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Electron microscopy of solubilized Acholeplasma laidlawii membrane proteins reaggregated with Mycoplasma pneumoniae glycolipids

1971; Elsevier BV; Volume: 233; Issue: 1 Linguagem: Inglês

10.1016/0005-2736(71)90359-2

1879-2642

Roger M. Cole, T J Popkin, Benjamin Prescott, Robert M. Chanock, Sergey V. Razin,

Antibiotics Pharmacokinetics and Efficacy

1. The purified glycolipid haptens of Mycoplasma pneumoniae were reaggregated with Acholeplasma laidlawii membrane proteins. The process consisted of the solubilization of lipid-depleted A. laidlawii membranes and M. pneumoniae glycolipids in 20 mM sodium dodecyl sulfate, and dialysis of the solution separately or in mixtures against 20 mM Mg2+. 2. The reaggregated material collected by centrifugation of the dialyzed solution of lipid-depleted A. laidlawii membrane proteins consisted of amorphous clumps, while the reaggregated M. pneumoniae glycolipids consisted of “myelin-like” globules and sheets composed of lamellae with a mean center-to-center distance of 37 Å. The reaggregated material of a mixture of lipid-depleted A. laidlawii membrane proteins and M. pneumoniae glycolipids contained, in addition to the amorphous clumps representing reaggregated proteins and the “myelin-like” structures representing reaggregated glycolipids, also long membranous sheets having a triple-layered structure with a mean center-to-center distance of the dense lines of 54 Å. The appearance and dimensions are closely similar to those of the original or reagregated A. laidlawii membranes. 3. It is suggested that these membrane-like structures are formed by the association of A. laidlawii membrane protein and M. pneumoniae glycolipids, and that these “hybrid” structures are responsible for the increased antigenicity of the reaggregated glycolipids.