Drug – bio-affecting and body treating compositions – Antigen – epitope – or other immunospecific immunoeffector – Amino acid sequence disclosed in whole or in part; or...
Reexamination Certificate
2007-02-13
2007-02-13
Chan, Christina (Department: 1644)
Drug, bio-affecting and body treating compositions
Antigen, epitope, or other immunospecific immunoeffector
Amino acid sequence disclosed in whole or in part; or...
C530S326000, C530S350000
Reexamination Certificate
active
09698551
ABSTRACT:
The present invention provides methods to produce toxoid vaccines, such as ricin A chain vaccines, with reduced ability to promote vascular leak syndrome (VLS) and catalytic toxicity associated with various proteinaceous toxins, such as ribosome inactivating proteins. The invention also provides toxoids which have been mutated to lack amino acid sequences which induce VLS and toxic catalytic activity.
REFERENCES:
patent: 4350626 (1982-09-01), Masuho et al.
patent: 4372883 (1983-02-01), Matuhashi et al.
patent: 4490362 (1984-12-01), Shionoya et al.
patent: 5453271 (1995-09-01), Lemley et al.
patent: 5578706 (1996-11-01), Ghetie et al.
patent: 5932217 (1999-08-01), Tuomanen et al.
Stryer et al, in Biochemistry, Third Edition, W. H. Freeman and Company, New York, pp. 31-33, 1988.
Ngo et al, 1994, The Protein Folding Problem and Tertiary Structure Prediction, pp. 492-495.
Skolnick et al., From genes to protein structure and function: novel applications of computational approaches in the genomic era, Jan. 2000, Trends in Biotech. 18(1): 34-39.
Abaza et al, J of Protein Chemistry 11(5): 433-444, 1992.
Kuby et al., 1994 Immunology, second edition, pp. 85-96.
Marsden et al, Eur J Biochem 271(1):153-62, 2004.
Griffiths et al, Vaccine 16(5): 530-5, Mar. 1998.
Baluna and Vitetta, “Anin vivomodel to study immunotoxin-induced vascular leak in human tissue,”J. Immunother., 22(1):41-47, 1999.
Baluna and Vitetta, “Vascular leak syndrome: A side effect of immunotherapy,”Immunopharmacology, 37:117-132, 1997.
Baluna et al., “Evidence for a structural motif in toxins and interleukin-2 that may be responsible for binding to endothelial cells and initiating vascular leak syndrome,”Proc Natl Acad Sci U S A., 96(7):3957-3962, 1999.
Baluna et al., “The effect of a monoclonal antibody coupled to ricin A chain-derived peptides on endothelial cells in vitro: insights into toxin-mediated vascular damage,”Exp Cell Res. 258(2):417-424, 2000.
Baluna et al., “Fibronectin inhibits the cytotoxic effect of ricin A chain on endothelial cells,”Int. J. Immunopharm., 18:355-361, 1996.
Chaddock and Roberts, “Mutagenesis and kinetic analysis of the active site Glu177 of ricin A-chain,”Protein Eng., 6(4):425-431, 1993.
Clements et al., “Identification of a key integrin-binding sequence in VCAM-1 homologous to the LDV active site in fibronectin,”J. Cell Sci., 107:2127-2135, 1994.
Engert et al., “The emerging role of ricin A-chain immunotoxins in leukemia and lymphoma,”In: Clinical Applications of Immunotoxins, Frankel (ed.), 2:13-33, 1997.
Frankel et al., “Role of arginine 180 and glutamic acid 177 of ricin toxin A chain in enzymatic inactivation of ribosomes,”Mol. Cell. Biol., 10(12):6257-6263, 1990.
Ghetie et al., “Evaluation of ricin A chain-containing immunotoxins directed against CD19 and CD22 antigens on normal and malignant human B-cells as potential reagents for in vivo therapy,”Cancer Res. 48:2610-2617, 1988.
Ghetie et al., “The GLP large scale preparation of immunotoxins deglycosylated ricin A chain and a hindered disulfide bond,”J. Immunol Methods, 142(2):223-230, 1991.
Hewetson et al. “Protection of mice from inhaled ricin by vaccination with ricin or by passive treatment with heterologous antibody,”Vaccine, 11(7):743-746, 1993. Abstract attached (Reports and Abstracts 138-139).
Hewetson et al., “A Formalinized Toxoid for Protection of Mice from Inhaled Ricin”, Vaccine Research, 4(4): 179-187, 1995.
Makarem and Humphries, “LDV: a novel cell adhesion motif recognized by the integrin α4β1,”Biochemical Society Transactions, 19:380S-381S, 1991.
Mlsna et al., “Structure of recombinant ricin A chain at 2.3 Å,”Protein Sci., 2:429-435, 1993.
Munishkin and Wool, “Systematic deletion analysis or ricin A-chain function,”J. Biol. Chem., 270(51):30581-30587, 1995.
Nowlin et al., “A novel cyclic pentapeptide inhibits α4β1 and α5β1 integrin-mediated cell adhesion,”J. Biol. Chem., 268(27):20352-20359, 1993.
Sausville and Vitetta, “Clinical studies with deglycosylated ricin A-chain immunotoxins,”In: Monoclonal Antibody-Based Therapy of Cancer, Grossbard (ed.), 4:81-89, 1997.
Soler-Rodriguez et al., “Ricin A-chain and ricin A-chain immunotoxins rapidly damage human endothelial cells: implications for vascular leak syndrome,”Exp. Cell Res., 206:227-234, 1993.
Tagge et al., “Cytotoxicity of KDEL-terminated ricin toxins correlates with distribution of the KDEL receptor in the golgi,”J. of Histochem. And Cytochem., 44(2):159-165, 1996.
Yan et al., “Persistence of immunity to ricin toxin evoked by vaccine incorporated into polylactide-CO-glycolide (PLG) microparticles,”Proceed. Intern. Symp. Control. Rel. Bioact. Mater., 21(#127):52-53, 1994.
“Vaccines I: Mucosal immunity,” Abstract from the93rdASM General Meeting, Session 279:152.
Baluna Roxana G.
Ghetie Victor F.
Smallshaw Joan E.
Vitetta Ellen S.
Board of Regents , The University of Texas System
Chan Christina
Fulbright & Jaworski
Huynh Phuong
LandOfFree
Ricin A chain mutants lacking enzymatic activity as vaccines... does not yet have a rating. At this time, there are no reviews or comments for this patent.
If you have personal experience with Ricin A chain mutants lacking enzymatic activity as vaccines..., we encourage you to share that experience with our LandOfFree.com community. Your opinion is very important and Ricin A chain mutants lacking enzymatic activity as vaccines... will most certainly appreciate the feedback.
Profile ID: LFUS-PAI-O-3818837