Inactivation of mrcA gene derepresses the basal-level expression of L1 and L2 β-lactamases in Stenotrophomonas maltophilia

Journal of Antimicrobial Chemotherapy

Volumn 66, Issue 9, 2011, Pages 2033-2037

  Lin, Cheng Wen ^a,b   Lin, Hsin Chieh ^a   Huang, Yi Wei ^c   Chung, Tung Ching ^c   Yang, Tsuey Ching ^a,d  

^a CHINA MEDICAL UNIVERSITY   (Taiwan)

^b ASIA UNIVERSITY   (Taiwan)

^c NATIONAL CHUNG HSING UNIVERSITY   (Taiwan)

^d NATIONAL YANG MING UNIVERSITY   (Taiwan)

Author keywords

PBPs; Penicillin binding proteins; S. maltophilia

Indexed keywords

AZTREONAM; BETA LACTAMASE; CARBENICILLIN; CEFEPIME; CEFOXITIN; CEFUROXIME; IMIPENEM; L1 BETA LACTAMASE; L2 BETA LACTAMASE; MEMBRANE PROTEIN; MEROPENEM; PENICILLIN BINDING PROTEIN 1A; PIPERACILLIN; PROTEIN AMPDI; PROTEIN AMPG; PROTEIN AMPN; PROTEIN AMPR; PROTEIN CREBC; PROTEIN MRCA; UNCLASSIFIED DRUG;

ALLELE; ARTICLE; ENZYME ACTIVITY; ENZYME SYNTHESIS; GENE EXPRESSION; GENE INACTIVATION; MINIMUM INHIBITORY CONCENTRATION; NONHUMAN; NUCLEOTIDE SEQUENCE; REGULON; STENOTROPHOMONAS MALTOPHILIA;

ANTI-BACTERIAL AGENTS; BETA-LACTAMASES; DNA PRIMERS; ENZYME INDUCTION; ESCHERICHIA COLI; GENES, BACTERIAL; LACTAMS; MICROBIAL SENSITIVITY TESTS; MOLECULAR SEQUENCE DATA; MUTATION; PLASMIDS; REGULON; STENOTROPHOMONAS MALTOPHILIA;

EID: 80051689677     PISSN: 03057453     EISSN: 14602091     Source Type: Journal    
DOI: 10.1093/jac/dkr276     Document Type: Article

References (15)

1. Henderson TA, Young KD, Denome SA et al. AmpC and AmpH, proteins related to the class C β-lactamases, bind penicillin and contribute to the normal morphology of Escherichia coli. J Bacteriol 1997; 179: 6112-21.
2. Jacobs C, Frere JM, Normark S. Cytosolic intermediates for cell wall biosynthesis and degradation control inducible β-lactam resistance in gram-negative bacteria. Cell 1997; 88: 823-32.
3. Moya B, Dotsch A, Juan C et al. β-Lactam resistance response triggered by inactivation of a nonessential penicillin-binding protein. PLos Pathog 2009; 5: e1000353.
4. Huang YW, Lin CW, Hu RM et al. AmpN-AmpG operon is essential for expression of L1 and L2 β-lactamases in Stenotrophomonas maltophilia. Antimicrob Agents Chemother 2010; 54: 2583-9.
5. I is involved in expression of the chromosomal L1 and L2 β-lactamases of Stenotrophomonas maltophilia. Antimicrob Agents Chemother 2009; 53: 2902-7.
6. Okazaki A, Avison MB. Induction of L1 and L2 β-lactamase production in Stenotrophomonas maltophilia is dependent on an AmpR-type regulator. Antimicrob Agents Chemother 2008; 52: 1525-8.
7. Lin CW, Huang YW, Hu RM et al. The role of AmpR in regulation of L1 and L2 β-lactamases in Stenotrophomonas maltophilia. Res Microbiol 2009; 160: 152-8.
8. Crossman LC, Gould VC, Dow JM et al. The complete genome, comparative and functional analysis of Stenotrophomonas maltophilia reveals an organism heavily shielded by drug resistance determinants. Genome Biol 2008; 9: R74.
9. Hu RM, Huang KJ, Wu LT et al. Induction of L1 and L2 β-lactamases of Stenotrophomonas maltophilia. Antimicrob Agents Chemother 2008; 52: 1198-200.
10. Alksen LE, Rasmussen BA. Expression of the AsbA1, OXA-12, and AsbM1 β-lactamases in Aeromonas jandaei AER14 is coordinated by a two-component regulon. J Bacteriol 1997; 179: 2006-13.
11. Oliva B, Bennett PM, Chopra I. Penicillin-binding protein 2 is required for induction of the Citrobacter freundii class I chromosomal β-lactamase in Escherichia coli. Antimicrob Agents Chemother 1989; 33: 1116-7.
12. Sanders CC, Bradford PA, Ehrhardt AF et al. Penicillin-binding proteins and induction of AmpC β-lactamase. Antimicrob Agents Chemother 1997; 41: 2013-5.
13. Pfeifle D, Janas E, Wiedemann B. Role of penicillin-binding proteins in the initiation of the AmpC β-lactamase expression in Enterobacter cloacae. Antimicrob Agents Chemother 2000; 44: 169-72.
14. Tayler AE, Ayala JA, Niumsup P et al. Induction of β-lactamase production in Aeromonas hydrophilia is responsive to β-lactam-mediated changes in peptidoglycan composition. Microbiology 2010; 156: 2327-35.
15. Zapun A, Contreras-Martel C, Vernet T. Penicillin-binding proteins and β-lactam resistance. FEMS Microbiol Rev 2008; 32: 361-85.