caa a22 4500 397593384 CHVBK 20180308164945.0 cr unu---uuuuu 161202e199604 xx s 000 0 eng 10.1093/jac/37.4.665 doi (NATIONALLICENCE)oxford-10.1093/jac/37.4.665 Temperature-dependent aminoglycoside resistance in Stenotrophomonas (Xanthomonas) maltophilia; alterations in protein and lipopolysaccharide with growth temperature [Elektronische Daten] [Ahmad Rahmati-Bahram, John T Magee, Simon K. Jackson] Clinical strains of Stenotrophomonas (Xanthomonas) maltophilia often show large, growth temperature-dependent, variations in their susceptibility (TDVS) to aminoglycoside antibiotics. Strains showing more than a fourfold increase in susceptibility between 30° and 37°C (TDVS+strains; n=23) were contrasted with those showing lesser variation (TDVS-strains; n=15) in studies of growth temperature-dependent variation in protein and cell-wall lipopolysaccharide (LPS) electrophoresis patterns in an attempt to determine the mechanism of TDVS. Several proteins showed increased intensity with increasing growth temperature. These comprised bands at c. 65, 55, 42.5, 26 and 21.5 kDa in the whole cell proteins, an outer membrane protein band at c. 21.5 kDa, and cytoplasmic membrane protein bands at c. 42.5 and 27 kDa. Two whole cell protein bands at c. 30 and 24 kDa and three outer membrane protein bands at c. 45, 30 and 24 kDa decreased in intensity with increasing growth temperature. However, there was no correlation with the extent of variation in susceptibility, either in the extent of temperature dependent changes in protein banding patterns, or the presence or absence of specific protein bands. By contrast, temperature-dependent variation in LPS patterns correlated well with TDVS. TDVS+ strains yielded intense ladder patterns of more than 30 discrete bands, and the mean molecular weight of the ladder pattern was markedly higher at growth temperatures ≤30°C, than at ≥37°C. TDVS- strains gave a clearly distinct high mol. wt LPS banding pattern showing fewer, less intense bands and a smaller and less consistent shift in mean molecular weight with temperature. Strains which were clearly resistant at 30° and 37°C, had a high mol. wt. polysaccharide component but an absence of the typical LPS-ladder pattern. We conclude that the temperature-dependent variation in the aminoglycoside susceptibility of this species was not correlated with any detectable change in protein composition, but correlated well with changes in LPS structure. © 1996 The British Society for Antimicrobial Chemotherapy Original articles nationallicence Rahmati-Bahram Ahmad Department of Medical Microbiology and Public Health Laboratory, University of Wales College of Medicine, Cardiff CF4 4XN, UK aut Magee John T. Department of Medical Microbiology and Public Health Laboratory, University of Wales College of Medicine, Cardiff CF4 4XN, UK aut Jackson Simon K. Department of Medical Microbiology and Public Health Laboratory, University of Wales College of Medicine, Cardiff CF4 4XN, UK aut Journal of Antimicrobial Chemotherapy Oxford University Press 37/4(1996-04), 665-676 0305-7453 37:4<665 1996 37 jac https://doi.org/10.1093/jac/37.4.665 text/html Onlinezugriff via DOI 1 research-article jats NATIONALLICENCE 856 40 https://doi.org/10.1093/jac/37.4.665 text/html Onlinezugriff via DOI NATIONALLICENCE 700 1- Rahmati-Bahram Ahmad Department of Medical Microbiology and Public Health Laboratory, University of Wales College of Medicine, Cardiff CF4 4XN, UK aut NATIONALLICENCE 700 1- Magee John T. Department of Medical Microbiology and Public Health Laboratory, University of Wales College of Medicine, Cardiff CF4 4XN, UK aut NATIONALLICENCE 700 1- Jackson Simon K. Department of Medical Microbiology and Public Health Laboratory, University of Wales College of Medicine, Cardiff CF4 4XN, UK aut NATIONALLICENCE 773 0- Journal of Antimicrobial Chemotherapy Oxford University Press 37/4(1996-04), 665-676 0305-7453 37:4<665 1996 37 jac Metadata rights reserved CC BY-NC-4.0 http://creativecommons.org/licenses/by-nc/4.0 nationallicence BK010053 XK010053 XK010000 NATIONALLICENCE NATIONALLICENCE NL-oxford