Device for detecting bacterial contamination and method of use

Chemistry: molecular biology and microbiology – Measuring or testing process involving enzymes or... – Involving viable micro-organism

Reexamination Certificate

Rate now

  [ 0.00 ] – not rated yet Voters 0   Comments 0

Details

C435S023000

Reexamination Certificate

active

11036761

ABSTRACT:
A device and method for detecting the presence or absence of a prokaryotic microorganism are provided, comprising the steps of identifying a protein, such as a microbial-specific protease that characterizes the presence of a specific prokaryotic microbe and thereby provides a marker for that microbe; detecting the protease that is a marker for the presence of a specific prokaryotic microbe by cleaving a substrate when the protease is present; and signaling the presence of that protease when cleavage has occurred. More specifically, the method comprises identifying at least one outer membrane protein or a secreted protein that is unique to a particular microbial pathogen such as for exampleListeria monocytogenesand that is substrate specific.

REFERENCES:
patent: 4897444 (1990-01-01), Brynes et al.
patent: 5330889 (1994-07-01), Monget
patent: 5512445 (1996-04-01), Yang et al.
patent: 5518894 (1996-05-01), Berg
patent: 5523205 (1996-06-01), Cossart et al.
patent: 5662905 (1997-09-01), Siadak et al.
patent: 5716799 (1998-02-01), Rambach
patent: 5783410 (1998-07-01), He et al.
patent: 5824468 (1998-10-01), Scherer et al.
patent: 5932415 (1999-08-01), Schubert et al.
patent: 5976827 (1999-11-01), Jeffrey et al.
patent: 5994059 (1999-11-01), Hogan et al.
patent: 6048688 (2000-04-01), Korth et al.
patent: 6051391 (2000-04-01), Schabert et al.
patent: 6235285 (2001-05-01), Burnham
patent: 6284517 (2001-09-01), Restaino
patent: 6294177 (2001-09-01), Fattom
patent: 6342581 (2002-01-01), Rosen et al.
patent: 0 428 000 (1991-05-01), None
patent: 0 430 608 (1991-06-01), None
patent: 0 864 864 (1998-09-01), None
patent: 0 122 028 (2002-07-01), None
patent: WO 91/16336 (1991-10-01), None
patent: WO 97/28261 (1997-08-01), None
patent: WO 9728261 (1997-08-01), None
patent: WO 00/50872 (2000-08-01), None
patent: WO 01/59149 (2001-08-01), None
patent: WO 02/10433 (2002-02-01), None
Domann et al., Infect. Immun., 59:65-72, 1991.
Altekruse S.F., et al., “Cheese-Associated Outbreaks of Human Illness in the United States, 1973 to 1992: Sanitary Manufacturing Practices Protect Consumers,”J. Food Prot., 61(10):1405-1407(1998).
Dalton C.B., et al., “An Outbreak of Gastroenteritis and Fever Due toListeria monocytogenesisin Milk,”N. Engl. J. Med., 336(2): 100-105 (1997).
Domann E., et al., “Molecular Cloning, Sequencing, and Identification of a Metalloprotease Gene fromListeria monocytogenesThat Is Species Specific and Physically Linked to Listeriolysin Gene,”Infection and Immunity., 59(1):65-72 (1991).
Engel, L.S., et al., “Pseudomonas aeruginosaProtease IV Produces Corneal Damage and Contributes to Bacterial Virulence,”Invest. Ophthalmol. Vis. Sci., 39(3):662-665 ( 1998).
Ericsson, H., et al., “An Outbreak of Listeriosis Suspected To Have Been Caused By Rainbow Trout,”J. Clin. Microbiol., 35(11):2904-2907(1997).
From the Centers for Disease Control and Prevention. Update: Multistate Outbreak of Listeriosis—United States, 1998-1999.JAMA,281(4):317-318(1999).
Gottesman S., “Proteases and Their Targets inEscherichia coli,” Annu. Rev. Genet. 30: 465-506(1996).
Häse C.C. and Finkelstein, R., “Bacterial Extracellular Zinc-Containing Metalloproteases,”Microbiological Reviews.,57(4):823-837(1993).
Liu Y., et al., “Use of a Fluorescence Plate Reader for Measuring Kinetic Parameters with Inner Filter Effect Correction,”Anal. Biochem., 267(2):331-335(1999).
Maeda H. “Role of Microbial Proteases in Pathogenesis,”Microbiol. Immunol., 40(10):685-699(1996).
Marquis H., et al. “Proteolytic Pathways of Activation and Degradation of a Bacterial Phospholipase C during Intracellular Infection byListeria monocytogenes,” J. Cell Biol., 137(6):1381-1392(1997).
Nair S. et al. “ClpE, a Novel Member of the HSP100 Family, is Involved in Cell Division and Virulence ofListeria monocytogenes,” Mol. Microbiol., 31(1):185-196 (1999).
Pallen M.J. and Wren, B., “The HtrA family of serine proteases,”Mol. Microbiol. 26(2) 209-221 (1997).
Poyart C., et al., “The Zinc Metalloprotease ofListeria monocytogenesIs Required for Muturation of Phosphatidylcholine Phospholipase C: Direct Evidence Obtained by Gene Complementation.”Infect.&Immun., 61(4) 1576-1580 (1993).
Rodriguez M., et al., “Evaluation of Proteolytic Activity of Micro-organisms Isolated From Dry Cured Ham,”J. Appl. Microbiol., 85(5): 905-912(1998).
Schwartz M.A., and Luna, E., “Binding and Assembly of Actin Filaments by Plasma Membranes fromDictyostelium Discoideum.” J. Cell Biol., 102(6):2067-2075(1986).
Smith G.A., et al., “The Tandem Repeat Domain in theListeria monocytogenesActA Protein Controls the Rate of Actin-based Motility, the Percentage of Moving Bacteria, and the Localization of Vasodilator-Stimulated Phosphoprotein and Profilin.”J. Cell Biol., 135(3): 647-660 (1996).
Trivett T.L.and Meyer, E., “Citrate Cycle and Related Metabolism ofListeria monocytogenes,” J. Bacteriol. 107(3):770-779 (1971).
Vollmer P., et al. “Novel Pathogenic Mechanism of Microbial Metalloproteinases: Liberation of Membrane-Anchored Molecules in Biologically Active Form Exemplified by Studies with the Human Interleukin-receptor.”Infection and Immunity.,64(9):3646-3651(1996).
Wang, Y-L, et al., “Analysis of Cytoskeletal Structures by Microinjection of Fluroescent Probes,”Eds. S. Grinstein and K. Foskett, in Noninvasive Techniques in Cell Biology, pp. 177-212 (1990).
Thompson, J.S., et al., “Rapid Biochemical Test To Identity Verocytotoxin-Positive Strains ofEscherichia coliSerotype O157,” J. Clin. Microbiol. 28(10): 2165-2168 (1990).
Keelan, S.L. and Flower, R., v“Multitest System for Biochemical Identification ofSalmonella, Escherichia coli, and OtherEnterobacteriaceaeIsolated from Foods: Collaborative Study,”J. Assoc. Off. Anal. Chem. 71(5): 968-972 (1988).
Braun, V. and Schmitz, G., “Excretion of a Protease by Serratia Marcescens,”Arch. Microbiol., 124:55-61, (1980).
Decedue, C.J., et al., “Purification and Characterization of the Extracellular Proteinase of Serratia Marcescens,”Biochim. Biophys. Acta, 569:293-301, (1979).
Kennedy, E.P. and Scarborough, G.A., “Mechanism of Hydrolysis of O-Nitrophenyl-β-Galactoside inStaphylococcus aureusand Its Significance for Theories of Sugar Transport,”Proc. Natl. Acad. Sci. USA, 58:225-228 (1967).
Molla, A., et al., “Characterization of 73kDa Thiol Protease from Serratia Marcescens and Its Effect on Plasma Proteins,”J. Biochem., 104:616-621, (1988).
Molla, A., et al., “Degradation of Protease Inhibitors, Immunoglobulins, and Other Serum Proteins by Serratia Protease and Its Toxicity to Fibroblasts in Culture,”Infection and Immununity, 53:522-529, (1986).
Oshida, T., et al., “AStaphylococcus aureusAutolysin That Has an N-Acetylmuramoyl-L-Alanine Amidase Domain and an Enod-β-N-Acetylglucosaminidase Domain: Cloning, Sequence, Analysis, and Characterization,”Proc. Natl. Acad. Sci. USA, 92:285-289, (1995).
Rice, K., et al., “Desciption ofStaphylococcusSerine Protease (ssp) Operon inStaphylococcus aureusand Nonpolar Inactivation ofsspA-Encoded Serine Protease,”Infection and Immunity, 69:159-169, (2001).
Rosenstein, R. and Götz, F., “StaphylococcalLipases: Biochemical and Molecular Characterization,”Biochimie82:1005-1014, (2000).
Salamone, P.R. and Wodzinski, R.J., “Production, Purification and Characterization of a 50-kDa Extracellular Metalloprotease From Serratia Marcescens,”Appl. Microbiol. Biotechnol., 48:317-324, (1997).
Shikata, S., et al., “Detection of Large COOH-Terminal Domains Processed From the Precursor of Serratia Marcescens Serine Protease in the Outer Membrane ofEscherichia Coli,” J. Biochem., 111:627-632, (1992).
Sugai, M., et al., “Identification of Endo-β-N-Acetylglucosami

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

Device for detecting bacterial contamination and method of use does not yet have a rating. At this time, there are no reviews or comments for this patent.

If you have personal experience with Device for detecting bacterial contamination and method of use, we encourage you to share that experience with our LandOfFree.com community. Your opinion is very important and Device for detecting bacterial contamination and method of use will most certainly appreciate the feedback.

Rate now

     

Profile ID: LFUS-PAI-O-3781624

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