Capsular polysaccharides (CPSs) are virulence factors for many important pathogens. In Escherichia coli, CPSs are synthesized via two distinct pathways, but both require proteins from the outer membrane polysaccharide export (OPX) family to complete CPS export from the periplasm to the cell surface. In this study, we compare the properties of the OPX proteins from the prototypical group 1 (Wzydependent) and group 2 (ABC transporter-dependent) pathways in E. coli K30 (Wza) and E. coli K2 (KpsD), respectively. In addition, we compare an OPX from Salmonella enterica serovar Typhi (VexA), which shares structural properties with Wza, while operating in an ABC transporter-dependent pathway. These proteins differ in distribution in the cell envelope and formation of stable multimers, but these properties do not align with acylation or the interfacing biosynthetic pathway. In E. coli K2, murein lipoprotein (Lpp) plays a role in peptidoglycan association of KpsD, and loss of this interaction correlates with impaired group 2 capsule production. VexA also depends on Lpp for peptidoglycan association, but CPS production is unaffected in an lpp mutant. In contrast, Wza and group 1 capsule production is unaffected by the absence of Lpp. These results point to complex structure-function relationships between different OPX proteins. IMPORTANCE Capsules are protective layers of polysaccharides that surround the cell surface of many bacteria, including that of Escherichia coli isolates and Salmonella enterica serovar Typhi. Capsular polysaccharides (CPSs) are often essential for virulence because they facilitate evasion of host immune responses. The attenuation of unencapsulated mutants in animal models and the involvement of protein families with conserved features make the CPS export pathway a novel candidate for therapeutic strategies. However, appropriate "antivirulence" strategies require a fundamental understanding of the underpinning cellular processes. Investigating export proteins that are conserved across different biosynthesis strategies will give important insight into how CPS is transported to the cell surface.

A new radiofrequency procedure, i.c., the CMT Selectotherm technique, permits to convey large heat quantities per volume unit also to deep-seated tumor tissues without causing thermal lesions in healthy tissues near or at the body surface. The improved spatial homogeneity of energy supply attainable by this method is demonstrated by measurements at a gelatine phantom and, in particular, by in vivo measurements on pigs. The appliability of local hyperthermy to tumors localized in different parts of the body is substantially improved (a) by the principle of superimposing local hyperthermy on an elevated temperature level of metabolically induced whole-body hyperthermy (CMT-spontaneous hyperthermy at 40 degrees C) and (b) by the principle of selective increasing the thermal sensitivity of tumor tissues by decreasing the pH in these areas (the CMT main step). It is shown that the temperature dose T. deltat necessary for the selective occlusion of the vasculature in tumor tissues can be obtained by the CMT Selectotherm process also in deep-seated tumors. This process is part of the 1977 CMT concept. The fundamentals of optimizing local hyperthermy with consideration of heat dissipation from the tissue by heat conduction and convection via the blood stream are demonstrated. Temperature profiles are calculated for some practice-relevant, typical examples (inner and outer parts of sphero-symmetrically shaped tumors). Finally, in vivo measurements and calculations on the time course of temperature under certain conditions and for different tissue layers are discussed.