Abstract
The chromosomally encoded beta-lactamase gene (blaOXY-2) of the wild-type Klebsiella oxytoca SL911 was cloned and sequenced. Its nucleotide sequence similarity with the previously sequenced K. oxytoca beta-lactamase gene (blaOXY-1) (Y. Arakawa, M. Ohta, N. Kido, M. Mori, H. Ito, T. Komatsu, Y. Fujii, and N. Kato, Antimicrob. Agents Chemother. 33:63-70, 1989) is 87.3%, and its amino acid similarity is 89.7%. This group of K. oxytoca beta-lactamases is related to chromosomal beta-lactamases of Citrobacter diversus, Proteus vulgaris, and Yersinia enterocolitica and to the plasmid-mediated extended-spectrum beta-lactamases MEN-1 and Toho-1. By colony hybridization with 86 strains susceptible and resistant to aztreonam, isolated in six countries, K. oxytoca beta-lactamase genes hybridized with either a specific blaOXY-1 DNA probe (668 bp) or a blaOXY-2 DNA probe (723 bp). Thus, beta-lactamase genes could be divided into two groups: blaOXY-1 (47% of the strains) and blaOXY-2 (53% of the strains). A study of isoelectric points confirmed the great variability reported in the literature. However, the two beta-lactamase groups were each represented by four different pIs: for OXY-2, 5.2, 5.7, 6.4, and 6.8, with the 5.2 form representing 59% of all OXY-2 enzymes, and for OXY-1, 7.1, 7.5, 8.2, and 8.8, with the 7.5 form representing 88% of all OXY-1 enzymes.
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- Ambler R. P., Coulson A. F., Frère J. M., Ghuysen J. M., Joris B., Forsman M., Levesque R. C., Tiraby G., Waley S. G. A standard numbering scheme for the class A beta-lactamases. Biochem J. 1991 May 15;276(Pt 1):269–270. doi: 10.1042/bj2760269. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Arakawa Y., Ohta M., Kido N., Fujii Y., Komatsu T., Kato N. Close evolutionary relationship between the chromosomally encoded beta-lactamase gene of Klebsiella pneumoniae and the TEM beta-lactamase gene mediated by R plasmids. FEBS Lett. 1986 Oct 20;207(1):69–74. doi: 10.1016/0014-5793(86)80014-x. [DOI] [PubMed] [Google Scholar]
- Arakawa Y., Ohta M., Kido N., Mori M., Ito H., Komatsu T., Fujii Y., Kato N. Chromosomal beta-lactamase of Klebsiella oxytoca, a new class A enzyme that hydrolyzes broad-spectrum beta-lactam antibiotics. Antimicrob Agents Chemother. 1989 Jan;33(1):63–70. doi: 10.1128/aac.33.1.63. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Arlet G., Philippon A. Construction by polymerase chain reaction and use of intragenic DNA probes for three main types of transferable beta-lactamases (TEM, SHV, CARB) [corrected]. FEMS Microbiol Lett. 1991 Jul 15;66(1):19–25. doi: 10.1016/0378-1097(91)90414-6. [DOI] [PubMed] [Google Scholar]
- Barthélémy M., Péduzzi J., Bernard H., Tancrède C., Labia R. Close amino acid sequence relationship between the new plasmid-mediated extended-spectrum beta-lactamase MEN-1 and chromosomally encoded enzymes of Klebsiella oxytoca. Biochim Biophys Acta. 1992 Jul 13;1122(1):15–22. doi: 10.1016/0167-4838(92)90121-s. [DOI] [PubMed] [Google Scholar]
- Boras G. J., Au S., Roy K. L., von Tigerstrom R. G. beta-Lactamase of Lysobacter enzymogenes: cloning, characterization and expression of the gene and comparison of the enzyme to other lactamases. J Gen Microbiol. 1993 Jun;139(Pt 6):1245–1252. doi: 10.1099/00221287-139-6-1245. [DOI] [PubMed] [Google Scholar]
- Bush K. Classification of beta-lactamases: groups 1, 2a, 2b, and 2b'. Antimicrob Agents Chemother. 1989 Mar;33(3):264–270. doi: 10.1128/aac.33.3.264. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Bush K., Jacoby G. A., Medeiros A. A. A functional classification scheme for beta-lactamases and its correlation with molecular structure. Antimicrob Agents Chemother. 1995 Jun;39(6):1211–1233. doi: 10.1128/aac.39.6.1211. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Chan P. T. Nucleotide sequence of the Staphylococcus aureus PC1 beta-lactamase gene. Nucleic Acids Res. 1986 Jul 25;14(14):5940–5940. doi: 10.1093/nar/14.14.5940. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Chardon H., Pachetti C., Collet L., Bellon O., Lagier E. Détermination du point isoélectrique des bêtalactamases extraites de 67 souches de Klebsiella oxytoca et comportement phénotypique vis-a-vis de huit bêtalactamines. Pathol Biol (Paris) 1993 Apr;41(4):343–348. [PubMed] [Google Scholar]
- Coque J. J., Liras P., Martín J. F. Genes for a beta-lactamase, a penicillin-binding protein and a transmembrane protein are clustered with the cephamycin biosynthetic genes in Nocardia lactamdurans. EMBO J. 1993 Feb;12(2):631–639. doi: 10.1002/j.1460-2075.1993.tb05696.x. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Dehottay P., Dusart J., De Meester F., Joris B., Van Beeumen J., Erpicum T., Frère J. M., Ghuysen J. M. Nucleotide sequence of the gene encoding the Streptomyces albus G beta-lactamase precursor. Eur J Biochem. 1987 Jul 15;166(2):345–350. doi: 10.1111/j.1432-1033.1987.tb13521.x. [DOI] [PubMed] [Google Scholar]
- Forsman M., Häggström B., Lindgren L., Jaurin B. Molecular analysis of beta-lactamases from four species of Streptomyces: comparison of amino acid sequences with those of other beta-lactamases. J Gen Microbiol. 1990 Mar;136(3):589–598. doi: 10.1099/00221287-136-3-589. [DOI] [PubMed] [Google Scholar]
- Fournier B., Arlet G., Lagrange P. H., Philippon A. Klebsiella oxytoca: resistance to aztreonam by overproduction of the chromosomally encoded beta-lactamase. FEMS Microbiol Lett. 1994 Feb 1;116(1):31–36. doi: 10.1111/j.1574-6968.1994.tb06671.x. [DOI] [PubMed] [Google Scholar]
- Fournier B., Lu C. Y., Lagrange P. H., Krishnamoorthy R., Philippon A. Point mutation in the pribnow box, the molecular basis of beta-lactamase overproduction in Klebsiella oxytoca. Antimicrob Agents Chemother. 1995 Jun;39(6):1365–1368. doi: 10.1128/aac.39.6.1365. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Gotoh O. An improved algorithm for matching biological sequences. J Mol Biol. 1982 Dec 15;162(3):705–708. doi: 10.1016/0022-2836(82)90398-9. [DOI] [PubMed] [Google Scholar]
- Hussain M., Pastor F. I., Lampen J. O. Cloning and sequencing of the blaZ gene encoding beta-lactamase III, a lipoprotein of Bacillus cereus 569/H. J Bacteriol. 1987 Feb;169(2):579–586. doi: 10.1128/jb.169.2.579-586.1987. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Ishii Y., Ohno A., Taguchi H., Imajo S., Ishiguro M., Matsuzawa H. Cloning and sequence of the gene encoding a cefotaxime-hydrolyzing class A beta-lactamase isolated from Escherichia coli. Antimicrob Agents Chemother. 1995 Oct;39(10):2269–2275. doi: 10.1128/aac.39.10.2269. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Jacob F., Joris B., Lepage S., Dusart J., Frère J. M. Role of the conserved amino acids of the 'SDN' loop (Ser130, Asp131 and Asn132) in a class A beta-lactamase studied by site-directed mutagenesis. Biochem J. 1990 Oct 15;271(2):399–406. doi: 10.1042/bj2710399. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Jaurin B., Grundström T. ampC cephalosporinase of Escherichia coli K-12 has a different evolutionary origin from that of beta-lactamases of the penicillinase type. Proc Natl Acad Sci U S A. 1981 Aug;78(8):4897–4901. doi: 10.1073/pnas.78.8.4897. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Joris B., Ghuysen J. M., Dive G., Renard A., Dideberg O., Charlier P., Frère J. M., Kelly J. A., Boyington J. C., Moews P. C. The active-site-serine penicillin-recognizing enzymes as members of the Streptomyces R61 DD-peptidase family. Biochem J. 1988 Mar 1;250(2):313–324. doi: 10.1042/bj2500313. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Joris B., Ghuysen J. M., Dive G., Renard A., Dideberg O., Charlier P., Frère J. M., Kelly J. A., Boyington J. C., Moews P. C. The active-site-serine penicillin-recognizing enzymes as members of the Streptomyces R61 DD-peptidase family. Biochem J. 1988 Mar 1;250(2):313–324. doi: 10.1042/bj2500313. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Joris B., Ledent P., Dideberg O., Fonzé E., Lamotte-Brasseur J., Kelly J. A., Ghuysen J. M., Frère J. M. Comparison of the sequences of class A beta-lactamases and of the secondary structure elements of penicillin-recognizing proteins. Antimicrob Agents Chemother. 1991 Nov;35(11):2294–2301. doi: 10.1128/aac.35.11.2294. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Juteau J. M., Levesque R. C. Sequence analysis and evolutionary perspectives of ROB-1 beta-lactamase. Antimicrob Agents Chemother. 1990 Jul;34(7):1354–1359. doi: 10.1128/aac.34.7.1354. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Lachapelle J., Dufresne J., Levesque R. C. Characterization of the blaCARB-3 gene encoding the carbenicillinase-3 beta-lactamase of Pseudomonas aeruginosa. Gene. 1991 Jun 15;102(1):7–12. doi: 10.1016/0378-1119(91)90530-o. [DOI] [PubMed] [Google Scholar]
- Livermore D. M. beta-Lactamases in laboratory and clinical resistance. Clin Microbiol Rev. 1995 Oct;8(4):557–584. doi: 10.1128/cmr.8.4.557. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Madgwick P. J., Waley S. G. beta-lactamase I from Bacillus cereus. Structure and site-directed mutagenesis. Biochem J. 1987 Dec 15;248(3):657–662. doi: 10.1042/bj2480657. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Mercier J., Levesque R. C. Cloning of SHV-2, OHIO-1, and OXA-6 beta-lactamases and cloning and sequencing of SHV-1 beta-lactamase. Antimicrob Agents Chemother. 1990 Aug;34(8):1577–1583. doi: 10.1128/aac.34.8.1577. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Monnet D., Freney J. Method for differentiating Klebsiella planticola and Klebsiella terrigena from other Klebsiella species. J Clin Microbiol. 1994 Apr;32(4):1121–1122. doi: 10.1128/jcm.32.4.1121-1122.1994. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Myers E. W., Miller W. Optimal alignments in linear space. Comput Appl Biosci. 1988 Mar;4(1):11–17. doi: 10.1093/bioinformatics/4.1.11. [DOI] [PubMed] [Google Scholar]
- Naas T., Nordmann P. Analysis of a carbapenem-hydrolyzing class A beta-lactamase from Enterobacter cloacae and of its LysR-type regulatory protein. Proc Natl Acad Sci U S A. 1994 Aug 2;91(16):7693–7697. doi: 10.1073/pnas.91.16.7693. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Naas T., Vandel L., Sougakoff W., Livermore D. M., Nordmann P. Cloning and sequence analysis of the gene for a carbapenem-hydrolyzing class A beta-lactamase, Sme-1, from Serratia marcescens S6. Antimicrob Agents Chemother. 1994 Jun;38(6):1262–1270. doi: 10.1128/aac.38.6.1262. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Neugebauer K., Sprengel R., Schaller H. Penicillinase from Bacillus licheniformis: nucleotide sequence of the gene and implications for the biosynthesis of a secretory protein in a Gram-positive bacterium. Nucleic Acids Res. 1981 Jun 11;9(11):2577–2588. doi: 10.1093/nar/9.11.2577. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Pearson W. R., Lipman D. J. Improved tools for biological sequence comparison. Proc Natl Acad Sci U S A. 1988 Apr;85(8):2444–2448. doi: 10.1073/pnas.85.8.2444. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Perilli M., Franceschini N., Segatore B., Amicosante G., Oratore A., Duez C., Joris B., Frère J. M. Cloning and nucleotide sequencing of the gene encoding the beta-lactamase from Citrobacter diversus. FEMS Microbiol Lett. 1991 Sep 15;67(1):79–84. doi: 10.1016/0378-1097(91)90448-j. [DOI] [PubMed] [Google Scholar]
- Reynaud A., Péduzzi J., Barthélémy M., Labia R. Cefotaxime-hydrolysing activity of the beta-lactamase of Klebsiella oxytoca D488 could be related to a threonine residue at position 140. FEMS Microbiol Lett. 1991 Jun 15;65(2):185–192. doi: 10.1016/0378-1097(91)90301-p. [DOI] [PubMed] [Google Scholar]
- Saitou N., Nei M. The neighbor-joining method: a new method for reconstructing phylogenetic trees. Mol Biol Evol. 1987 Jul;4(4):406–425. doi: 10.1093/oxfordjournals.molbev.a040454. [DOI] [PubMed] [Google Scholar]
- Seoane A., García Lobo J. M. Nucleotide sequence of a new class A beta-lactamase gene from the chromosome of Yersinia enterocolitica: implications for the evolution of class A beta-lactamases. Mol Gen Genet. 1991 Aug;228(1-2):215–220. doi: 10.1007/BF00282468. [DOI] [PubMed] [Google Scholar]
- Shlaes D. M., Currie-McCumber C., Hull A., Behlau I., Kron M. OHIO-1 beta-lactamase is part of the SHV-1 family. Antimicrob Agents Chemother. 1990 Aug;34(8):1570–1576. doi: 10.1128/aac.34.8.1570. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Spratt B. G., Hedge P. J., te Heesen S., Edelman A., Broome-Smith J. K. Kanamycin-resistant vectors that are analogues of plasmids pUC8, pUC9, pEMBL8 and pEMBL9. Gene. 1986;41(2-3):337–342. doi: 10.1016/0378-1119(86)90117-4. [DOI] [PubMed] [Google Scholar]
- Sutcliffe J. G. Nucleotide sequence of the ampicillin resistance gene of Escherichia coli plasmid pBR322. Proc Natl Acad Sci U S A. 1978 Aug;75(8):3737–3741. doi: 10.1073/pnas.75.8.3737. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Tamaki M., Nukaga M., Sawai T. Replacement of serine 237 in class A beta-lactamase of Proteus vulgaris modifies its unique substrate specificity. Biochemistry. 1994 Aug 23;33(33):10200–10206. doi: 10.1021/bi00199a049. [DOI] [PubMed] [Google Scholar]
- Timm J., Perilli M. G., Duez C., Trias J., Orefici G., Fattorini L., Amicosante G., Oratore A., Joris B., Frère J. M. Transcription and expression analysis, using lacZ and phoA gene fusions, of Mycobacterium fortuitum beta-lactamase genes cloned from a natural isolate and a high-level beta-lactamase producer. Mol Microbiol. 1994 May;12(3):491–504. doi: 10.1111/j.1365-2958.1994.tb01037.x. [DOI] [PubMed] [Google Scholar]
- Yanisch-Perron C., Vieira J., Messing J. Improved M13 phage cloning vectors and host strains: nucleotide sequences of the M13mp18 and pUC19 vectors. Gene. 1985;33(1):103–119. doi: 10.1016/0378-1119(85)90120-9. [DOI] [PubMed] [Google Scholar]