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Interaction of mycoplasmas with host cells.
  • S. Rottem
  • Biology
    Physiological reviews
  • 1 April 2003
Present knowledge is collated on the strategies employed by mycoplasmas while interacting with their host eukaryotic cells to demonstrate an impressive capability of maintaining a dynamic surface architecture that is antigenically and functionally versatile.
Cloning, characterization, and expression in Escherichia coli of the gene coding for the CpG DNA methylase from Spiroplasma sp. strain MQ1(M.SssI).
The cloning, characterization and expression in E. coli of the gene coding for a DNA methylase from Spiroplasma sp.Q1 (M.SssI) shows de novo methylase activity, characteristic of prokaryotic cytosine DNA methylases.
Beware of mycoplasmas.
Identification of Mycoplasma and Other Microorganisms by Polyacrylamide-Gel Electrophoresis of Cell Proteins
Preliminary results indicate that this electrophoretic method may also be used for the identification and classification of other microorganisms.
Contamination of Tissue Cultures by Mycoplasmas
The intriguing questions of how a mycoplasma infecting tissue culture cells subvert and damage the host cells by mediating transformation of the cells, affecting the signal-transduction pathways and the metabolism of immune and nonimmune cells are discussed.
Procaryotic and eucaryotic traits of DNA methylation in spiroplasmas (mycoplasmas)
Differences in the type of base methylated (cytosine or adenine) and in the extent of methylation were detected by high-pressure liquid chromatography in the DNAs of five spiroplasmas, and the MQ-1 methylase differed from eucaryotic methylases by showing high activity on nonmethylated DNA duplexes, low activity with hemimethylated DNA Duplexes and no activity on single-stranded DNA.
Mycoplasma fermentans Binds to and Invades HeLa Cells: Involvement of Plasminogen and Urokinase
Adherence of Mycoplasma fermentans to HeLa cells followed saturation kinetics, required a divalent cation, and was enhanced by preincubation of the organism at 37°C for 1 h in a low-osmolarity solution, supporting the notion that M. fermentans utilizes at least two surface components for adhesion, a protease-sensitive surface protein and a phosphocholine-containing glycolipid.
Ether lipids in the cell membrane of Mycoplasma fermentans.
The ether lipids of M. fermentans are structurally similar to platelet activating factor; it was demonstrated that the 2-O-acetylated lyso form lipid can mimic platelet-activating factor activity in isolated perfused and ventilated rat lungs.