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Antimicrobial Agents and Chemotherapy logoLink to Antimicrobial Agents and Chemotherapy
. 1990 Sep;34(9):1725–1732. doi: 10.1128/aac.34.9.1725

Nucleotide sequence and phylogeny of SHV-2 beta-lactamase.

A Huletsky 1, F Couture 1, R C Levesque 1
PMCID: PMC171913  PMID: 2285285

Abstract

We determined the nucleotide sequence of the blaSHV-2(pBP60-1) gene from Klebsiella ozaenae which confers resistance to broad-spectrum cephalosporins. The structural gene encodes a polypeptide product of 286 amino acids, and the estimated molecular weight of the mature protein is 28,900. Amino acid sequence comparison of the SHV-2pBP60-1 enzyme with all known class A beta-lactamases and homology studies showed that the residues were highly conserved. Furthermore, SHV-2pBP60-1 was clearly related to SHV-1, LEN-1, and OHIO-1. The SHV-2pBP60-1 enzyme differed from SHV-1 isolated from Klebsiella pneumoniae by seven amino acid substitutions. One of these substitutions, the Gly----Ser substitution at position 234, is probably a key region for the novel activity of cefotaxime hydrolysis. A phylogenetic tree was constructed by using all class A beta-lactamases of known sequences by a progressive alignment method. The data suggested that the beta-lactamases of gram-positive Streptomyces, Staphylococcus, and Bacillus species appeared early in evolution, followed by the PSE and CARB enzymes of Pseudomonas species and, more recently, by the SHV-type and TEM-type enzymes found in enteric bacteria. Larger evolutionary distances separated clusters of the gram-positive beta-lactamases than separated clusters of the gram-negative enzymes. Results of this phylogenetic study suggested that extended-spectrum enzymes are recent derivatives that are selected by the use of new cephalosporins.

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Selected References

These references are in PubMed. This may not be the complete list of references from this article.

  1. Ambler R. P. The structure of beta-lactamases. Philos Trans R Soc Lond B Biol Sci. 1980 May 16;289(1036):321–331. doi: 10.1098/rstb.1980.0049. [DOI] [PubMed] [Google Scholar]
  2. 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]
  3. Barthélémy M., Peduzzi J., Labia R. Complete amino acid sequence of p453-plasmid-mediated PIT-2 beta-lactamase (SHV-1). Biochem J. 1988 Apr 1;251(1):73–79. doi: 10.1042/bj2510073. [DOI] [PMC free article] [PubMed] [Google Scholar]
  4. Barthélémy M., Péduzzi J., Ben Yaghlane H., Labia R. Single amino acid substitution between SHV-1 beta-lactamase and cefotaxime-hydrolyzing SHV-2 enzyme. FEBS Lett. 1988 Apr 11;231(1):217–220. doi: 10.1016/0014-5793(88)80734-8. [DOI] [PubMed] [Google Scholar]
  5. Boissinot M., Levesque R. C. Nucleotide sequence of the PSE-4 carbenicillinase gene and correlations with the Staphylococcus aureus PC1 beta-lactamase crystal structure. J Biol Chem. 1990 Jan 15;265(2):1225–1230. [PubMed] [Google Scholar]
  6. Boyer H. W., Roulland-Dussoix D. A complementation analysis of the restriction and modification of DNA in Escherichia coli. J Mol Biol. 1969 May 14;41(3):459–472. doi: 10.1016/0022-2836(69)90288-5. [DOI] [PubMed] [Google Scholar]
  7. Buré A., Legrand P., Arlet G., Jarlier V., Paul G., Philippon A. Dissemination in five French hospitals of Klebsiella pneumoniae serotype K25 harbouring a new transferable enzymatic resistance to third generation cephalosporins and aztreonam. Eur J Clin Microbiol Infect Dis. 1988 Dec;7(6):780–782. doi: 10.1007/BF01975048. [DOI] [PubMed] [Google Scholar]
  8. Bush K. Characterization of beta-lactamases. Antimicrob Agents Chemother. 1989 Mar;33(3):259–263. doi: 10.1128/aac.33.3.259. [DOI] [PMC free article] [PubMed] [Google Scholar]
  9. 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]
  10. Bush K. Classification of beta-lactamases: groups 2c, 2d, 2e, 3, and 4. Antimicrob Agents Chemother. 1989 Mar;33(3):271–276. doi: 10.1128/aac.33.3.271. [DOI] [PMC free article] [PubMed] [Google Scholar]
  11. 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]
  12. 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]
  13. Feng D. F., Doolittle R. F. Progressive sequence alignment as a prerequisite to correct phylogenetic trees. J Mol Evol. 1987;25(4):351–360. doi: 10.1007/BF02603120. [DOI] [PubMed] [Google Scholar]
  14. Fitch W. M., Margoliash E. Construction of phylogenetic trees. Science. 1967 Jan 20;155(3760):279–284. doi: 10.1126/science.155.3760.279. [DOI] [PubMed] [Google Scholar]
  15. Guerry P., LeBlanc D. J., Falkow S. General method for the isolation of plasmid deoxyribonucleic acid. J Bacteriol. 1973 Nov;116(2):1064–1066. doi: 10.1128/jb.116.2.1064-1066.1973. [DOI] [PMC free article] [PubMed] [Google Scholar]
  16. Gutmann L., Ferré B., Goldstein F. W., Rizk N., Pinto-Schuster E., Acar J. F., Collatz E. SHV-5, a novel SHV-type beta-lactamase that hydrolyzes broad-spectrum cephalosporins and monobactams. Antimicrob Agents Chemother. 1989 Jun;33(6):951–956. doi: 10.1128/aac.33.6.951. [DOI] [PMC free article] [PubMed] [Google Scholar]
  17. Herzberg O., Moult J. Bacterial resistance to beta-lactam antibiotics: crystal structure of beta-lactamase from Staphylococcus aureus PC1 at 2.5 A resolution. Science. 1987 May 8;236(4802):694–701. doi: 10.1126/science.3107125. [DOI] [PubMed] [Google Scholar]
  18. 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]
  19. Jarlier V., Nicolas M. H., Fournier G., Philippon A. Extended broad-spectrum beta-lactamases conferring transferable resistance to newer beta-lactam agents in Enterobacteriaceae: hospital prevalence and susceptibility patterns. Rev Infect Dis. 1988 Jul-Aug;10(4):867–878. doi: 10.1093/clinids/10.4.867. [DOI] [PubMed] [Google Scholar]
  20. 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]
  21. 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]
  22. Kliebe C., Nies B. A., Meyer J. F., Tolxdorff-Neutzling R. M., Wiedemann B. Evolution of plasmid-coded resistance to broad-spectrum cephalosporins. Antimicrob Agents Chemother. 1985 Aug;28(2):302–307. doi: 10.1128/aac.28.2.302. [DOI] [PMC free article] [PubMed] [Google Scholar]
  23. Klotz L. C., Blanken R. L. A practical method for calculating evolutionary trees from sequence data. J Theor Biol. 1981 Jul 21;91(2):261–272. doi: 10.1016/0022-5193(81)90233-2. [DOI] [PubMed] [Google Scholar]
  24. Knothe H., Shah P., Krcmery V., Antal M., Mitsuhashi S. Transferable resistance to cefotaxime, cefoxitin, cefamandole and cefuroxime in clinical isolates of Klebsiella pneumoniae and Serratia marcescens. Infection. 1983 Nov-Dec;11(6):315–317. doi: 10.1007/BF01641355. [DOI] [PubMed] [Google Scholar]
  25. Medeiros A. A. Beta-lactamases. Br Med Bull. 1984 Jan;40(1):18–27. doi: 10.1093/oxfordjournals.bmb.a071942. [DOI] [PubMed] [Google Scholar]
  26. Medeiros A. A., Levesque R., Jacoby G. A. An animal source for the ROB-1 beta-lactamase of Haemophilus influenzae type b. Antimicrob Agents Chemother. 1986 Feb;29(2):212–215. doi: 10.1128/aac.29.2.212. [DOI] [PMC free article] [PubMed] [Google Scholar]
  27. 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]
  28. Messing J. New M13 vectors for cloning. Methods Enzymol. 1983;101:20–78. doi: 10.1016/0076-6879(83)01005-8. [DOI] [PubMed] [Google Scholar]
  29. Needleman S. B., Wunsch C. D. A general method applicable to the search for similarities in the amino acid sequence of two proteins. J Mol Biol. 1970 Mar;48(3):443–453. doi: 10.1016/0022-2836(70)90057-4. [DOI] [PubMed] [Google Scholar]
  30. 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]
  31. Oliver D. Protein secretion in Escherichia coli. Annu Rev Microbiol. 1985;39:615–648. doi: 10.1146/annurev.mi.39.100185.003151. [DOI] [PubMed] [Google Scholar]
  32. Philippon A., Labia R., Jacoby G. Extended-spectrum beta-lactamases. Antimicrob Agents Chemother. 1989 Aug;33(8):1131–1136. doi: 10.1128/aac.33.8.1131. [DOI] [PMC free article] [PubMed] [Google Scholar]
  33. Radloff R., Bauer W., Vinograd J. A dye-buoyant-density method for the detection and isolation of closed circular duplex DNA: the closed circular DNA in HeLa cells. Proc Natl Acad Sci U S A. 1967 May;57(5):1514–1521. doi: 10.1073/pnas.57.5.1514. [DOI] [PMC free article] [PubMed] [Google Scholar]
  34. Sanger F., Nicklen S., Coulson A. R. DNA sequencing with chain-terminating inhibitors. Proc Natl Acad Sci U S A. 1977 Dec;74(12):5463–5467. doi: 10.1073/pnas.74.12.5463. [DOI] [PMC free article] [PubMed] [Google Scholar]
  35. 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]
  36. Shlaes D. M., Medeiros A. A., Kron M. A., Currie-McCumber C., Papa E., Vartian C. V. Novel plasmid-mediated beta-lactamase in members of the family Enterobacteriaceae from Ohio. Antimicrob Agents Chemother. 1986 Aug;30(2):220–224. doi: 10.1128/aac.30.2.220. [DOI] [PMC free article] [PubMed] [Google Scholar]
  37. Sloma A., Gross M. Molecular cloning and nucleotide sequence of the type I beta-lactamase gene from Bacillus cereus. Nucleic Acids Res. 1983 Jul 25;11(14):4997–5004. doi: 10.1093/nar/11.14.4997. [DOI] [PMC free article] [PubMed] [Google Scholar]
  38. 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]
  39. Vieira J., Messing J. Production of single-stranded plasmid DNA. Methods Enzymol. 1987;153:3–11. doi: 10.1016/0076-6879(87)53044-0. [DOI] [PubMed] [Google Scholar]
  40. Woese C. R. Bacterial evolution. Microbiol Rev. 1987 Jun;51(2):221–271. doi: 10.1128/mr.51.2.221-271.1987. [DOI] [PMC free article] [PubMed] [Google Scholar]

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