Adherence of Mycoplasma gallisepticum to glass.
Attachment of washed Mycoplasma gallisepticum cells to glass was quantified with organisms in which membrane lipids were labelled with 3H. Siliconization of the test tubes decreased attachment, while centrifugation increased it. Attachment increased with temperature, decreased with increasing pH and ionic strength of the attachment mixture, but was unaffected by Ca2+, Mg2+ and EDTA. This suggests that ionic bonds, but not salt bridges, participate in the attachment process. Glycophorin, the major receptor responsible for M. gallisepticum attachment to erythrocytes, partially inhibited the attachment of the organisms to glass. However, bovine serum albumin also decreased attachment. Extensive pretreatment of the organisms with trypsin decreased their ability to attach to glass by about 35 to 40%. Trypsin and pronase failed to detach the organisms already bound to glass, suggesting that external mycoplasma cell components, other than membrane proteins, also participate in attachment of the organisms to glass.
D002452:Cell Count; D005898:Glass; D006021:Glycophorins / Q000494:pharmacology; D006358:Hot Temperature; D006863:Hydrogen-Ion Concentration; D008563:Membrane Lipids / Q000502:physiology; D009174:Mycoplasma / Q000187:drug effects / Q000502:physiology*; D009994:Osmolar Concentration; D012710:Serum Albumin, Bovine / Q000494:pharmacology; D012828:Silicones
D006021:Glycophorins; D008563:Membrane Lipids; D012828:Silicones; D012710:Serum Albumin, Bovine