprotein and the attachment site of the lipid. Eur J Biochem. 1972 Jun 23;28(1):51–69. doi: 10.1111/j.1432-1033.1972.tb01883.x. [DOI] [PubMed] [Google Scholar]
- Braun V., Gnirke H., Henning U., Rehn K. Model for the structure of the shape-maintaining layer of the Escherichia coli cell envelope. J Bacteriol. 1973 Jun;114(3):1264–1270. doi: 10.1128/jb.114.3.1264-1270.1973. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Caldwell H. D., Kromhout J., Schachter J. Purification and partial characterization of the major outer membrane protein of Chlamydia trachomatis. Infect Immun. 1981 Mar;31(3):1161–1176. doi: 10.1128/iai.31.3.1161-1176.1981. [DOI] [PMC free article] [PubMed] [Google Scholar]
- EAGLE H. The binding of penicillin in relation to its cytotoxic action. III. The binding of penicillin by mammalian cells in tissue culture (HeLa and L strains). J Exp Med. 1954 Jul 1;100(1):117–124. doi: 10.1084/jem.100.1.117. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Eagle H., Musselman A. D. THE SLOW RECOVERY OF BACTERIA FROM THE TOXIC EFFECTS OF PENICILLIN. J Bacteriol. 1949 Oct;58(4):475–490. doi: 10.1128/jb.58.4.475-490.1949. [DOI] [PMC free article] [PubMed] [Google Scholar]
- FURNESS G., GRAHAM D. M., REEVE P. The titration of trachoma and inclusion blennorrhoea viruses in cell cultures. J Gen Microbiol. 1960 Dec;23:613–619. doi: 10.1099/00221287-23-3-613. [DOI] [PubMed] [Google Scholar]
- Fox G. E., Stackebrandt E., Hespell R. B., Gibson J., Maniloff J., Dyer T. A., Wolfe R. S., Balch W. E., Tanner R. S., Magrum L. J. The phylogeny of prokaryotes. Science. 1980 Jul 25;209(4455):457–463. doi: 10.1126/science.6771870. [DOI] [PubMed] [Google Scholar]
- Garrett A. J., Harrison M. J., Manire G. P. A search for the bacterial mucopeptide component, muramic acid, in Chlamydia. J Gen Microbiol. 1974 Jan;80(1):315–318. doi: 10.1099/00221287-80-1-315. [DOI] [PubMed] [Google Scholar]
- Ghuysen J. M. Use of bacteriolytic enzymes in determination of wall structure and their role in cell metabolism. Bacteriol Rev. 1968 Dec;32(4 Pt 2):425–464. [PMC free article] [PubMed] [Google Scholar]
- Haller I., Henning U. Cell envelope and shape of Escherichia coli K12. Crosslinking with dimethyl imidoesters of the whole cell wall. Proc Natl Acad Sci U S A. 1974 May;71(5):2018–2021. doi: 10.1073/pnas.71.5.2018. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Henning U. L. Determination of cell shape in bacteria. Annu Rev Microbiol. 1975;29:45–60. doi: 10.1146/annurev.mi.29.100175.000401. [DOI] [PubMed] [Google Scholar]
- JENKIN H. M. Preparation and properties of cell walls of the agent of meningopneumonitis. J Bacteriol. 1960 Nov;80:639–647. doi: 10.1128/jb.80.5.639-647.1960. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Jones J. B., Bowers B., Stadtman T. C. Methanococcus vannielii: ultrastructure and sensitivity to detergents and antibiotics. J Bacteriol. 1977 Jun;130(3):1357–1363. doi: 10.1128/jb.130.3.1357-1363.1977. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Kingsbury D. T. Estimate of the genome size of various microorganisms. J Bacteriol. 1969 Jun;98(3):1400–1401. doi: 10.1128/jb.98.3.1400-1401.1969. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Kingsbury D. T., Weiss E. Lack of deoxyribonucleic acid homology between species of the genus Chlamydia. J Bacteriol. 1968 Oct;96(4):1421–1423. doi: 10.1128/jb.96.4.1421-1423.1968. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Kramer M. J., Gordon F. B. Ultrastructural analysis of the effects of penicillin and chlortetracycline on the development of a genital tract Chlamydia. Infect Immun. 1971 Feb;3(2):333–341. doi: 10.1128/iai.3.2.333-341.1971. [DOI] [PMC free article] [PubMed] [Google Scholar]
- MOULDER J. W., NOVOSEL D. L., OFFICER J. E. INHIBITION OF THE GROWTH OF AGENTS OF THE PSITTACOSIS GROUP BY D-CYCLOSERINE AND ITS SPECIFIC REVERSAL BY D-ALANINE. J Bacteriol. 1963 Mar;85:707–711. doi: 10.1128/jb.85.3.707-711.1963. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Manire G. P. Structure of purified cell walls of dense forms of meningopneumonitis organisms. J Bacteriol. 1966 Jan;91(1):409–413. doi: 10.1128/jb.91.1.409-413.1966. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Manire G. P., Tamura A. Preparation and chemical composition of the cell walls of mature infectious dense forms of meningopneumonitis organisms. J Bacteriol. 1967 Oct;94(4):1178–1183. doi: 10.1128/jb.94.4.1178-1183.1967. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Matsumoto A. Fine structures of cell envelopes of Chlamydia organisms as revealed by freeze-etching and negative staining techniques. J Bacteriol. 1973 Dec;116(3):1355–1363. doi: 10.1128/jb.116.3.1355-1363.1973. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Matsumoto A., Manire G. P. Electron Microscopic Observations on the Fine Structure of Cell Walls of Chlamydia psittaci. J Bacteriol. 1970 Dec;104(3):1332–1337. doi: 10.1128/jb.104.3.1332-1337.1970. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Matsumoto A., Manire G. P. Electron microscopic observations on the effects of penicillin on the morphology of Chlamydia psittaci. J Bacteriol. 1970 Jan;101(1):278–285. doi: 10.1128/jb.101.1.278-285.1970. [DOI] [PMC free article] [PubMed] [Google Scholar]
- PERKINS H. R., ALLISON A. C. Cell-wall constituents of rickettsiae and psittacosis-lymphogranuloma organisms. J Gen Microbiol. 1963 Mar;30:469–480. doi: 10.1099/00221287-30-3-469. [DOI] [PubMed] [Google Scholar]
- Schachter J., Caldwell H. D. Chlamydiae. Annu Rev Microbiol. 1980;34:285–309. doi: 10.1146/annurev.mi.34.100180.001441. [DOI] [PubMed] [Google Scholar]
- Schwarz U., Leutgeb W. Morphogenetic aspects of murein structure and biosynthesis. J Bacteriol. 1971 May;106(2):588–595. doi: 10.1128/jb.106.2.588-595.1971. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Shiao L. C., Wang S. P., Grayston J. T. Sensitivity and resistance of TRIC agents to penicillin, tetracycline and sulfa drugs. Am J Ophthalmol. 1967 May;63(5 Suppl):1558–1568. doi: 10.1016/0002-9394(67)94147-5. [DOI] [PubMed] [Google Scholar]
- Sonntag I., Schwarz H., Hirota Y., Henning U. Cell envelope and shape of Escherichia coli: multiple mutants missing the outer membrane lipoprotein and other major outer membrane proteins. J Bacteriol. 1978 Oct;136(1):280–285. doi: 10.1128/jb.136.1.280-285.1978. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Spratt B. G. Properties of the penicillin-binding proteins of Escherichia coli K12,. Eur J Biochem. 1977 Jan;72(2):341–352. doi: 10.1111/j.1432-1033.1977.tb11258.x. [DOI] [PubMed] [Google Scholar]
- Stock J. B., Rauch B., Roseman S. Periplasmic space in Salmonella typhimurium and Escherichia coli. J Biol Chem. 1977 Nov 10;252(21):7850–7861. [PubMed] [Google Scholar]
- Tamura A., Manire G. P. Effect of penicillin on the multiplication of meningopneumonitis organisms (Chlamydia psittaci). J Bacteriol. 1968 Oct;96(4):875–880. doi: 10.1128/jb.96.4.875-880.1968. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Tamura A., Manire G. P. Preparation and chemical composition of the cell membranes of developmental reticulate forms of meningopneumonitis organisms. J Bacteriol. 1967 Oct;94(4):1184–1188. doi: 10.1128/jb.94.4.1184-1188.1967. [DOI] [PMC free article] [PubMed] [Google Scholar]
- WEIDEL W., PELZER H. BAGSHAPED MACROMOLECULES--A NEW OUTLOOK ON BACTERIAL CELL WALLS. Adv Enzymol Relat Areas Mol Biol. 1964;26:193–232. doi: 10.1002/9780470122716.ch5. [DOI] [PubMed] [Google Scholar]
- WEISS E. The effect of antibiotics on agents of the psittacosis-lymphogranuloma group. I. The effect of penicillin. J Infect Dis. 1950 Nov-Dec;87(3):249–263. doi: 10.1093/infdis/87.3.249. [DOI] [PubMed] [Google Scholar]
- Weiss E., Schramek S., Wilson N. N., Newman L. W. Deoxyribonucleic Acid Heterogeneity Between Human and Murine Strains of Chlamydia trachomatis. Infect Immun. 1970 Jul;2(1):24–28. doi: 10.1128/iai.2.1.24-28.1970. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Woese C. R., Magrum L. J., Fox G. E. Archaebacteria. J Mol Evol. 1978 Aug 2;11(3):245–251. doi: 10.1007/BF01734485. [DOI] [PubMed] [Google Scholar]