Studies with lectins on the surface carbohydrate structures of mycoplasma membranes.
PDF (1.2M)
Journal: 1975/January - Journal of Bacteriology
ISSN: 0021-9193
PUBMED: 4138526
Abstract:
The surface carbohydrate structures on the cell membranes of various mycoplasma species have been investigated by using lectins, which are sugar-specific proteins. Carbohydrate structures presumably bound to glycolipids, with both galactose and glucose units, were found to be exposed on the surface of Mycoplasma pneumoniae and its temperature-sensitive mutants, M. mycoides var. mycoides and capri, M. pulmonis, M. gallinarum, and M. gallisepticum. Lipid-bound glucose was found on M. neurolyticum. The possible relationship of the lipid-bound surface carbohydrate groups to the known serological cross-reactions and lipid compositions of the various mycoplasma species is discussed. Intact Acholeplasma laidlawii and M. fermentans have no lectin-binding sites exposed on their surfaces; galactose groups were discovered only after Pronase digestion of the organisms, suggesting that their glycolipids are hidden under a protein layer. Neither intact nor Pronase-digested M. hominis reacted with the lectins; this is fully consistent with the lipid composition of this organism, which contains glycolipids. The lectins from Vicia cracca and Phaseolus vulgaris, which react with N-acetyl-galactosamine groups, agglutinated M. gallinarum, M. gallisepticum, M. mycoides var. capri, and M. pulmonis. The agglutinability was lost after Pronase treatment, indicating that the corresponding carbohydrates are presumably protein bound. They may be correlated with the extracellular structures observed by electron microscopy of both sectioned and negatively stained mycoplasma species.
Open in
PUBMED | PMC | Google Scholar | Wikipedia
Relations:
Content
Citations
(22)
References
(39)
Chemicals
(6)
Organisms
(2)
Processes
(2)
Anatomy
(1)
Similar articles
Articles by the same authors
Discussion board
J Bacteriol 120(1): 81-88
PMID: 4138526

Studies with Lectins on the Surface Carbohydrate Structures of Mycoplasma Membranes

Abstract

The surface carbohydrate structures on the cell membranes of various mycoplasma species have been investigated by using lectins, which are sugar-specific proteins. Carbohydrate structures presumably bound to glycolipids, with both galactose and glucose units, were found to be exposed on the surface of Mycoplasma pneumoniae and its temperature-sensitive mutants, M. mycoides var. mycoides and capri, M. pulmonis, M. gallinarum, and M. gallisepticum. Lipid-bound glucose was found on M. neurolyticum. The possible relationship of the lipid-bound surface carbohydrate groups to the known serological cross-reactions and lipid compositions of the various mycoplasma species is discussed. Intact Acholeplasma laidlawii and M. fermentans have no lectin-binding sites exposed on their surfaces; galactose groups were discovered only after Pronase digestion of the organisms, suggesting that their glycolipids are hidden under a protein layer. Neither intact nor Pronase-digested M. hominis reacted with the lectins; this is fully consistent with the lipid composition of this organism, which contains glycolipids. The lectins from Vicia cracca and Phaseolus vulgaris, which react with N-acetyl-galactosamine groups, agglutinated M. gallinarum, M. gallisepticum, M. mycoides var. capri, and M. pulmonis. The agglutinability was lost after Pronase treatment, indicating that the corresponding carbohydrates are presumably protein bound. They may be correlated with the extracellular structures observed by electron microscopy of both sectioned and negatively stained mycoplasma species.

Full text

Full text is available as a scanned copy of the original print version. Get a printable copy (PDF file) of the complete article (1.2M), or click on a page image below to browse page by page. Links to PubMed are also available for Selected References.
icon of scanned page 81
81
icon of scanned page 82
82
icon of scanned page 83
83
icon of scanned page 84
84
icon of scanned page 85
85
icon of scanned page 86
86
icon of scanned page 87
87
icon of scanned page 88
88

Selected References

These references are in PubMed. This may not be the complete list of references from this article.
  • Black FT, Birch-Andersen A, Freundt EA. Morphology and ultrastructure of human T-mycoplasmas. J Bacteriol. 1972 Jul;111(1):254–259.[PMC free article] [PubMed] [Google Scholar]
  • Burger MM. A difference in the architecture of the surface membrane of normal and virally transformed cells. Proc Natl Acad Sci U S A. 1969 Mar;62(3):994–1001.[PMC free article] [PubMed] [Google Scholar]
  • CHANOCK RM, HAYFLICK L, BARILE MF. Growth on artificial medium of an agent associated with atypical pneumonia and its identification as a PPLO. Proc Natl Acad Sci U S A. 1962 Jan 15;48:41–49.[PMC free article] [PubMed] [Google Scholar]
  • Chu HP, Horne RW. Electron microscopy of Mycoplasma gallisepticum and Mycoplasma mycoides using the negative staining technique and their comparison with myxovirus. Ann N Y Acad Sci. 1967 Jul 28;143(1):190–203. [PubMed] [Google Scholar]
  • DOMERMUTH CH, NIELSEN MH, FREUNDT EA, BIRCH-ANDERSEN A. ULTRASTRUCTURE OF MYCOPLASMA SPECIES. J Bacteriol. 1964 Sep;88:727–744.[PMC free article] [PubMed] [Google Scholar]
  • Gilliam JM, Morowitz HJ. Characterization of the plasma membrane of Mycoplasma laidlawii. IX. Isolation and characterization of the membrane polyhexosamine. Biochim Biophys Acta. 1972 Aug 9;274(2):353–363. [PubMed] [Google Scholar]
  • Gourlay RN, Thrower KJ. Morphology of Mycoplasma mycoides thread-phase growth. J Gen Microbiol. 1968 Nov;54(1):155–159. [PubMed] [Google Scholar]
  • Hayflick L. Tissue cultures and mycoplasmas. Tex Rep Biol Med. 1965 Jun;23(Suppl):285+–285+. [PubMed] [Google Scholar]
  • Henning R, Uhlenbruck G. Detection of carbohydrate structures on isolated subcellular organelles of rat liver by heterophile agglutinins. Nat New Biol. 1973 Mar 28;242(117):120–122. [PubMed] [Google Scholar]
  • HUMMELER K, TOMASSINI N, HAYFLICK L. ULTRASTRUCTURE OF A MYCOPLASMA (NEGRONI) ISOLATED FROM HUMAN LEUKEMIA. J Bacteriol. 1965 Aug;90:517–523.[PMC free article] [PubMed] [Google Scholar]
  • Kenny GE. Serological cross-reaction between lipids of Mycoplasma pneumoniae and Mycoplasma neurolyticum. Infect Immun. 1971 Aug;4(2):149–153.[PMC free article] [PubMed] [Google Scholar]
  • Klenk HD, Rott R, Becht H. On the structure of the influenza virus envelope. Virology. 1972 Mar;47(3):579–591. [PubMed] [Google Scholar]
  • Köhler W, Prokop O. Agglutination von Streptokokken der Gruppe C durch ein Agglutinin aus Helix pomatia. Z Immunitatsforsch Allerg Klin Immunol. 1967 Jun;133(1):50–53. [PubMed] [Google Scholar]
  • Köhler W, Prokop O. Agglutinationversuche an Streptokokken mit dem Phytagglutinin aus Dolichos biflorus. Z Immunitatsforsch Allerg Klin Immunol. 1967 Jul;133(2):171–175. [PubMed] [Google Scholar]
  • Kornfeld R, Kornfeld S. The structure of a phytohemagglutinin receptor site from human erythrocytes. J Biol Chem. 1970 May 25;245(10):2536–2545. [PubMed] [Google Scholar]
  • Lemcke RM, Marmion BP, Plackett P. Immunochemical analysis of Mycoplasma pneumoniae. Ann N Y Acad Sci. 1967 Jul 28;143(1):691–702. [PubMed] [Google Scholar]
  • Lemcke RM, Shaw EJ, Marmion BP. Related antigens in Mycoplasma pneumoniae and Mycoplasma mycoides var. mycoides. Aust J Exp Biol Med Sci. 1965 Dec;43(6):761–770. [PubMed] [Google Scholar]
  • Lis H, Sharon N. The biochemistry of plant lectins (phytohemagglutinins). Annu Rev Biochem. 1973;42(0):541–574. [PubMed] [Google Scholar]
  • LOWRY OH, ROSEBROUGH NJ, FARR AL, RANDALL RJ. Protein measurement with the Folin phenol reagent. J Biol Chem. 1951 Nov;193(1):265–275. [PubMed] [Google Scholar]
  • Ne'eman Z, Kahane I, Kovartovsky J, Razin S. Characterization of the myoplasma membrane proteins. 3. Gel filtration and immunological characterization of Acholeplasma laidlawii membrane proteins. Biochim Biophys Acta. 1972 Apr 14;266(1):255–268. [PubMed] [Google Scholar]
  • Nicolson GL, Blaustein J, Etzler ME. Characterization of two plant lectins from Ricinus communis and their quantitative interaction with a murine lymphoma. Biochemistry. 1974 Jan 1;13(1):196–204. [PubMed] [Google Scholar]
  • Pardoe GI, Bird GW, Uhlenbruck G. On the specificity of lectins with a broad agglutination spectrum. I. The nature of the specific receptors for Ricinus communis and Solanum tuberosum Lectins. Z Immunitatsforsch Allerg Klin Immunol. 1969 May;137(5):442–457. [PubMed] [Google Scholar]
  • Plackett P, Marmion BP, Shaw EJ, Lemcke RM. Immunochemical analysis of Mycoplasma pneumoniae. 3. Separation and chemical identification of serologically active lipids. Aust J Exp Biol Med Sci. 1969 Apr;47(2):171–195. [PubMed] [Google Scholar]
  • Poretz RD, Goldstein IJ. An examination of the topography of the saccharide binding sites of concanavalin A and of the forces involved in complexation. Biochemistry. 1970 Jul 7;9(14):2890–2896. [PubMed] [Google Scholar]
  • Prescott B, Sobeslavsky O, Caldes G, Chanock RM. Isolation and characterization of fractions of Mycoplasma pneumoniae. I. Chemical and chromatographic separation. J Bacteriol. 1966 Jun;91(6):2117–2125.[PMC free article] [PubMed] [Google Scholar]
  • Rapport MM, Graf L. Immunochemical reactions of lipids. Prog Allergy. 1969;13:273–331. [PubMed] [Google Scholar]
  • Razin S. Physiology of mycoplasmas. Adv Microb Physiol. 1973;10:1–80. [PubMed] [Google Scholar]
  • Razin S, Prescott B, Caldes G, James WD, Chanock RM. Role of Glycolipids and Phosphatidylglycerol in the Serological Activity of Mycoplasma pneumoniae. Infect Immun. 1970 Apr;1(4):408–416.[PMC free article] [PubMed] [Google Scholar]
  • Rottem S, Razin S. Membrane lipids of Mycoplasma hominis. J Bacteriol. 1973 Feb;113(2):565–571.[PMC free article] [PubMed] [Google Scholar]
  • Rottem S, Samuni A. Effect of proteins on the motion of spin-labeled fatty acids in mycoplasma membranes. Biochim Biophys Acta. 1973 Feb 27;298(1):32–38. [PubMed] [Google Scholar]
  • Rottem S, Stein O, Razin S. Reassembly of Mycoplasma membranes disaggregated by detergents. Arch Biochem Biophys. 1968 Apr;125(1):46–56. [PubMed] [Google Scholar]
  • Sharon N, Lis H. Lectins: cell-agglutinating and sugar-specific proteins. Science. 1972 Sep 15;177(4053):949–959. [PubMed] [Google Scholar]
  • Shaw N. Bacterial glycolipids. Bacteriol Rev. 1970 Dec;34(4):365–377.[PMC free article] [PubMed] [Google Scholar]
  • Smith PF. Lipid composition of Mycoplasma neurolyticum. J Bacteriol. 1972 Oct;112(1):554–558.[PMC free article] [PubMed] [Google Scholar]
  • Smith PF, Koostra WL. Phospholipids and glycolipids of sterol-requiring Mycoplasma. J Bacteriol. 1967 Jun;93(6):1853–1862.[PMC free article] [PubMed] [Google Scholar]
  • Steinberg P, Horswood RL, Chanock RM. Temperature-sensitive mutants of Mycoplasma pneumoniae. I. In vitro biologic properties. J Infect Dis. 1969 Aug;120(2):217–224. [PubMed] [Google Scholar]
  • Terry TM, Zupnik JS. Weak association of glucosamine-containing polymer with the Acholeplasma laidlawii membrane. Biochim Biophys Acta. 1973 Jan 2;291(1):144–148. [PubMed] [Google Scholar]
  • Uhlenbruck G, Pardoe GI, Bird GW. On the specificity of lectins with a broad agglutination spectrum. II. Studies on the nature of the T-antigen and the specific receptors for the lectin of Arachis hypogoea (ground-nut). Z Immunitatsforsch Allerg Klin Immunol. 1969 Nov;138(5):423–433. [PubMed] [Google Scholar]
  • Winzler RJ. Carbohydrates in cell surfaces. Int Rev Cytol. 1970;29:77–125. [PubMed] [Google Scholar]
Institut für Medizinische Mikrobiologie, D-63 Giessen, Federal Republic of Germany
Copyright notice
Abstract
The surface carbohydrate structures on the cell membranes of various mycoplasma species have been investigated by using lectins, which are sugar-specific proteins. Carbohydrate structures presumably bound to glycolipids, with both galactose and glucose units, were found to be exposed on the surface of Mycoplasma pneumoniae and its temperature-sensitive mutants, M. mycoides var. mycoides and capri, M. pulmonis, M. gallinarum, and M. gallisepticum. Lipid-bound glucose was found on M. neurolyticum. The possible relationship of the lipid-bound surface carbohydrate groups to the known serological cross-reactions and lipid compositions of the various mycoplasma species is discussed. Intact Acholeplasma laidlawii and M. fermentans have no lectin-binding sites exposed on their surfaces; galactose groups were discovered only after Pronase digestion of the organisms, suggesting that their glycolipids are hidden under a protein layer. Neither intact nor Pronase-digested M. hominis reacted with the lectins; this is fully consistent with the lipid composition of this organism, which contains glycolipids. The lectins from Vicia cracca and Phaseolus vulgaris, which react with N-acetyl-galactosamine groups, agglutinated M. gallinarum, M. gallisepticum, M. mycoides var. capri, and M. pulmonis. The agglutinability was lost after Pronase treatment, indicating that the corresponding carbohydrates are presumably protein bound. They may be correlated with the extracellular structures observed by electron microscopy of both sectioned and negatively stained mycoplasma species.
Collaboration tool especially designed for Life Science professionals.Drag-and-drop any entity to your messages.