Susceptibility to β-lactam antibiotics of mutant strains of Xanthomonas maltophilia with high- and low-level constitutive expression of L1 and L2 β-lactamases

References

1. Müder RR, Yu VL, Dummer JS, Vinson C, Lumish RM. Infections caused by Pseudomonas maltophilia: expanding clinical spectrum. Arch Intern Med 1987; 147:1672–1674
   [Google Scholar]
2. von Graevenitz A. Ecology, clinical significance and antimicrobial susceptibility of infrequently encountered glucose-non-fermenting gram-negative rods. Gilardi G. ed Nonfermentative gram-negative rods: laboratory identification and clinical aspects (Microbiology series 16) New York: Marcel Dekker Inc; 1985181–232
   [Google Scholar]
3. Marshall WF, Keating MR, Anhalt JP, Steckelberg JM. Xanthomonas maltophilia: an emerging nosocomial pathogen. Mayo Clin Proc 1989; 64:1097–1104
   [Google Scholar]
4. Rolston KVI, Anaissie EA, Bodey GP. In-vitro susceptibility of Pseudomonas species to fifteen antimicrobial agents. J Antimicrob Chemother 1987; 19:193–196
   [Google Scholar]
5. Saino Y, Kobayashi F, Inoue M, Mitsuhashi S. Purification and properties of inducible penicillin β-lactamases isolated from Pseudomonas maltophilia. Antimicrob Agents Chemother 1982; 22:564–570
   [Google Scholar]
6. Saino Y, Inoue M, Mitsuhashi S. Purification and properties of an inducible cephalosporinase from Pseudomonas maltophilia GN12873. Antimicrob Agents Chemother 1984; 25:362–365
   [Google Scholar]
7. Mett H, Rosta S, Schacher B, Frei R. Outer membrane permeability and β-lactamases content in Pseudomonas maltophilia clinical isolates and laboratory mutants. Rev Infect Dis 1988; 10:765–769
   [Google Scholar]
8. Bicknell R, Emanuel EL, Gagnon J, Waley SG. The production and molecular properties of the zinc β-lactamases of Pseudomonas maltophilia IID 1275. Biochem J 1985; 229:791–797
   [Google Scholar]
9. Cartwright SJ, Waley SG. Purification of β-lactamases by affinity chromatography on phenylboronic acid-agarose. Biochem J 1984; 221:505–512
   [Google Scholar]
10. Edwards JR, Turner PJ, Wannop C, Withnell ES, Grindey AJ, Nairn K. In-vitro antibacterial activity of SM-7338, a carbapenem antibiotic with stability to dehydropeptidase I. Antimicrob Agents Chemother 1989; 33:215–222
    [Google Scholar]
11. King A, Boothman C, Phillips I. Comparative in-vitro activity of meropenem on clinical isolates from the United Kingdom. J Antimicrob Chemother 1989; 24:Suppl A31–45
    [Google Scholar]
12. Cullmann W, Dalhoff A, Dick W. Nonspecific induction of β-lactamase in Enterobacter cloacae. J Gen Microbiol 1984; 130:1781–1786
    [Google Scholar]
13. Yang Y, Livermore DM, Williams RJ. Chromosomal β-lactamase expression and antibiotic resistance in Enterobacter cloacae. J Med Microbiol 1988; 25:227–233
    [Google Scholar]
14. Lowry OH, Rosebrough NJ, Farr AL, Randall RJ. Protein measurement with the Folin phenol reagent. J Biol Chem 1951; 193:265–275
    [Google Scholar]
15. Matthew M, Harris AM, Marshall MJ, Ross GW. The use of analytical isoelectric focusing for detection and identification of β-lactamases. J Gen Microbiol 1975; 88:169–178
    [Google Scholar]
16. Yang Y. Chromosomal β-lactamases expression and antibiotic resistance in enterobacteria. PhD Thesis University of London: 1990
    [Google Scholar]
17. Dufresne J, Vézina G, Levesque RC. Molecular cloning and expression of the imipenem-hydrolyzing β-lactamases gene from Pseudomonas maltophilia in Escherichia coli. Rev Infect Dis 1988; 10:806–817
    [Google Scholar]
18. Livermore DM. Clinical significance of beta-lactamase-induc-tion and stable derepression in gram-negative rods. Eur J Clin Microbiol 1987; 6:439–445
    [Google Scholar]