Cell-based fluorescence resonance energy transfer (FRET)...

Chemistry: molecular biology and microbiology – Measuring or testing process involving enzymes or... – Involving antigen-antibody binding – specific binding protein...

Reexamination Certificate

Rate now

  [ 0.00 ] – not rated yet Voters 0   Comments 0

Details

C435S023000, C435S069100, C435S252300, C435S471000, C530S350000, C536S023700

Reexamination Certificate

active

10261161

ABSTRACT:
The present invention provides a method of determining clostridial toxin activity by (a) contacting with a sample a cell containing a clostridial toxin substrate that includes a donor fluorophore; an acceptor having an absorbance spectrum overlapping the emission spectrum of the donor fluorophore; and a clostridial toxin recognition sequence containing a cleavage site that intervenes between the donor fluorophore and the acceptor, where resonance energy transfer is exhibited between the donor fluorophore and the acceptor under the appropriate conditions; (b) exciting the donor fluorophore; and (c) determining resonance energy transfer of the contacted cell relative to a control cell, where a difference in resonance energy transfer of the contacted cell as compared to the control cell is indicative of clostridial toxin activity.

REFERENCES:
patent: 5804604 (1998-09-01), Frankel et al.
patent: 5962637 (1999-10-01), Shone et al.
patent: 5965699 (1999-10-01), Schmidt et al.
patent: 5981200 (1999-11-01), Tsien et al.
patent: 5989545 (1999-11-01), Foster et al.
patent: 6043042 (2000-03-01), Shone et al.
patent: 6762280 (2004-07-01), Schmidt et al.
patent: 2003/0104975 (2003-06-01), Auwerx et al.
patent: 2003/0149254 (2003-08-01), Anderson et al.
patent: WO 95/33850 (1995-12-01), None
patent: WO 99/29721 (1999-06-01), None
patent: WO 99/55899 (1999-11-01), None
patent: WO 00/34308 (2000-06-01), None
patent: WO 02/25284 (2002-03-01), None
patent: WO 03/020948 (2003-03-01), None
Clegg , Current Opinion in Biotechnology vol. 6, pp. 103-110, 1995.
Majajan et al (Chemistry and Biology; 6:401-409, May 21, 1999).
Clegg et al (Current Opinion in Biotechnology, 6:103-110, 1995).
Siegel et al (STKE, Jun. 27, 2000 of record).
Active Motif, LLC., “The vehicle of the future for protein transfection,” Chariot Protein Transfection Product; http://www.activemotif.com/products/chariot1.html.
Anne et al., “High-Throughput Fluorogenic Assay for Determination of Botulinum Type B Neurotoxin Protease Activity,”Analytical Biochemistry291:253-261 (2001).
Calbiochem, “SNAPtide® Botulinum Toxin A Substrate, Fluorogenic,” www.calbiochem.com, printed on Dec. 17, 2002.
Clegg, “Fluorescence Resonance Energy Transfer,”Current Opinion in Biotechnology6:103-110 (1995).
Cornille et al., “Solid-Phase Synthesis, Conformational Analysis andIn VitroCleavage of Synthetic Human Synaptobrevin II 1-93 by Tetanus Toxin L Chain,”Eur. J. Biochem.222:173-181 (1994).
De Paiva et al., “Functional repair of motor endplates after botulinum neurotoxin type A poisoning: Biphasic switch of synaptic activity between nerve sprouts and their parent terminals,”Proc. Natl. Acad. Sci. USA96:3200-3205 (1999).
Dunican and Doherty, “Designing cell-permeant phosphopeptides to modulate intracellular signaling pathways,”Biopolymers(Peptide Sci.) 60:45-60 (2001).
Ekong et al., “Recombinant SNAP-25 is an Effective Substrate forClostridium botulinumType A Toxin Endopeptidase Activityin vitro,”Microbiology143:3337-3347 (1997).
Florentin et al., “A Highly Sensitive Fluorometric Assay for ‘Enkephalinase,’ a Neutral Metalloendopeptidase That Release Tyrosine-Glycine-Glycine from Enkephalins,”Analytical Biochemistry141:62-69 (1984).
Foran et al., “Differences in the Protease Activities of Tetanus and Botulinum B Toxins Revealed by the Cleavage of Vesicle-Associated Membrane Protein and Various Sized Fragments,”Biochemistry33:15365-15374 (1994).
Ford et al., “Protein transduction: An alternative to genetic intervention?”Gene Therapy8:1-4 (2001).
Fujiwara et al., “Suppression of transmitter release by Tat HPC-1/syntaxin 1A fusion protein,”Biochim. Biophysica Acta.1539:225-232 (2001).
Geoghegan et al., “Fluorescence-based Continuous Assay for the Aspartyl Protease of Human Immunodeficiency Virus-1,”FEBS262:119-122 (1990).
Goudreau et al., “Dns-Gly- (p-NO2) Phe-βAla, a Specific Fluorogenic Substrate for Neutral Endopeptidase 24.11,”Analytical Biochemistry219:87-95 (1994).
Graham et al., “A method to measure the interaction of Rac/Cdc42 with their binding partners using fluorescence resonance energy transfer between mutants of green fluorescent protein,”Analytical Biochem.296:208-217 (2001).
Hallis et al., “Development of Novel Assays for Botulinum Type A and B Neurotoxins Based on Their Endopeptidase Activities,”J. Clin. Microbiol.34:1934-1938 (1996).
Hanson and Stevens, “Cocrystal Structure of Synaptobrevin-II Bound to Botulinum Neurotoxin Type B at 2.0 Å Resolution,”Nature Structural Biology7:687-692 (2000).
Ho, et al., “Synthetic protein transduction domains: Enhanced transduction potentialin Vitroandin Vivo,”Cancer Res.61:474-477 (2001).
Hodel, “Molecules in Focus: SNAP-25,”J. Biochem.&Cell Biol.30:1069-1073 (1998).
Holskin et al., “A Continuous Fluorescence-Based Assay of Human Cytomegalovirus Protease Using a Peptide Substrate,”Analytical Biochemistry226:148-155 (1995).
Huang et al., Ca2+influx and cAMP elevation overcame botulinum toxin A but not tetanus toxin inhibition of insulin exocytosis,Am. J. Physiol. Cell Physiol.281:C740-C750 (2001).
Humeau et al., “How Botulinum and Tetanus Neurotoxins Block Neurotransmitter Release,”Biochimie82:427-446 (2000).
Kakiuchi et al., “A High Throughput Assay of the Hepatitis C Virus Nonstructural Protein 3 Serine Proteinase,”Journal of Virological Methods80:77-84 (1999).
Kam et al., “Probing molecular processes in live cells by quantitative multidimensional microscopy,”Trends in Cell Biology11:329-334 (2001).
Knapp et al., The Crystal Structure of Botulinum Toxin A zinc Protease Domain,37thAnnual Meeting of the Interagency Botulism Research Coordinating CommitteeAsilomar, CA (2000).
Lacy et al., “Crystal Structure of Botulinum Neurotoxin Type A and Implications for Toxicity,”Nature Structural Biology5:898-902 (1998).
Le Bonniec et al., “Characterization of the P2′ and P3′ Specificities of Thrombin Using Fluorescence-Quenched Substrates and Mapping of the Subsites by Mutagenesis,”Biochemistry35:7114-7122 (1996).
Lippincott-Schwartz et al., “Studying protein dynamics in living cells,”Nature2:444:456 (2001).
List Biological Laboratories, “SNAPtide For Fluorometric Measurement of Botulinum Toxin Type A Activity,” www.listlabs.com, printed on Dec. 23, 2002.
Matayoshi et al., “Novel Fluorogenic Substrates for Assaying Retroviral Proteases by Resonance Energy Transfer,”Science247:954-958 (1990).
Matsumoto et al., “A High-Throughput Screening Utilizing Intramolecular Fluorescence Resonance Energy Transfer for the Discovery of the Molecules that Bind HIV-1 TAR RNA Specifically,”Bioorganic&Medicinal Chemistry Letters10:1857-1861 (2000).
Mahajan et al., “Novel Mutant Green Fluorescent Protein Protease Substrates Reveal the Activation of Specific Caspases During Apoptosis,”Chemistry&Biology6:401-409 (1999).
McInnes and Dolly, “Ca2+-dependent noradrenaline release from permeabilised PCl2 cells is blocked by botulinum neurotoxin A or its light chain,”FEBS Letters261:323-326 (1990).
Montecucco and Schiavo, “Structure and Function of Tetanus and Botulinum Neurotoxins,”Quarterly Reviews of Biophysics28:423-472 (1995).
Morris et al., “A new potent HIV-1 reverse transcriptase inhibitor,”J. Biol. Chem.274:24941-24946 (1999).
Morris et al., “A peptide carrier for the delivery of biologically active proteins into mammalian cells,”Nature Biotech.19:1173-1176 (2001).
Morris et al., “A novel potent strategy for gene delivery using a single peptide vector as a carrier,”Nucl. Acids Res.27:3510-3517 (1999).
Nakatsuka et al., “D-aspartate is stored in secretory granules and released through a Ca

LandOfFree

Say what you really think

Search LandOfFree.com for the USA inventors and patents. Rate them and share your experience with other people.

Rating

Cell-based fluorescence resonance energy transfer (FRET)... does not yet have a rating. At this time, there are no reviews or comments for this patent.

If you have personal experience with Cell-based fluorescence resonance energy transfer (FRET)..., we encourage you to share that experience with our LandOfFree.com community. Your opinion is very important and Cell-based fluorescence resonance energy transfer (FRET)... will most certainly appreciate the feedback.

Rate now

     

Profile ID: LFUS-PAI-O-3847255

  Search
All data on this website is collected from public sources. Our data reflects the most accurate information available at the time of publication.