WO2011020434A1 - Anticorps se liant à la protéine du bactériophage de mycobacterium tuberculosis, et procédé de préparation et utilisation de celui-ci - Google Patents

Anticorps se liant à la protéine du bactériophage de mycobacterium tuberculosis, et procédé de préparation et utilisation de celui-ci Download PDF

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Publication number
WO2011020434A1
WO2011020434A1 PCT/CN2010/076121 CN2010076121W WO2011020434A1 WO 2011020434 A1 WO2011020434 A1 WO 2011020434A1 CN 2010076121 W CN2010076121 W CN 2010076121W WO 2011020434 A1 WO2011020434 A1 WO 2011020434A1
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Prior art keywords
antibody
mycobacterium tuberculosis
phage
protein
fragment
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PCT/CN2010/076121
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English (en)
Chinese (zh)
Inventor
胡志能
杨挥
Original Assignee
上海英伯肯医学生物技术有限公司
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Priority claimed from CN 200910057771 external-priority patent/CN101993490B/zh
Priority claimed from CN 200910057772 external-priority patent/CN101993491B/zh
Priority claimed from CN 200910057773 external-priority patent/CN101995464B/zh
Application filed by 上海英伯肯医学生物技术有限公司 filed Critical 上海英伯肯医学生物技术有限公司
Publication of WO2011020434A1 publication Critical patent/WO2011020434A1/fr

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    • G—PHYSICS
    • G01—MEASURING; TESTING
    • G01N—INVESTIGATING OR ANALYSING MATERIALS BY DETERMINING THEIR CHEMICAL OR PHYSICAL PROPERTIES
    • G01N33/00—Investigating or analysing materials by specific methods not covered by groups G01N1/00 - G01N31/00
    • G01N33/48—Biological material, e.g. blood, urine; Haemocytometers
    • G01N33/50—Chemical analysis of biological material, e.g. blood, urine; Testing involving biospecific ligand binding methods; Immunological testing
    • G01N33/53—Immunoassay; Biospecific binding assay; Materials therefor
    • G01N33/569—Immunoassay; Biospecific binding assay; Materials therefor for microorganisms, e.g. protozoa, bacteria, viruses
    • G01N33/56911—Bacteria
    • G01N33/5695—Mycobacteria
    • C—CHEMISTRY; METALLURGY
    • C07—ORGANIC CHEMISTRY
    • C07K—PEPTIDES
    • C07K16/00—Immunoglobulins [IGs], e.g. monoclonal or polyclonal antibodies
    • C07K16/08—Immunoglobulins [IGs], e.g. monoclonal or polyclonal antibodies against material from viruses
    • C—CHEMISTRY; METALLURGY
    • C07—ORGANIC CHEMISTRY
    • C07K—PEPTIDES
    • C07K16/00—Immunoglobulins [IGs], e.g. monoclonal or polyclonal antibodies
    • C07K16/12—Immunoglobulins [IGs], e.g. monoclonal or polyclonal antibodies against material from bacteria
    • C07K16/1267—Immunoglobulins [IGs], e.g. monoclonal or polyclonal antibodies against material from bacteria from Gram-positive bacteria
    • C07K16/1289—Immunoglobulins [IGs], e.g. monoclonal or polyclonal antibodies against material from bacteria from Gram-positive bacteria from Mycobacteriaceae (F)
    • G—PHYSICS
    • G01—MEASURING; TESTING
    • G01N—INVESTIGATING OR ANALYSING MATERIALS BY DETERMINING THEIR CHEMICAL OR PHYSICAL PROPERTIES
    • G01N2333/00—Assays involving biological materials from specific organisms or of a specific nature
    • G01N2333/195—Assays involving biological materials from specific organisms or of a specific nature from bacteria
    • G01N2333/35—Assays involving biological materials from specific organisms or of a specific nature from bacteria from Mycobacteriaceae (F)

Definitions

  • the present invention relates to an antibody, and more particularly to an antibody which binds to the Mycobacterium tuberculosis phage tail protein; in addition, the present invention also relates to a method and an application for the preparation of the antibody against the Mycobacterium tuberculosis phage tail protein. Background technique
  • Tuberculosis is a chronic infectious disease caused by Mycobacterium tuberculosis, which is the main cause of death from a single infectious bacterium.
  • AIDS the increase in the number of patients with multiple malignancies, and the emergence of multiple drug-resistant strains, it has increased the difficulty in the prevention and treatment of tuberculosis infection.
  • tuberculosis There are 330 million tuberculosis patients in China, 6 million tuberculosis patients, and 250,000 deaths due to tuberculosis each year, which is twice the death rate of various infectious diseases. Therefore, China has raised tuberculosis from Class C infectious diseases to Class B infectious diseases. , included in the strict management category. According to WHO statistics, between 50,000 and 100 million people worldwide are infected with tuberculosis each year, and about 3 million people die of tuberculosis, more than 80% of which are in developing countries. Therefore, how to quickly diagnose and treat as soon as possible becomes a key link in controlling the spread and spread of tuberculosis.
  • tuberculosis is mainly based on sputum examination, including acid-fast bacilli smear microscopy and tuberculosis culture.
  • the bacteriological examination of Mycobacterium tuberculosis is an important basis for the diagnosis of tuberculosis. Acid-fast bacilli smears have low sensitivity, poor specificity, and are incapable of determining bacterial life and death.
  • Mycobacterium tuberculosis culture usually inoculates the specimen to be inoculated to a modified Roche medium, and cultures at 37 ° C for 20 to 60 days.
  • phage rapid amplification has utilized the rapid growth characteristics of M. smegmatis and the relative specificity of D29 phage for rapid detection of Mycobacterium tuberculosis.
  • the core content of this method is:
  • the method has strong specificity and clear results, and can be used for rapid identification of live Mycobacterium tuberculosis in various samples to be tested without special instruments; however, the entire test takes at least 48 hours to complete, and the operation is complicated and the sensitivity is also Not high enough.
  • PCR polymerase chain reaction
  • ELISA ⁇ per ear immunity Enzyme linked immunosorbent assay
  • DIGFA dot immuno-gold filtration assay
  • ICT immunochromatographic assay
  • Polymerase chain reaction is an in vitro enzymatic amplification technique that mediates a specific sequence fragment of Mycobacterium tuberculosis DNA in a specimen to be examined by a pair of specific oligonucleotide primers, through three different temperatures, dozens of denaturation, renaturation, extension Cycles, specific target sequences can be amplified millions of times, showing their rapid, high sensitivity, quantitative analysis, and theoretically high specificity.
  • the method is more complex Miscellaneous, the technical requirements for operating equipment and personnel are high, and the laboratory is prone to pollution.
  • Enzyme-linked immunosorbent assay, dot immunogold filtration assay and immunochromatography are all assays based on the development of serum immunology. These methods are based on the characteristic antigen of Mycobacterium tuberculosis, and the labeled anti-human immunoglobulin or Staphylococal Protein A (SPA) is used as an indicator system to detect the presence of anti-tuberculosis mycobacteria in the patient. Circulating antibodies, indirectly diagnose the patient's condition. Enzyme labeling requires specialized instruments and highly skilled professionals. Both immunofiltration and immunochromatography do not require any instrument, and the time required for detection is greatly shortened, the operation is simple, and the results are intuitive.
  • SPA Staphylococal Protein A
  • One of the technical problems to be solved by the present invention is to provide an antibody which binds to a Mycobacterium tuberculosis bacteriophage protein.
  • the second technical problem to be solved by the present invention is to provide a method for preparing the antibody which binds to the Mycobacterium tuberculosis bacteriophage protein.
  • the third technical problem to be solved by the present invention is to provide an application of the antibody against the Mycobacterium tuberculosis bacteriophage protein in the detection of Mycobacterium tuberculosis.
  • an antibody that binds to a Mycobacterium tuberculosis phage protein which recognizes Mycobacterium tuberculosis bacteriophage.
  • the bacteriophage protein refers to a phage tail protein or a head protein.
  • the present invention first provides an antibody that binds to the Mycobacterium tuberculosis phage tail protein, which recognizes Mycobacterium tuberculosis bacteriophage.
  • the antibody is a monoclonal antibody.
  • the antibody is an antibody fragment.
  • the antibody is a Fab.
  • the antibody is a labeled antibody.
  • the antibody is a colloidal gold-labeled antibody.
  • the antibody is obtained by immunizing a mouse with a polypeptide comprising amino acids 20 to 80 of the Mycobacterium tuberculosis phage tail protein; the Mycobacterium tuberculosis phage tail protein fragment has the nucleotide sequence shown in SEQ ID NO: 1 and SEQ ID NO: 2 The amino acid sequence shown.
  • a method for producing an antibody that binds to a Mycobacterium tuberculosis phage tail protein comprising the steps of:
  • mice were immunized with the phage phage tail protein fragment purified by the step (1), and the spleen cells were fused with the myeloma cells, and the cell line producing the antibody was selected, and the mouse peritoneal cavity was injected; the ascites was taken about 10 days after the injection. And purify the antibody.
  • the present invention provides an antibody which binds to a Mycobacterium tuberculosis phage head protein which recognizes Mycobacterium tuberculosis bacteriophage.
  • the antibody is a monoclonal antibody.
  • the antibody is an antibody fragment.
  • the antibody is a Fab.
  • the antibody is a labeled antibody.
  • the antibody is a colloidal gold-labeled antibody.
  • the antibody is obtained by immunizing a mouse with a polypeptide comprising amino acids 180 to 230 of the Mycobacterium tuberculosis phage head protein; the Mycobacterium tuberculosis phage head protein fragment has the nucleotide sequence and SEQ ID of SEQ ID NO: NO: The amino acid sequence shown in 4.
  • a method for producing an antibody that binds to a Mycobacterium tuberculosis phage head protein comprising the steps of:
  • mice were immunized with the phage phage head protein fragment purified by the step (1), and the spleen cells were fused with the myeloma cells, and the cell line producing the antibody was selected, and the mouse peritoneal cavity was injected; about 10 days after the injection. Ascites and purified antibodies.
  • a method for detecting Mycobacterium tuberculosis by using an antibody against Mycobacterium tuberculosis phage protein and a method for detecting a Mycobacterium tuberculosis phage by a colloidal gold immunochromatographic test, and testing a colloidal gold label in a pen
  • the antibody is an antibody that binds to the Mycobacterium tuberculosis phage protein
  • the antibody immobilized on the test line is an antibody that binds to the Mycobacterium tuberculosis phage protein.
  • the bacteriophage protein is selected from the group consisting of a phage tail protein and a phage head protein as described above.
  • the present invention has the following beneficial effects:
  • the antibody recognizes the bacterial protein of Mycobacterium tuberculosis phage D29, thereby recognizing the Mycobacterium tuberculosis bacteriophage D29, and further determines whether there is a live Mycobacterium tuberculosis in the test sample by the established method.
  • the antibody of the present invention can rapidly recognize the phage, further shorten the time for detecting the Mycobacterium tuberculosis by the phage amplification method, and at the same time, improve the sensitivity of the detection.
  • a method for detecting Mycobacterium tuberculosis which can quickly recognize Mycobacterium tuberculosis phage, thereby reflecting the number of Mycobacterium tuberculosis, which greatly shortens the detection time because the detection step is simplified.
  • the present invention provides a method for detecting Mycobacterium tuberculosis, comprising the following steps:
  • a phage colloidal gold immunochromatographic test pen was prepared using an anti-phage antibody gold standard, and the phage was detected using the test pen.
  • the colloidal gold-labeled antibody in the test pen described in the above step 3 is an antibody that recognizes the Mycobacterium tuberculosis phage head protein or the tail protein, and the antibody immobilized on the test line is an antibody that recognizes the Mycobacterium tuberculosis phage head protein or the tail protein.
  • the colloidal gold-labeled antibody in the test pen is an antibody that recognizes the Mycobacterium tuberculosis phage head protein
  • the antibody immobilized on the test line is also an antibody that recognizes the Mycobacterium tuberculosis phage head protein.
  • the colloidal gold-labeled antibody in the pen is an antibody that recognizes the Mycobacterium tuberculosis phage head protein, and the antibody immobilized on the test line is an antibody that recognizes the Mycobacterium tuberculosis phage tail protein.
  • the colloidal gold-labeled antibody in the test pen is an antibody that recognizes the Mycobacterium tuberculosis phage tail protein, and the antibody immobilized on the test line is an antibody that recognizes the Mycobacterium tuberculosis phage head protein.
  • the antibody recognizing the Mycobacterium tuberculosis phage tail protein specifically binds to Mycobacterium tuberculosis phage tail protein, which has the nucleotide sequence shown in SEQ ID NO: 1 and the amino acid sequence shown in SEQ ID NO: 2.
  • the antibody recognizing the Mycobacterium tuberculosis phage head protein specifically binds to a Mycobacterium tuberculosis phage head protein fragment having the nucleotide sequence shown in SEQ ID NO: 3 and the nucleotide sequence shown in SEQ ID NO: Amino acid sequence.
  • Step 1) Specifically divided into two categories:
  • the enrichment liquid is 5-7 parts by weight of Mich 7H9 medium, 1-2 parts by weight of calcium chloride, 25-50 parts by weight of ampicillin, 25-50 parts by weight of amphotericin B, and bovine serum albumin 100- 200 parts by weight, 10-15 parts by weight of glucose, 1-2 parts by weight of oleic acid and 0.1-0.2 parts by weight of catalase are prepared by dissolving in 1000 parts by weight of pure water.
  • the present invention has the following beneficial effects: With the method of the present invention, the Mycobacterium tuberculosis phage can be quickly recognized, thereby reflecting the number of Mycobacterium tuberculosis. Since it is neither necessary to kill the phage that is vaccinated nor to be added to the phobic bacillus incubation or overnight culture on the agar plate to form plaques, the detection step is not only simplified, but also the detection time is shortened.
  • mAb monoclonal antibody
  • monoclonal antibody refers to an immunoglobulin obtained from a pure lineage cell which has the same structural and chemical properties and is specific for a single antigenic determinant. Unlike monoclonal antibody preparations (typically having different antibodies to different determinants), monoclonal antibodies are directed against a single determinant on the antigen. In addition to their specificity, Monoclonal antibodies also have the advantage that they are obtained by hybridoma or recombinant engineered cell culture without intermixing with other immunoglobulins. The modifier “monoclonal” indicates the identity of the antibody and is obtained from a homogeneous population of antibodies, which should not be construed as requiring any particular method of production of the antibody.
  • the nucleotide sequence of the Mycobacterium tuberculosis phage D29 tail protein fragment is shown in SEQ ID NO: 1, and the amino acid sequence of the Mycobacterium tuberculosis phage D29 tail protein fragment is shown in SEQ ID NO: 2.
  • the nucleic acid containing the sequence of SEQ ID ⁇ : 1 was inserted into the pcDNA3 vector (purchased from Invitrogen) by molecular cloning, and the correct clone was amplified by sequencing, and the DNA was extracted, transformed into E. coli, and the D29 tail protein fragment was expressed and purified.
  • the previously purified D29 tail protein fragment was mixed with an equal volume of Freund's adjuvant to prepare a water-in-oil emulsion.
  • Each mouse was intraperitoneally injected with 0.5 ml of the above mixture (containing the tail protein fragment 100 ⁇ ⁇ ), and a total of 6 BALB/ c mice. Two weeks later, the same dose of antigen plus Freund's incomplete adjuvant was used to boost the immunization.
  • the indirect ELISA was used to detect the titer of the serum tail protein polyclonal antibody in mice. The high titer was then immunized once in the tail vein, each 20 ⁇ ⁇ , 3 Cell fusion was performed after the day.
  • the spleen cell suspension of the immunized mouse and the SP2/0 myeloma cells were fused in a ratio of 5:1 by a conventional method under the action of polyethylene glycol, and cultured by using HAT complete 1640 medium.
  • the D29 tail protein (lg/ml) was used as an antigen-coated 96-well plate, and the hybridoma cell culture supernatant was detected by indirect ELISA.
  • the OD490 (absorption at 490 nm) was 10 times higher than that of the negative control.
  • the antibody hybridoma cell line is extensively expanded and cryopreserved, and after long-term subculture, it is again cloned and identified in the same manner.
  • mice BALB/c mice were injected with 0.5 ml of incomplete Freund's adjuvant in the peritoneal cavity. After 5-7 days, each mouse was intraperitoneally injected with 0.5 ml of a solution containing 2 ⁇ 10 6 hybridoma cells, and 7 to 10 days later, the mice were treated. Ascites was collected for the degree of abdominal distension.
  • the monoclonal antibody against the D29 tail protein was purified by 50% (mass to volume) saturated ammonium sulfate salting out and Protein G affinity chromatography, and the obtained monoclonal antibody was identified by protein electrophoresis.
  • Example 2 Amplification and detection of D29 phage in Mycobacterium tuberculosis and Mycobacterium tuberculosis
  • enrichment liquid (7 g of M. 7H9 medium, 2 g of CaCl 2 , 50 g of ampicillin, 50 g of amphotericin B, 200 g of BSA, 15 g of glucose, 2 g of oleic acid and 0.2 g of catalase were dissolved in 1 L of water. 2ml, 37 ° C culture for 18 to 24 hours;
  • the phage solution can be obtained by the method described in Chinese Patent Application Specification No. 200810043709.4, filed on August 14, 2008, entitled “A Method and Kit for Rapid Detection of Mycobacterium Tuberculosis”
  • a colloidal gold immunochromatographic test pen (a gold probe was obtained by labeling an antibody against the D29 tail protein prepared in Example 1 with colloidal gold, and a test line antibody was also used for the antibody) to detect a phage concentration, thereby indirectly detecting Mycobacterium tuberculosis.
  • Tuberculosis rod detected by this method At least 100 bacteria.
  • the nucleotide sequence of the Mycobacterium tuberculosis phage D29 head protein fragment is shown in SEQ ID NO: 3, and the amino acid sequence of the Mycobacterium tuberculosis phage D29 head protein fragment is shown in SEQ ID NO: 4.
  • the nucleic acid containing the sequence of SEQ ID NO: 3 was inserted into the pcDNA3 vector (purchased from Invitrogen) by molecular cloning, and the correct clone was amplified after sequencing, and the DNA was extracted and transformed into E. coli, and the D29 head protein was expressed and purified. Fragment.
  • the previously purified D29 head protein fragment was mixed with an equal volume of Freund's adjuvant to prepare a water-in-oil emulsion.
  • Each mouse was intraperitoneally injected with 0.5 ml of the above mixture (containing the head protein fragment 100 ⁇ ⁇ ), and a total of 6 injections were made.
  • BALB/c mice Two weeks later, the same dose of antigen plus Freund's incomplete adjuvant was used to boost the immunization.
  • the indirect ELISA was used to detect the titer of the serum cephalosporin polyclonal antibody in mice. The valency of the head vein was again immunized once, each 20 ⁇ ⁇ , Cell fusion was performed 3 days later.
  • the spleen cell suspension of the immunized mouse and the SP2/0 myeloma cells were fused in a ratio of 5:1 by a conventional method under the action of polyethylene glycol, and cultured by using HAT complete 1640 medium.
  • the D29 head protein (lg/ml) was used as an antigen-coated 96-well plate, and the hybridoma cell culture supernatant was detected by indirect ELISA.
  • the OD490 (absorption at 490 nm) was 10 times higher than that of the negative control. Subcloning is performed and amplification is performed. After three times of limiting dilution cloning, the hybridoma cell line secreting the specific antibody was extensively expanded and frozen, and after long-term subculture, it was cloned and identified again by the same method.
  • mice BALB/c mice were injected with 0.5 ml of incomplete Freund's adjuvant in the peritoneal cavity. After 5-7 days, each mouse was intraperitoneally injected with 0.5 ml of a solution containing 2 ⁇ 10 6 hybridoma cells, and 7 to 10 days later, the mice were treated. Ascites was collected for the degree of abdominal distension. d) purification of monoclonal antibodies
  • the monoclonal antibody against the D29 head protein was purified by 50% (mass to volume) saturated ammonium sulfate salting out and Protein G affinity chromatography, and the obtained monoclonal antibody was identified by protein electrophoresis.
  • Example 4 Amplification and detection of D29 phage in Mycobacterium tuberculosis and Mycobacterium tuberculosis
  • enrichment liquid (7 g of M. 7H9 medium, 2 g of CaCl 2 , 50 g of ampicillin, 50 g of amphotericin B, 200 g of BSA, 15 g of glucose, 2 g of oleic acid and 0.2 g of catalase were dissolved in 1 L of water. 2ml, 37 ° C culture for 18 to 24 hours;
  • the phage solution can be obtained by the method described in Chinese Patent Application Specification No. 200810043709.4, filed on August 14, 2008, entitled “A Method and Kit for Rapid Detection of Mycobacterium Tuberculosis”
  • a colloidal gold immunochromatographic test pen (a gold probe was obtained by labeling an antibody against D29 head protein prepared in Example 3 with colloidal gold, and a test line antibody was also used for the antibody) to detect a phage concentration, thereby indirectly detecting Mycobacterium tuberculosis.
  • the number of tuberculosis bacteria detected by this method is at least 100.

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Abstract

L’invention concerne un anticorps qui peut se lier à la protéine du bactériophage de Mycobacterium tuberculosis. L’invention concerne également un procédé de préparation de l’anticorps, une utilisation de l’anticorps pour la détection de Mycobacterium tuberculosis, et un procédé de détection de Mycobacterium tuberculosis.
PCT/CN2010/076121 2009-08-20 2010-08-19 Anticorps se liant à la protéine du bactériophage de mycobacterium tuberculosis, et procédé de préparation et utilisation de celui-ci WO2011020434A1 (fr)

Applications Claiming Priority (6)

Application Number Priority Date Filing Date Title
CN 200910057771 CN101993490B (zh) 2009-08-20 2009-08-20 结合结核杆菌噬菌体尾部蛋白的抗体及其制备方法和应用
CN200910057773.2 2009-08-20
CN 200910057772 CN101993491B (zh) 2009-08-20 2009-08-20 结合结核杆菌噬菌体头部蛋白的抗体及其制备方法和应用
CN 200910057773 CN101995464B (zh) 2009-08-20 2009-08-20 一种检测结核杆菌的方法
CN200910057771.3 2009-08-20
CN200910057772.8 2009-08-20

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WO2011020434A1 true WO2011020434A1 (fr) 2011-02-24

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Citations (2)

* Cited by examiner, † Cited by third party
Publication number Priority date Publication date Assignee Title
CN101329342A (zh) * 2007-06-22 2008-12-24 王霁 检测结核菌和抗结核药物敏感性的方法及试剂盒
CN101650365A (zh) * 2008-08-14 2010-02-17 上海英伯肯医学生物技术有限公司 一种快速检测结核杆菌的方法和试剂盒

Patent Citations (2)

* Cited by examiner, † Cited by third party
Publication number Priority date Publication date Assignee Title
CN101329342A (zh) * 2007-06-22 2008-12-24 王霁 检测结核菌和抗结核药物敏感性的方法及试剂盒
CN101650365A (zh) * 2008-08-14 2010-02-17 上海英伯肯医学生物技术有限公司 一种快速检测结核杆菌的方法和试剂盒

Non-Patent Citations (1)

* Cited by examiner, † Cited by third party
Title
MICHAEL E. FORD ET AL.: "Genome Structure of Mycobacteriophage D29: Implications for Phage Evolution", J. MOL. BIOL., vol. 279, 1998, pages 143 - 164, XP004462420, DOI: doi:10.1006/jmbi.1997.1610 *

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