Fig. 3.

Native TprC and TprI are amphiphilic but tethered to the peptidoglycan sacculus, whereas TprF is tightly bound to the peptidoglycan sacculus. a Triton X-114 phase partitioning of T. pallidum lysates without (−) or with (+) pre-solubilization with 2% DDM. Whole cells (WC), Triton X-114-insoluble material (Ins), and aqueous and Triton X-114-enriched phases (Aq and Det, respectively) were separated by SDS-PAGE followed by immunoblotting using antisera specific for TprC (top), TprI (middle), or TprI and F (bottom). Arrowheads in bottom panel indicate TprF; TprI is the larger protein. Reproduced from reference (Anand et al. 2015). b Extensively washed Triton X-114-insoluble material visualized in negatively stained whole mounts by transmission electron microscopy. Previous studies have shown that this material contains the peptidoglycan sacculus (Radolf et al. 1989a). Reproduced from reference (Anand et al. 2015). c Bipartite model for Tpr C/D and TprI. d Structural model of TprC (Nichols) generated using TMBpro (Randall et al. 2008) predicts a 10-stranded β-barrel