Chemistry: molecular biology and microbiology – Enzyme – proenzyme; compositions thereof; process for... – Hydrolase
Reexamination Certificate
2011-08-09
2011-08-09
Swope, Sheridan (Department: 1652)
Chemistry: molecular biology and microbiology
Enzyme , proenzyme; compositions thereof; process for...
Hydrolase
Reexamination Certificate
active
07993896
ABSTRACT:
This invention relates to enzymatic removal of type A and B antigens from blood group A, B, and AB reactive cells in blood products, and thereby converting these to non-A and non-B reactive cells. The invention further relates to using unique α-N-acetylgalactosaminidases and α-galactosidases with superior kinetic properties for removing the immunodominant monosaccharides of the blood group A and B antigens and improved performance in enzymatic conversion of red blood cells. The preferred unique α-N-acetylgalactosaminidases and α-galactosidases exhibit the following characteristics: (i) exclusive, preferred or no less than 10% substrate specificity for the type A and B branched polysaccharide structures relative to measurable activity with simple mono- and disaccharide structures and aglycon derivatives hereof; (ii) optimal performance at neutral pH with blood group oligosaccharides and in enzymatic conversion of cells; and (iii) a favorable kinetic constant Kmwith mono- and oligosaccharide substrates. The conversion methods of the invention use significantly lower amounts of recombinant glycosidase enzymes than previous and result in complete sero-conversion of all blood group A and B red cells.
REFERENCES:
patent: 4209509 (1980-06-01), Inouye et al.
patent: 4330619 (1982-05-01), Goldstein
patent: 4427777 (1984-01-01), Goldstein
patent: 4609627 (1986-09-01), Goldstein
patent: 5082778 (1992-01-01), Overbeeke et al.
patent: 5478738 (1995-12-01), Goldstein et al.
patent: 5491075 (1996-02-01), Desnick et al.
patent: 5606042 (1997-02-01), Smith et al.
patent: 5633130 (1997-05-01), Smith et al.
patent: 5731426 (1998-03-01), Smith et al.
patent: 5925541 (1999-07-01), Goldstein et al.
patent: 6184017 (2001-02-01), Smith et al.
patent: 6228631 (2001-05-01), Zhu et al.
patent: 6329191 (2001-12-01), Ivy et al.
patent: 6423525 (2002-07-01), Landry
patent: 6458573 (2002-10-01), Landry
patent: 7767415 (2010-08-01), Clausen et al.
patent: 2001/0006772 (2001-07-01), Goldstein et al.
patent: WO 94/09123 (1994-04-01), None
patent: WO 94/12628 (1994-06-01), None
patent: WO 94/23869 (1994-10-01), None
patent: WO 96/23869 (1996-08-01), None
patent: WO 96/40714 (1996-12-01), None
patent: WO 99/23210 (1999-05-01), None
Clausen, et al. (1985). Proc Natl Acad Sci USA 82: 1199-1203.
Clausen, et al. (1986). J Biol Chem 261(3): 1380-1387.
Clausen, et al. (1986). Biochem 25(22): 7075-7085.
Clausen, et al. (1987). J Biol Chem 262(29): 14228-14234.
Clausen and Hakmomori (1989). Vox Sang 56(1): 1-20.
Courtois and Petek (1996). Methods Enzymol 3: 565-571.
Davis, et al. (1996). Biochem & Molecular Biolo Int'l 39(3): 471-485.
Dean and Sweeley (1979). J Biol Chem 254(20): 10001-10005.
Falk, et al. (1991). Arch Biochem Biophys 290(2): 312-319.
Goldstein (1984). Prog Clin Biol Res 165: 139-157.
Hata, et al. (1992). Biochem Int 28 (1): 77-86.
Henrissat, et al. (1998). Biochem Soc Trans 26(2): 153-156.
Hoskins, et al. (1997). J Bio Chem 272(12): 7932-7939.
Hoskins, et al. (2001). Transfusion 41: 908-916.
Hsieh, et al. (2000). IUBMB Life 50(2): 91-97.
Izumi, et al. (1992). Biochem Biophys Acta 1116(1): 72-74.
Kruskall, et al. (2000). Transfusion 40: 1290-1298.
Levy and Animoff (1980). J Biol Chem 255(24): 11737-11742.
Rye and Withers (2000). Curr Opin Chem Biol 4: 573-580.
Tsuji, et al. (1989). Biochem Biophys Res Comm 163(3): 1498-1504.
Vosnidou (1998). Biochem Mol Biol Int 46(1): 175-186.
Wang, et al. (1990). J Biol Chem 265(35) : 21859-21866.
Zhu, et al. (1995). Arch Biochem Biophys 324(1) : 65-70.
Zhu, et al. (1996). Arch Biochem Biophys 327(2) : 324-329.
Zhu, et al. (1995). Protein Expression and Purification 8: 456-462.
Bakunina, et al. (1998). Biochem (Moscow) 63: 1209-1215.
Harpaz, et al. (1977). Eur J Biochem 77: 419-429.
Hobbs, et al. (1995). Biomed & Pharmacother 5 : 144-250.
International Search Report for PCT/US02/30403, Mailed Aug. 8, 2003.
Larson, et al.; Degradation of human intestinal glycoshpingolipids by extracellular glycosidases from mucin-degrading bacteria of the human fecal flora; Journal of Biological Chemistry; vol. 263, No. 22, 1998, pp. 10790-10798.
Hoskins, et al.; Blood group A immunodeterminants on human red cells differ in biologic activity and sensitivity to alpha-N-acetylgalactosaminidase; Transfusion (Bethesda), vol. 35, No. 10, 1995, pp. 813-821.
Phillips, et al.; Characterization of Gallus Domesticus alpha-N-acetyl-galactosaminidase blood group A2 activity; Artificial Cells, Blood Substitutes, and Immobilization Biotechnology; Marcel Dekker Inc., US, vol. 23, No. 1, 1995, pp. 63-79.
O'Neill, R.A.; Enzymatic release of oligosaccharides from glycoproteins for chromatographic and electrophoretic analysis; Journal of Chromatography A, Elsevier, Amsterdam. NL, vol. 720, No. 1, Jan. 12, 1996, pp. 201-215.
Ito, et al.; Histochemical localization and analysis of blood group-related antigens in human pancreas using immunostaining with monoclonal antibodies and exoglycosidase digestion; Journal of Histochemistry and Cytochemistry, vol. 38, No. 9, 1990, pp. 1331-1340.
Sarode, et al.; Role of A and B blood group antigens in the expression of adhesive activity of von Willebrand factor; British Journal of Haematology, vol. 109, No. 4, Jun. 2000, pp. 857-864.
Goldstein, et al.; Further evidence for the presence of a antigen on group B erythrocytes through the use of specific exoglycosidases; Vox Sanguinis, vol. 57, No. 2, 1989, pp. 142-146.
Kruskall, et al.; Transfusion to blood group A and O patients of group B RBCs that have been enzymatically converted to group O; Transfusion (Bethesda), vol. 40, No. 11, Nov. 2000, pp. 1290-1298.
Schmidt et al.; “The Determination of Antibody to Group aStreptococcal polysaccharidein Human Sera by Hemagglutination;” J. Exp. Med.; 1965; vol. 121; pp. 793-806.
Oishi & Aida, “Some Kinetic Properties of α-D-Galactosidase fromStreptomyces9917S2”,Agr. Biol. Chem., 1976, vol. 40, pp. 57-65.
USPTO in house search of the ATCC bacterial database for “PTA-4077”; Mar. 3, 2008.
Oishi, et al., “Conversion of Human Blood Group B and AB Red Blood Cells to Group O and A Cells byStreptomycesEnzyme”, Agr. Biol. Chem., vol. 40(1), pp. 67-71.
Kondoh, et al., “Cloning and Expression of the Gene EncodingStreptomyces coelicolorA3(2) Alpha-Galactosidase Belonging to Family 36”, Biotechnol Lett., May 2005, vol. 25(9), pp. 641-647.
Leder, et al., “Alpha-Galactosidase of Bifidobacterium Adolescentis DSM 20083”, Curr Microbiol., Feb. 1999, vol. 38(2), pp. 101-106.
Ito et al., “Estimation and comparison of the contents of blood group B antigens in selected human tissues by microphotometric quantification of Griffonia simplicifolia agglutinin I-B4 staining”, Histol Histopathol. 1997, vol. 12, pp. 415-424.
Chien et al., “The conversion of group B red blood cells into group O by an alpha-D-galactosidase from taro (Colocasia esculenta)”, Carbohydr Res., 1991, vol. 18, pp. 191-200.
Davis et al., “Cloning, sequence, and expression of a blood group B active recombinant alpha-D-galactosidase from pinto bean (Phaseolus vulgaris)”, Biochem Mol Biol Int. 1997, vol. 42, pp. 453-467.
Guyton and Hall, “Normal hydrogen ion concentran and pH of body fluids”, In: Textbook of Medical Physiology W.B. Saunders Col, Philadelphia, PA, 1996, p. 386.
Willard et al., J. Exp. Med., 1965, 121: 793-806.
Extended European Search Report—(EP10182388.8), Date of Completion of the Search Feb. 8, 2011.
Lopez-Fernandez, et al., “Application of the Affinity Binding of Xylanases to Oat-spelt Xylan in the Purification of Endoxylanase CM-2 fromStreptomyces ChattanoogensisCECT 3336”,Applied Microbiology and Biotechnology, Springer Verlag, Berlin, DE, 1998, vol. 50, pp. 284-287.
Boeck, et al., “Production of Anticapsin byStreptomyces griseoplanus”, Applied Microbiology, 1971, vol. 21, pp. 1075-1079.
Williams, et al., “Numerical Classification ofStreptomycesand Related Genera”,Journal of General Micr
Clausen Henrik
de la Vega Humberto
Hill Cheryl
Liu Qiyong Peter
Ewing James F.
Foley & Lardner LLP
Morency Michel
Swope Sheridan
Velico Medical, Inc.
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