Inhibition of metallo-β-lactamase

Organic compounds -- part of the class 532-570 series – Organic compounds – Carbohydrates or derivatives

Reexamination Certificate

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C536S024330

Reexamination Certificate

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07456274

ABSTRACT:
A method to identify a high affinity nucleic acid ligand to inhibit the activity of a lactamase enzyme. The method comprises several steps that initially involve preparing a candidate mixture of nucleic acids. The candidate mixture of nucleic acids is then allowed to make contact with the lactamase enzyme under controlled conditions of temperature, ionic strength and pH; the combination forms a candidate-enzyme mixture. The target nucleic acids are partitioned from the remainder of the candidate mixture. The target nucleic acids that have been partitioned are amplified to yield a pool of nucleic acids enriched with target nucleic acid sequences. The enriched pool of target nucleic acids have a relatively higher affinity and specificity for binding to the lactamase, whereby nucleic acid ligand of the lactamase are identified. Nucleic acid ligands that inhibit an activity of lactamase. The lactamase includes class B, metallo-β-lactamase.

REFERENCES:
patent: 5637459 (1997-06-01), Burke et al.
patent: 5705340 (1998-01-01), Rasmussen et al.
patent: 5773598 (1998-06-01), Burke et al.
patent: 2002/0095073 (2002-07-01), Jacobs et al.
patent: WO 9902165 (1999-01-01), None
Allawi, H. T. and SantaLucia, J. Jr. (1997), “Thermodynamics and NMR of Internal G-T Mismatches in DNA”,Biochemistry36, 10581-10594.
Ambler, R. P., Daniel, M., Fleming, J., Hermoso, J. -M., Pang, C. and Waley, S. G. (1985), “The Amino Acid Sequence of the Zinc-Requiring β-Lactamase II from the bacteriumBacillus cereus”, FEBS Lett.189, 207-211.
Bartel, D. P. and Szostak, J. W., (1993), “Isolation New Ribozymes from a Large Pool of Random Sequences”,Science261, 1411-1418.
Bicknell, R., Schaeffer, A., Waley, S. G. and Auld, D. S. (1986), “Changes in the Coordination Geometry of the Active-Site Metal During Catalysis of Benzylpenicillin Hydrolysis byBacillus cereusβ-Lactamase II”,Biochemistry25, 7208-7215.
Bock, L. C., Griffin, L. C., Latham, J. A., Vermass, E. H. and Toole, J. J. (1992), “Selection of Single-Stranded DNA Molecules that bind and Inhibit Human Thrombin”,Nature355, 564-566.
Chen, H. and Gold, L., (1994), “Selection of High-Affinity RNA Ligands to Reverse Transcriptase”,Biochemistry33, 8746-8756.
Concha, N. O., Janson, C. A., Rowling, P., Pearson, S., Cheever, C. A., Clarke, B. P., Lewis, C., Galleni, M., Frere, J. M., Payne, D. J., Bateson, J. H. and Abdel-Meguid, S. S. (2000), “Crystal of the IMP-1 Metallo-β-Lactamase fromPseudomonas aeruginosaand its Complex with a Mercaptocarboxylate Inhibitor”,Biochemistry15, 4288-4298.
Crompton, B., Jago, M., Crawford, K., Newton, G. G. F. and Abraham, E. P. (1962), “Behaviour of Some Derivatives of 7-Aminocephalosporanic Acid as Substrates, Inhibitors and Inducers of Penicillanases”,Biochem. J.83, 52-63.
Davies, R. B. and Abraham, E. P. (1974), “Metal Cofactor Requirements of β-Lactamase II”,Biochem. J.143, 129-135.
Davies, R. B. Abraham, E. P. and Melling, J. (1974), “Separation, Purification and Properties of β-Lactamase I and β-Lactamase II fromBacillus cereus569/H/9”, Biochem.J.143, 115-127.
Davies, R. B. Abraham, E. P. Melling, J. and Pollock, M. R. (1975),“Comparison of β-lactamase II fromBacillus cereus569/H/9 with a β-Lactamase fromBacillus cereus5/B/6”,Biochem. J.145, 409-411.
Farmulok, M. and Szostak, J. W. (1992), “In Vitro Selection of Specific Ligand Binding Nucleic Acids”, Angew. Chem. Int. Ed. Engl. 31, 979-988.
Felici, A. and Amicosante, G. (1995), “Kinetic Analysis of Extension of Substrate Specificity withXanthomonas maltophilia, Aeromonas hydrophyliaandBacillus cereusMetallo-β-Lactamases”,Antimicrob. Agents Chemother. 39, 192-199.
Felici, A., Amicosante, G., Oratore, A., Strom, R., Ledent, P., Joris, B., Fanuel, L. and Frere, J. -M. (1993), “An Overview of the Kinetic Parameters of Class B β-Lactamases”, Biochem.J.291, 151-155.
Felici, A., Perilli, M., Franceschini, N., Rossolini, G. M., Galleni, M., Frere, J. -M., Oratore, A. and Amicosante, G. (1997), “Sensitivity ofAeromonas hydrophiliaCarbapenemase to Δ3-Cephems”,Antimicrob. Agents Chemother. 41, 866-868.
Hicke, B. J. and Stephens, A. W. (2000), “Escort Aptamers”,J. Clin. Invest.106, 923-928.
Hilliard, N. P., (1995), Structure-Function Relationships in the Metallo-β-Lactamase ofBacillus cereus5/B/6, Ph.D. thesis, Texas Tech University.
Hussain, M., Pastor, F. I. J. and Lampen, J. O. (1987), “Cloning and Sequencing of theblaZGene Encoding β-Lactamase III, a Lipoprotein ofBacillus cereus569/H”, J.Bacteriol.169, 579-586.
Jaeger, J. A., Turner, D. H. and Zuker, M. (1989), “Improved Predictions of Secondary Structures for RNA”,Proc. Natl. Acad. Sci. USA86, 7706-7710.
Jaeger, J. A., Turner, D. H. and Zuker, M. (1990), “Predicting Optimal and Suboptimal Secondary Structure for RNA”,In Methods in Enzymology183, 281-306.
Jellinek, D., Green, L. S., Bell, C. and Janjic, N. (1994), “Inhibition of Receptor Binding by High-Affinity RNA Ligands to Vascular Endothelial Growth Factor”,Biochemistry33, 10450-10456.
Kogut, M., Pollock, M. R. and Tridgell, E. J. (1956), “Purification of Penicillin-Induced Penicillinase ofBacillus cereusNRRL 569”,Biochem. J.62, 391-401.
Kuwabara, S., Adams, E. P. and Abraham, E. P. (1970),“Composition of β-lactamase I and β-Lactamase II fromBacillus cereus569/H”,Biochem. J.118, 475-480.
Kuwabara, S. and Lloyd, P. H. (1971), “Protein and Carbohydrate Moieties of a Preparation of β-Lactamase II”,Biochem. J.124, 215-220.
Ledent, P., Raquet, X., Joris, B., Van Beeumen, J. and Frere, J. -M. (1993), “A Comparative Study of Class D Beta-Lactamases”, Biochem.J.292, 555-562.
Lim, H. M., Pene, J. J. and Shaw, R. W. (1988), “Cloning, Nucleotide Sequence and Expression of theBacillus cereus5/B/6 β-Lactamase II Structural Gene” J.Bacteriol.170, 2873-2878.
Macaya, R. F., Waldron, J. A., Beutel, B. A., Gao, H., Joeston, M. E., Yang, M., Patel, R., Bertelsen, A. H. and Cook, A. G. (1995), “Structural and Functional Characterization of Potent Antithrombotic Oligonucleotides Possessing Both Quadruplex and Duplex Motifs”, Biochemistry 34, 4478-4492.
Matagne, A., Ledent, P., Monnaie, D., Felici, A., Jamin, M., Raquet, X., Galleni, M., Klein, D., Francois, I. and Frere, J. M. (1995), “Kinetic Study of Interaction Between BRL 42715, β-Lactamases and D-Alanyl-D-Alanyl Peptidases”, Antimicrob.Agents Chemother39, 227-231.
Neu, H. C. (1992), “The Crisis in Antibiotic Resistance”,Science257, 1064-1073.
Payne, D. J. (1993),“Metallo-β-lactamases-A New Therapeutic Challenge”,J. Med. Microbiol.39, 993-999.
Rasmussen, B. A., Yang, Y., Jacobs, N. and Bush, K. (1994), “Contribution of Enzymatic Properties, Cell Permeability and Enzyme Expression to Microbial Activities of Beta-lactams in ThreeBacteroids fragilisIsolates that Harbor a Metallo-β-Lactamase gene”,Antimicrob. Agents Chemother.38, 2116-2120.
Robertson, D. L. and Joyce, G. F. (1990), “Selection in vitro of an RNA Enzyme that Specifically Cleaves Single-Stranded DNA”,Nature344, 467-468.
Ruckman, J., Green, L. S., Beeson, J., Waugh, S., Gillette, W. L., Henninger, D. D., Claesson-Welsh, L. and Janjic, N. (1998), 2′-Fluoropyrimidine RNA-Based Aptamers to the 165-Amino Acid Form of Vascular Endothelial Growth Factor (VEGF165),Journal of Biological Chemistry273, 20556-20567.
Sabath, L. D. and Abarham, E. P. (1966), “Zinc as a Cofactor for Cephalosporinase fromBacillus cereus569”,Biochem. J.98, 11c-13c.
Sutton, B. J., Artymiuk, P. J., Cordero-Borboa, A. E., Little, C., Philips, D. C. and Waley, S. G. (1987), “X-Ray Crystallographic Study of β-Lactamase II fromBacillus cereusat 0

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