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(12) United States Patent (10) Patent No.: US 8,183,002 B2 Adamczyk Et Al

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(12) United States Patent (10) Patent No.: US 8,183,002 B2 Adamczyk Et Al USOO81830O2B2 (12) United States Patent (10) Patent No.: US 8,183,002 B2 Adamczyk et al. (45) Date of Patent: May 22, 2012 (54) AUTOANTIBODY ENHANCED Adamczyk et al., “Modulation of the Chemiluminescent Signal From MMUNOASSAYS AND KITS N10-(3-Sulfopropyl)-N-Sulfonylacridinium-9-carboxamides.” Tet (75) Inventors: Maciej Adamczyk, Gurnee, IL (US); rahedron, 1999, pp. 10899-10914, vol. 55. Jeffrey R. Brashear, Mundelein, IL Adamczyk et al., “Neopentyl 3-Triflyloxypropanesulfaonate Areac (US); Phillip G. Mattingly, Third Lake, tive Sulfopropylation Reagent for the Preparation of Chemiluminescent Labels.” J Org Chem, 1998, pp. 5636-5639, vol. IL (US) 63. (73) Assignee: Abbott Laboratories, Abbott Park, IL Adamczyk et al., “Regiodependent Luminescence Quenching of (US) Biotinylated N-Sulfonyl-acridinium-9-carboxamides by Avidin.” Organic Letters, 2003, pp. 3779-3782, vol. 5 (21). (*) Notice: Subject to any disclaimer, the term of this Adamczyk et al., “Synthesis of a Chemiluminescent Acridinium patent is extended or adjusted under 35 Hydroxylamine (AHA) for the Direct Detection of Abasic Sites in U.S.C. 154(b) by 351 days. DNA.” Organic Letters, 1999, pp. 779-781, vol. 1 (5). Akerstromet al., “Protein G: A Powerful Tool for Binding and Detec (21) Appl. No.: 12/630,697 tion of Monoclonal and Polyclonal Antibodies.” Immunology, 1985, vol. 135 (4) pp. 2589-2592. (22) Filed: Dec. 3, 2009 Clackson T. et al., “Making antibody fragments using phage display libraries. Nature, 1991, 352, 624–628. (65) Prior Publication Data Coligan, et al., Current Protocols in Protein Science, TOC, U.S. Appl. US 2011 FO136103 A1 Jun. 9, 2011 No. 12/443,492, filled on Oct. 12, 2007. Co-pending U.S. Appl. No. 06/921,979. (51) Int. Cl. Co-pending U.S. Appl. No. 07/150,278. GOIN33/53 (2006.01) Co-pending U.S. Appl. No. 07/375,029. Daniel P. Stites, et al., “Basic and Clinical Immunology” LANGE GOIN3L/00 (2006.01) medical book, 1991. (52) U.S. Cl. ......... 435/7.21: 435/4; 435/7.1; 435/287.9; David J. Asai, et al. "Methods in Cell Biology’ Antibodies in Cell 436/501; 436/518; 436/525; 436/529; 436/535: Biology, vol. 37, 1993. 436/809; 427/287; 427/337; 427/338; 530/300; Goran Kronvall, et al. "A Surface Component in Group A, C, and G 530/350 Streptococci With Non-Immune Reactivity for Immunoglobulin G” (58) Field of Classification Search ........................ None Boilinology, vol. 111 (5), 1973. See application file for complete search history. Griffiths A. D., et al., "Human anti-self antibodies with high speci ficity from phage display libraries.” The EMBO J, 1993, 12 (2), (56) References Cited 725-734. Hoogenboom H. R., et al., Multi-subunit proteins on the surface of U.S. PATENT DOCUMENTS filamentous phage: methodologies for displaying antibody (Fab) heavy and light chains, Nucleic Acids Research, 1991, 19 (15), 3,817,837 A 6, 1974 Rubenstein et al. 3,850,752 A 11/1974 Schuurs et al. Oxford University Press, 4133-4137. 3,939,350 A 2f1976 Kronicket al. Kohler G. et al., “Continuous cultures of fused cells Secreting anti 3.996,345 A 12/1976 Ullman et al. body of predefined specificity.” Nature, 1975, 256 (5517), 495-497. 4,275,149 A 6, 1981 Litman et al. Langone, et al., “Production of Antisera with Small Doses of 4,277.437 A 7, 1981 Maggio Immunogen: Multiple Intradermal Injections'. MethodsEnzymol 4,366,241 A 12/1982 Tom et al. ogy, vol. 73, 46-52, 1981. 5,006,309 A 4, 1991 Khali1 et al. Marks, J. D. et al., “By-passing immunization. Human antibodies 5,063,081 A 11, 1991 Cozzette et al. from V-gene libraries displayed on phage.” J Mol Biol. 1991, vol. 5,089,424 A 2f1992 Khali1 et al. 222, pp. 581-597. 5,244,630 A 9, 1993 Khali1 et al. Marks, J.D. etal. (1992). “By-Passing Immunization: Building High 5,468,646 A 1 1/1995 Mattingly et al. Affinity Human Antibodies by Chain Shuffling.” Bio/Technol. 5,543,524 A 8/1996 Mattingly et al. 5,783,699 A 7/1998 Mattingly et al. 10:779:783. cited by other. 6,670,115 B1 12/2003 Zhang Mattingly et al., “Chemiluminescent N-Sulfonylacridinium-9- 6,682,648 B1 1/2004 MacPhee et al. Carboxamides and Their Application in Clinical Assays.” Lumines 6,887,714 B2 5, 2005 Fritsch et al. cence Biotechnology: Instruments and Applications (CRC Press: 7,045,310 B2 5/2006 Buck, Jr. et al. Boca Raton 2000), 2002, pp. 77-105. 7,045,364 B2 5/2006 Limoges et al. Mattingly Phillip G. "Chemiluminescent 10-Methyl-Acridinium 2003/0170881 A1 9, 2003 Davis et al. 9(N-Sulphonylcarboxamide) Salts. Synthesis and Kinetics of Light 2004/OO18577 A1 1/2004 Emerson Campbell et al. Emission.” Journal of Bioluminescence and Chemiluminescence, 2005.0054O78 A1 3/2005 Miller et al. 1991, pp. 107-114, vol. 6. 2006,016O164 A1 7/2006 Miller et al. FOREIGN PATENT DOCUMENTS (Continued) EP 425633 B1 T 1994 Primary Examiner — Lisa Cook EP 273.115 B1 9, 1994 EP 424,634 B1 6, 1995 (74) Attorney, Agent, or Firm — Cheryl L. Becker EP 406473 B1 9, 1995 EP 326100 B1 9, 1996 (57) ABSTRACT The present disclosure provides immunoassays and kits for OTHER PUBLICATIONS detection or quantification of an analyte of interest in a test Adamczyk et al., “Linker-Medicated Modulation of the sample that potentially contains endogenously produced Cheiluminescent Signal From N10-(3-Sulfopropyl)-N- autoantibodies reactive with the analyte. Sulfonylacridinium-9-carboxamide Tracers.” Bioconjugate Chem. 2000, pp. 714-724, vol. 11. 19 Claims, 4 Drawing Sheets US 8,183,002 B2 Page 2 OTHER PUBLICATIONS Razavi, “Stable and versatile active acridinium esters I. Lumines McCafferty J., et al., “Phage antibodies: filamentous phage display- cence, 2000, pp. 239-244, vol. 15. ing antibody variable domains.” Nature, 1990, 348, 552-554. Razavi, “Stable and versatile active acridinium esters II. Lumines McCapra, et al., “Chemiluminescence Involving Peroxide Decom- cence, 2000, pp. 245-249, vol. 15. positions'. Photochemistry and Photobiology, 1965, 4, 1111-1121. U.S. Appl. No. 1 1/588,073, filed Oct. 26, 2006. U.S. Patent May 22, 2012 Sheet 1 of 4 US 8,183,002 B2 Symbol Key: Detection antibody (DA) Analyte (A) A Analyte-epitopes Capture antibody (CA) Solid support (SS) Auto-antibodies (AA) Unrelated antibodies (UA) Immunodetection Test Sample complex Signal FIG. 1 U.S. Patent May 22, 2012 Sheet 2 of 4 US 8,183,002 B2 y - Test Sample Immunodetection complex FIG. 2 U.S. Patent May 22, 2012 Sheet 3 of 4 US 8,183,002 B2 18OOOO 16OOOO 140000 ----------------- 120000 1OOOOO 8OOOO 6OOOO 4OOOO 20000 | O f p O 5 1O 15 20 25 higG) (mg/mL) FIG. 3 U.S. Patent May 22, 2012 Sheet 4 of 4 US 8,183,002 B2 25000 - 111 20000 15000 10000 5000 2.08 mg/mL I- - O O.5 1 15 2 2.5 higG) (mg/mL) FIG. 4 US 8,183,002 B2 1. 2 AUTOANTIBODY ENHANCED SUMMARY IMMUNOASSAYS AND KITS In one aspect, the present disclosure relates to an immu RELATED APPLICATION INFORMATION noassay for detecting an analyte of interest in a test sample, the immunoassay comprising the steps of None. (a) contacting a test sample Suspected of containing an analyte of interest with a first antibody that binds to at least TECHNICAL FIELD one epitope on the analyte of interest to form a first antibody analyte complex, wherein the first antibody is immobilized on The present disclosure relates to immunoassays and kits 10 a Solid phase, and further wherein at least one autoantibody in for detecting an analyte of interest in a test sample, and in the test sample binds to at least one epitope on the analyte of particular to methods and kits for detecting an analyte in a interest to form an autoantibody-analyte complex, wherein human test sample that may contain endogenous anti-analyte said autoantibody binds to the solid phase: antibodies. (b) contacting said mixture comprising a first antibody 15 analyte complex and an autoantibody-analyte complex with a BACKGROUND second antibody to form a measurable assembly comprising a first antibody-analyte-second antibody complex and an Immunoassay techniques have been known for the last few autoantibody-analyte-second antibody complex; wherein the decades and are now commonly used in medicine for a wide second antibody binds to at least one epitope on the analyte of variety of diagnostic purposes to detect target analytes in a interest, and further wherein, an optical, electrical, or change biological sample. Immunoassays exploit the highly specific of-state signal of the assembly is measured. binding of an antibody to its corresponding antigen, wherein In the above immunoassay, the second antibody can be the antigen is the target analyte. Typically, quantification of conjugated to a detectable label, wherein the detectable label either the antibody or antigen is achieved through some form is an enzyme, oligonucleotide, nanoparticle chemilumino of labeling Such as radio- or fluorescence-labeling. Sandwich 25 phore, fluorophore, fluorescence quencher, chemilumines immunoassays involve binding the target analyte in the cence quencher, or biotin. sample to the antibody site (which is frequently bound to a In the above immunoassay, an optical signal can be mea Solid Support), binding labeled antibody to the captured ana Sured as an analyte concentration-dependent change in lyte, and then measuring the amount of bound labeled anti chemiluminescence, fluorescence, phosphorescence, electro body, wherein the label generates a signal proportional to the 30 chemiluminescence, ultraviolet absorption, visible absorp concentration of the target analyte inasmuch as labeled anti tion, infrared absorption, refraction, Surface plasmon reso body does not bind unless the analyte is present in the sample.
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