Binding of plant lectins to mycoplasma cells and membranes.
The binding of iodinated wheat germ agglutinin, Ricinus communis agglutinin, and concanavalin A to mycoplasma cells and membranes was examined. All mycoplasmas studied specifically bound concanavalin A  or R. communis agglutinin and, to a lesser degree, wheat germ agglutinin. The binding of lectins to whole cells was similar to that recorded for membranes, suggesting that significant binding only occurred on the outer surface of the mycoplasma membrane. Proteolysis of the membrane almost always increased the capacity to bind lectins, which indicates that additional carbohydrate groups on the mycoplasma membrane are masked by a protein layer or protein complexes on the membrane. The observation that carbohydrates are apparently exposed on the surface of mycoplasma membranes should stimulate more concentrated study on the isolation and chemical characterization of these substances since it is quite likely that they are responsible for a variety of reactions between mycoplasmas and host cells.
D000127:Acholeplasma / Q000378:metabolism*; D000128:Acholeplasma laidlawii / Q000378:metabolism; D002462:Cell Membrane / Q000378:metabolism; D003208:Concanavalin A / Q000378:metabolism; D037102:Lectins; D009174:Mycoplasma / Q000378:metabolism*; D009176:Mycoplasma mycoides / Q000378:metabolism; D011402:Pronase / Q000494:pharmacology; D011952:Receptors, Concanavalin A / Q000187:drug effects; D011955:Receptors, Drug / Q000187:drug effects; D014357:Trypsin / Q000494:pharmacology
D037102:Lectins; D011952:Receptors, Concanavalin A; D011955:Receptors, Drug; D003208:Concanavalin A; D014357:Trypsin; D011402:Pronase