Gorton T S, Geary S J
University of Connecticut, Department of Pathobiology, Storrs, USA.
FEMS Microbiol Lett. 1997 Oct 1;155(1):31-8. doi: 10.1111/j.1574-6968.1997.tb12682.x.
A variant phenotype of Mycoplasma gallisepticum S6 was isolated from an in vitro antibody-culture system utilizing metabolism-inhibiting antibodies against the 64 kDa lipoprotein (LP64). M. gallisepticum populations grown in medium alone or medium containing normal rabbit serum maintained expression of the parental phenotype. This paper describes the identification of proteins which undergo variable expression. Several of these were integral membrane proteins, with estimated molecular masses of 91, 43, 41, 38, 37, and 18 kDa, which were expressed in the variant phenotype but not in the parental phenotype. Three proteins (LP64, p63 and p47) were expressed in the parental phenotype, but not in the variant phenotype. The data suggest that the interaction of specific immunoglobulins with target epitopes resulted in the selection of a subpopulation of organisms expressing an alternative array of membrane proteins which, lacking the target epitopes, was able to escape the metabolism-inhibiting effects of the specific antibodies.
