Method of reducing complement - mediated disruption of cells

Details Method of reducing complement - mediated disruption of cells Method of reducing complement - mediated disruption of cells

2007-09-04

2007-09-04

Saidha, Tekchand (Department: 1652)

Chemistry: molecular biology and microbiology

Measuring or testing process involving enzymes or...

C435S069100, C435S212000, C536S023200

Reexamination Certificate

active

11294087

ABSTRACT:
Disclosed is a pO157 plasmid-specified polypeptide found inE. coliEDL933 and otherE. colithat binds to and cleaves C1-esterase inhibitor, and antibodies specific for the polypeptide. Also disclosed are methods employing the polypeptide for diagnosing enterohemorrhagicE. coliinfection, identifying potential inhibitors of its activity, and reducing viscosity of material containing glycosylated polypeptides.

REFERENCES:
patent: 6872559 (2005-03-01), Welch et al.
patent: WO 02/34918 (2002-05-01), None
Bauer, M.E. et al., “Characterization of an RTX toxin from enterohemorrhagicEscherichia coliO157:H7,” Infect. Immun. (1996) 64:167-175.
Bergamaschini, L. et al., “Endothelial targeting with C1-inhibitor reduces complement activation in vitro and during ex vivo reperfusion of pig liver,” Clin. Exp. Immunol. (2001) 126:412-420.
Berggard, K. et al., “Binding of human C4BP to the hypervariable region of M protein: a molecular mechanism of phagocytosis resistance in streptococcus pyogenes,” Mol. Microbiol. (2001) 42:539-551.
Boucher, R.C., “An overview of the pathogenesis of cystic fibrosis lung disease,” Adv. Drug Delivery Reviews (2002) 54:1359-1371.
Brunder, W., “E. coli3.3kb DNA fragment from plasmid p0157,” Database EMBL 'Online! Database Entry EC33P0157, Y11831.1 (1999) 1-2.
Brunder, W., “Hypothetical 34.0 kDa protein (Fragment),” Database SWALL 'Online! Entry No. Q9ZAL1 (1999) 1.
Burak, K.W. et al., “C1 inhibitor deficiency and angioedema of the small intesting masquerading as Crohn's disease,” Can. J. Gastroenterol (2000) 14(4):349-351.
Burland, V. et al., “The complete DNA sequence and analysis of the large virulence plasmic ofEscherichia coli0157:H7 plasmid p0157, complete sequence,” Database EMBL 'Online! Database Entry AF074613 (1998) 1-54.
Burland, V. et al., “The complete DNA sequence and analysis of the large virulence plasmic ofEscherichia coli0157:H7,” Nucleic Acids Res. (1998) 26(18):4196-4204.
Cai, S. et al., “Complement regulatory protein C1 inhibitor binds to selectins and interferes with endothelial-leukocyte adhesion,” J. Immunol. (2003) 171:4786-4791.
Caldwell, E.E. et al., “Heparin binding and augmentation of C1 inhibitor activity,” Arch. Biochem. Biophys. (1999) 361:215-222.
Caliezi, C. et al., “C1-esterase inhibitor: an anti-inflammatory agent and its potential use in the treatment of diseases other than hereditary angioedema,” Pharmacol. Rev. (2000) 52:91-112.
Caprioli, A. et al., “Pheno-genotyping of verotoxin 2 (VT2)-producingEscherichia colicausing haemorrhagic colitis and haemolytic uraemic syndrome by direct analysis of patients' stools,” J. Med. Microbiol. (1995) 43:348-353.
Catanese, J. et al., “Enzymatic intactivation of human plasma C1-inhibitor and alpha1 antichymotrypsin by pseudomonas aeruginosa proteinase and elastase,” Biochim. Biophys. Acta (1984) 789:37-43.
Chan, J.Y. et al., “The inhibition of activated factor XII (Hageman factor) by antithrombin III: the effect of other plasma proteinase inhibitors,” Biochim Biophys. Res. Commun. (1977) 74:150-158.
Cooper, N.R., “Complement evasion strategies of microorganisms,” Immunol. Today (1991) 12:327-331.
Coutinho, M. et al., “Functional analysis of the serpin domain of C1 inhibitor,” J. Immunol. (1994) 153:3648-3654.
Datsenko et al., “One-step inactivation of chromosomal genes inEscherichia coliK-12 using PCR products,” PNAS (2000) 97:6640-6645.
De Agostini, A. et al., “Human plasma kallikrein and C1 inhibitor form a complex possessing an epitope that is not detectable on the parent molecules: demonstration using a monoclonal antibody,” PNAS (1985) 82:5190-5193.
De Lorenzo, V.D. et al., “Analysis and construction of stable phenotypes in gram-negative bacteria with Tn5- and Tn10-derived minitransposons,” Bacterial Pathogenesis, Clark & Bavoil, eds., Academic Press, San Diego (1994) 235:386-405.
Dean-Nystrom, E. et al., “Vaccination of pregnant dams with intimin O157 protects suckling piglets fromEscherichia coliO157:H7 infection,” Inf. Immun. (2002) 70(5):2414-2418.
Deloney et al., “Role for phosphoglucomutase in vibrio fischeri-euprymna scolopes symbiosis,” J. Bacteriol. (2002) 184(18):5121-5129.
Donnenberg, M.S. et al., “Methods for studying adhesion of diarrheagenicEscherichia coli,” Meth. Enzym. (1992) 253:324-327.
Elson, C. et al., “Generalized systemic and mucosal immunity in mice after mucosal stimulation with cholera toxin,” J. Immun. (1984) 132(6):2736-2741.
Elson, C. et al., “Cholera toxin feeding did not induce oral tolerance in mice and abrogated oral tolerance to an unrelated protein antigen,” J. Immunol. (1984) 133(6):2892-2897.
Eriksson, K. et al., “Cholera toxin and its B subunit promote dendritic cell vaccination with different influences on Th1 and Th2 development,” Inf. Immun. (2003) 71(4):1740-1747.
Frank, M.M. et al., “Complement,” Fundamental Immunology, W.E. Paul, ed., Raven Press, NY (1989).
Frank, M.M., “The mechanism by which microorganisms avoid complement attack,” Curr. Opin. Immunol. (1992) 4:14-19.
Frankel, G. et al., “Enteropathogenic and enterohaemorrhagicEscherichia coli: more subversive elements,” Mol. Microbiol. (1998) 30:911-921.
Gadek, J.E. et al., “Replacement therapy in hereditary angioedema. Successful treatment of acute episodes of angioedema with partly purified C1 inhibitor,” N. Engl. J. Med. (1980) 302:542-546.
Gigli, I. et al., “Modulation of the classical pathway C3 convertase by plasma proteins C4 binding protein and C3b inactivator,” PNAS (1979) 76:6596-6600.
Grys, T.E. et al., “The StcE protease contributes to intimate adherence of enterohemorrhagicEscherichia coliO157:H7 to host cells,” Inf. Immun. (2005) 73(3):1295-1303.
Harlow, E. et al., Antibodies: A Laboratory Manual, Cold Spring Harbor Laboratory Press, Cold Spring Harbor (1988).
Hauert, J. et al., “C1 inhibitor cross-linking by tissue transglutaminase,” J. Biol. Chem. (2000) 275:14558-14562.
Hellwage, J. et al., “The complement regulator factor H binds to the surface protein OspE of borrelia burgdorferi,” J. Biol. Chem. (2001) 276:8427-8435.
Hong, Y.Q. et al, “Effect of pseudomonas aeruginosa elastase and alkaline protease on serum complement and isolated components C1q and C3,” Clin. Immun. Immunopath. (1992) 62:133-138.
Huntington, J.A. et al., “Structure of a serpin-protease complex shows inhibition by deformation,” Nature (2000) 407:923-926.
Jiang, H. et al., “Complement 1 inhibitor is a regulator of the alternative complement pathway,” J. Exp. Med. (2001) 194:1609-1616.
Jiang, W. et al., “Families of metalloendopeptidases and their relationships,” FEBS Letters (1992) 312:110-114.
Judge, N. et al., “Plant cell-based intimin vaccine given orally to mice primed with intimin reduces time ofEscherichia coliO157:H7 shedding in feces,” Inf. Immun. (2004) 72(1):168-175.
Jung, C.-M. et al., “Identification of metal ligands in the clostridium histolyticum ColH collagenase,” J. Bact. (1999) 181:2816-2822.
Karmali, M.A. et al., “Sporadic cases of haemolytic-uraemic syndrome associated with faecal cytotoxin and cytotoxin-producingEscherichia coliin stools,” Lancet (1983) 1:619-620.
Knutton, S. et al., “Actin accumulation at sites of bacterial adhesion to tissue culture cells: basis of a new diagnostic test for enteropathogenic and enterohemorrhagicEscherichia coli,” Inf. Immun. (1989) 1290-1298.
Kuno, K. et al., “ADAMTS-1 is an active metalloproteinase associated with the extracellular matrix,” J. Biol. Chem. (1999) 274:18821-18826.
Lathem, W.W. et al, “StcE, a metalloprotease secreted byEscherichia co

Affiliated with

Also associated with

Rating

Method of reducing complement - mediated disruption of cells does not yet have a rating. At this time, there are no reviews or comments for this patent.

If you have personal experience with Method of reducing complement - mediated disruption of cells, we encourage you to share that experience with our LandOfFree.com community. Your opinion is very important and Method of reducing complement - mediated disruption of cells will most certainly appreciate the feedback.

Rate now

Comments { 0 }

Profile ID: LFUS-PAI-O-3759887