Archives of Microbiology

, Volume 127, Issue 3, pp 297–299 | Cite as

Differentiation of mycoplasmatales from bacterial protoplast L-forms by assay for penicillin binding proteins

  • Hans Herbert Martin
  • Wolfgang Schilf
  • Hans-Gerd Schiefer


Membrane proteins with the specific ability for binding penicillin with high affinity (penicillin binding proteins) were found to be present in two strains of the cell wall-less protoplast L-form of P. MIrabilis and were absent from different species of Mycoplasma and from Acholeplasma laidlawii. Thus, the assay for penicillin binding proteins appeared to be suitable for the differentiation of the cell wall-less procaryotes. The absence of penicillin binding proteins from the mycoplasmatales further confirmed the unrelatedness of this group to the bacteria.

Key words

Cell wall-less procaryotes Mycoplasma Protoplast L-form Penicillin binding proteins 

Non-Standard Abbreviation


penicillin binding protein


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  1. Blumberg PM, Strominger JL (1974) Interaction of penicillin with the bacterial cell: Penicillin binding proteins and penicillin sensitive enzymes. Bacteriol Rev 38:291–335Google Scholar
  2. Hofschneider PH, Martin HH (1968) Diversity of surface layers in L-forms of Proteus mirabilis. J Gen Microbiol 51:23–33Google Scholar
  3. Kandler O, Kandler G (1956) Trennung und Charakterisierung verschiedener L-Phasen-Typen von Proteus vulgaris. Z Naturforschg 11b:252–259Google Scholar
  4. Kandler O, Hund A, Zehender C (1958) Cell wall composition in bacterial and L-forms of Proteus vulgaris. Nature (Lond) 181:572–573Google Scholar
  5. Kandler O, Kandler G (1960) Die L-Phase der Bakterien. Erg Mikrobiol, Immunitätsforsch u Experim Therapie 33:97–127Google Scholar
  6. Kroll HP, Gmeiner J, Martin HH (1980) Membranes of the protoplast L-form of Proteus mirobilis. Arch Microbiol 127:223–229Google Scholar
  7. Martin HH (1964) Composition of the mucopolymer in cell walls of the unstable and stable L-form of Proteus mirabilis. J Gen Microbiol 36:441–450Google Scholar
  8. Martin HH, Maskos C, Burger R (1975) d-Alanyl-d-alanine carboxypeptidase in the bacterial form and L-form of Proteus mirabilis. Eur J Biochem 55:465–473Google Scholar
  9. Ohya S, Yamazaki M, Sugawara S, Matsuhashi M (1979) Penicillin-binding in Proteus species. J Bacteriol 137:474–479Google Scholar
  10. Razin S (1978) The mycoplasmas. Microbiol Rev 42:414–470Google Scholar
  11. Rottem S, Stein O, Razin S (1968) Reassembly of mycoplasma membranes disaggregated by detergents. Arch Biochem Biophys 125:46–56Google Scholar
  12. Rottem S, Razin S (1972) Isolation of mycoplasma membranes by digitonin. J Bacteriol 110:699–705Google Scholar
  13. Schiefer HG, Gerhardt U, Brunner H, Krüpe M (1974) Studies with lectins of the surface carbohydrate structures of mycoplasma membranes. J Bacteriol 120:81–88Google Scholar
  14. Schilf W, Martin HH (1980) Purification of two DD-carboxypeptidases/transpeptidases with different penicillin sensitivities from Proteus mirabilis. Eur J Biochem 105:361–370Google Scholar
  15. Spratt BG (1978) The mechanism of action of penicillin. Sci Prog Oxf 65:101–128Google Scholar
  16. Spratt BG, Jobanputra V, Schwarz U (1977) Mutants of Escherichia coli which lack a component of penicillin-binding protein 1 are viable. FEBS Lett 79:374–378Google Scholar
  17. Taubeneck U (1962) Untersuchungen über die L-Form von Proteus mirabilis Hauser. II. Entwicklung und Wesen der L-Form. Z All Mikrobiol 2:132–156Google Scholar

Copyright information

© Springer-Verlag 1980

Authors and Affiliations

  • Hans Herbert Martin
    • 1
  • Wolfgang Schilf
    • 1
  • Hans-Gerd Schiefer
    • 2
  1. 1.Institut für MikrobiologieTechnische HochschuleDarmstadtFederal Republic of Germany
  2. 2.Institut für Medizinische MikrobiologieJustus Liebig UniversitätGiessenFederal Republic of Germany

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