(12) United States Patent (10) Patent No.: US 6,191,108 B1 Rodkey Et Al

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(12) United States Patent (10) Patent No.: US 6,191,108 B1 Rodkey Et Al USOO619 1108B1 (12) United States Patent (10) Patent No.: US 6,191,108 B1 Rodkey et al. (45) Date of Patent: Feb. 20, 2001 (54) RH BLOOD GROUPANTIGEN Moore et al., “Evaluation of monoclonal anti-Rh antibodies COMPOSITIONS AND METHODS OF USE as reagents for blood grouping and for the identification of (76) Inventors: L. Scott Rodkey, 6234 Yarwell, red cell membrane components associated with Rh antigen Houston, TX (US) 77096; Marwan A. activity,” Revue Francaise de Transfusion et Immuno-hé Yared; Kenneth J. Moise, Jr., both of matologie, 31(2):141-144, 1988. 4234 Tennyson, Houston, TX (US) 77005 Paradis et al., “Protective Effect of the Membrane Skeleton (*) Notice: Under 35 U.S.C. 154(b), the term of this on the Immunologic Reactivity of the Human Red Cell patent shall be extended for 0 days. Rho(D) Antigen,” J. Immunol., 137:240–244, 1986. Plapp et al., “Partial Purification of Rh(D) Antigen from Rh (21) Appl. No.: 09/164,789 Positive and Negative Erythrocytes,” Proc. Natl. Acad. Sci. (22) Filed: Oct. 1, 1998 USA, 76:2964-2968, 1979. Related U.S. Application Data Yokoi et al. “Isolation and Purification of Rh(D) Antigen of Human Erythrocyte Membrane and Its Serological Prop 62) DivisiVision off application No.NO. 08/715,173,f3, filedilled On Sep. 17If, 1996, now Pat. No. 5,840,585. erty,’” J. Exp. Med., 141:143–154, 1983. (51) Int. Cl." ..................................................... A61K 38/00 Foreign Search Report dated Dec. 2, 1997. (52) U.S. Cl. ............................................... 514/12; 530/380 (58) Field of Search ................................ 514/12; 530/380 Oellerich M., “Enzyme-Immunoassay: A Review,” J. Clin. Chem. Clin. Biochem, 22:895–904, 1984. (56) References Cited Sambrook, J. et al. “Molecular Cloning A Laboratory U.S. PATENT DOCUMENTS Manual,” Cold Spring Harbor, New York: Cold Spring 5,068,191 11/1991 Clausen et al. ...................... 435/193 5,387,511 2/1995 Davidson et al. .... ... 435/101 Harbor Laboratory Press, Second Edition, pp. 18.16-18.18, 5,840,585 11/1998 Rodkey et al. ...................... 435/161 1989. FOREIGN PATENT DOCUMENTS Suyama et al. “Antibody produced against isolated Rh(D) 242716 2/1987 (DE). polypeptide reacts with other Rh-related antigens,” Chemi WO 90/13032 11/1990 (WO). cal Abstracts, vol. 109, Abstract No. 228.190, Blood, OTHER PUBLICATIONS 72(5):1622–1626, 1988. Agre and Cartron, “Molecular Biology of the Rh Antigens,” Blood, 78:551-563, 1991. * cited by examiner Carter, “Preliminary Report on a Substance Which Inhibits Anti-Rh Serum,' Am. J. Clin. Path., 17:646–649, 1947. Carter, “Rh Hapten: Its Preparation, Assay and Nature,” J. Primary Examiner. Sheela Huff Immunol., 61:79–88, 1949. (74) Attorney, Agent, or Firm Mark B. Wilson Carter, “Preparation and Assay of a Red Cell Fraction of the (57) ABSTRACT Rh Factor,” Am. J. Clin. Path., 21:561-565, 1951. Carter, “The Results in Clinical Use of Rh Hapten,” Am. J. Ob. Gyn., 102:447–450, 1968. Disclosed are novel protein and peptide compositions com Carter et al., “Evaluation of Rh Hapten,” Am. J. Ob. Gyn., prising Soluble and bound forms of immunologically-active 72:655-659, 1956. blood group antigens including mammalian Rh antigens. In Carter and Lewis, “The Effects of Orally Administered Rh preferred embodiments methods for the isolation and puri Hapten. A Study of 17 Cases,” Am. J. Ob. Gyn., fication of Serologically-active human Rh antigens Such as 76:1286-1287, 1958. Iyer et al., “Distribution of IgG Subtypes in Maternal D, c, C, E, and e are disclosed. Also disclosed are methods Anti-D Sera and Their Prognostic Value in Rh Haemolytic for the adsorption of immunologically-active Rh antigens to Disease of the New-Born.” Acta Haematol., 88::78-81, Solid Supports. Diagnostic kits, methods, and devices for the 1992. detection of Rh antibodies in clinical and non-clinical Masouredis, “Quantitative Studies of the Rh(D) Antigenic Samples are also disclosed. Devices, compositions and meth Determinants on Gorilla Erythrocytes,” Transfusion 11(5):270–280, 1971. ods for the isolation, purification and quantitation of anti-Rh Moore et al., “Isolation of Membrane Components Associ antibodies from Solution are also provided. ated with Human Red Cell Antigens Rh(D), (c), (E) and Fya,” Nature, 295:529-531, 1982. 25 Claims, 20 Drawing Sheets U.S. Patent Feb. 20, 2001 Sheet 1 of 20 US 6,191,108 B1 G? S8ld|9||Il 90Sºd/800HeNW§.09 'quulunx0001```] 00||08090#7030 U.S. Patent Feb. 20, 2001 Sheet 3 of 20 US 6,191,108 B1 N001 !È,N. U.S. Patent Feb. 20, 2001 Sheet 4 of 20 US 6,191,108 B1 00|| G8 08 030 Hdjy? U.S. Patent Feb. 20, 2001 Sheet 5 of 20 US 6,191,108 B1 0? 0"| Hd U.S. Patent Feb. 20, 2001 Sheet 8 of 20 US 6,191,108 B1 U.S. Patent Feb. 20, 2001 Sheet 9 of 20 US 6,191,108 B1 000€ U.S. Patent Feb. 20, 2001 Sheet 10 0f 20 US 6,191,108 B1 2 U.S. Patent Feb. 20, 2001 Sheet 11 of 20 US 6,191,108 B1 U.S. Patent Feb. 20, 2001 Sheet 12 of 20 US 6,191,108 B1 O CN ol{\}oleucoupoleo U.S. Patent Feb. 20, 2001 Sheet 13 of 20 US 6,191,108 B1 8?0 ßN• 970#7’0 (10Wu08Z@ // TOHINO0ô?/TVIOI U.S. Patent Feb. 20, 2001 Sheet 14 of 20 US 6,191,108 B1 0’llHd ??00ON U.S. Patent Feb. 20, 2001 Sheet 15 of 20 US 6,191,108 B1 G? Wu08Z©00 Gl70||-|| #7ZHd 0’llHd ??00ON U.S. Patent Feb. 20, 2001 Sheet 16 of 20 US 6,191,108 B1 000!00800||080||000€000‘01000?09000'001 ~0 WIll G07010 U.S. Patent Feb. 20, 2001 Sheet 17 of 20 US 6,191,108 B1 000'00?000'08000‘01000€000!008 00|| 08 Will 907010 U.S. Patent Feb. 20, 2001 Sheet 20 of 20 US 6,191,108 B1 Optional 1 Fittingleur-Lok -Optional Inlet Pump/Walve Inlet Optional Inlet Pump/Valve FIG. 19B US 6,191,108 B1 1 2 RH BLOOD GROUPANTIGEN to develop Strong anti-Rh immune responses. For these COMPOSITIONS AND METHODS OF USE Women, in utero transfusion of the fetus under ultrasound guidance is the only current treatment available for high-risk This is a divisional of application Ser. No. 08/715,173, cases when the woman has previously developed a Strong immune response against the Rh antigen. Because eighty filed Sep. 17, 1996 now U.S. Pat. No. 5,840,585. five percent of the Caucasian population is Rh", a consid 1. BACKGROUND OF THE INVENTION erable number of women and their offspring are potentially at risk for contracting the disease. 1.1 Field of the Invention 1.2.3 Attempts To Isolate Active Solid-Phase Rh Antigen The present invention relates to the fields of protein Have Failed chemistry and hematology. More particularly, the invention Unfortunately, attempts to isolate active Rh antigen have discloses novel compositions comprising Solid-phase, i.e., been disappointing, and no Successful attempts at preparing bound forms of the antigen have been reported. bound, forms of immunologically-active Rh antigen. Also Indeed, a definitive review (Agre and Cartron, 1991) disclosed are diagnostic kits and devices for the detection reported that Rh antigenic activity was lost after membranes and quantitation of Rh antibodies in clinical and non-clinical 15 are Solubilized or transferred onto immunoblot membranes, Samples. In another aspect, the invention relates to devices, and most biochemical methods therefore actually kill the compositions and methods for the isolation, identification, antigenic activity that identifies and defines the Rh antigen. quantitation, and purification of anti-Rh antibodies from Moore et al. (1982) and Plapp et al. (1979) each reported Solution. isolation of Small amounts of Rh antigen after affinity 1.2 Description of the Related Art chromatography of deoxycholate solubilized RBC. Plapp et 1.2.1 Rh Antigens al. (1979) solubilized the cells in deoxycholate, added the The Rh blood group system is one of the most complex mixture to an affinity column made of immobilized anti-Rh polymorphisms in humans. Human red blood cells (RBCs) antibodies and eluted the bound fraction. The resulting may be subdivided into Rh" and Rh groups according to the eluate was active in inhibition of a reaction between Rh" presence or absence of the major Rh blood group antigen, 25 RBC and antibody. Disappointingly, however, extracts from Rhesus D (RhD) (Cartron and Agre, 1993). Several genes both Rh" and Rh cells inhibited the reaction, with the have been implicated as encoding the major Rh antigen authors postulating that Rh antigen was merely “hidden' in epitopes, D, C, c, E, and e, while a host of others are Rh cells. speculated to be involved in the determinants of a host of That conclusion, however, was disproved when modem rare alleles. molecular biology methods conclusively showed that Rh Rh antigens, including Rh. D., are carried on an integral (D) antigen is not present in Rh cells (Agre and Cartron, membrane protein which has a molecular weight of approxi 1991), and that the Rh antigen polypeptides had molecular mately 30 kDa (Moore et al., 1982, Gahmberg, 1982; 1983). Weights of between 28 and 32 kDa (Agre and Cartron, This protein has been implicated in the molecular adhesion 1991). Clearly the 7 kDa polypeptide reported by Plapp and of the submembranous cytoskeleton to the erythrocyte cell 35 coworkers could not be the Rh antigen polypeptide. Moore membrane (Ridgwell et al., 1984), and persons lacking the et al.
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