WO2002026812A1 - Nouveau polypeptide, proteine de type humain 16.17 de liaison a la repetition adn cgg, et polynucleotide codant ce polypeptide - Google Patents

Nouveau polypeptide, proteine de type humain 16.17 de liaison a la repetition adn cgg, et polynucleotide codant ce polypeptide Download PDF

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Publication number
WO2002026812A1
WO2002026812A1 PCT/CN2001/000910 CN0100910W WO0226812A1 WO 2002026812 A1 WO2002026812 A1 WO 2002026812A1 CN 0100910 W CN0100910 W CN 0100910W WO 0226812 A1 WO0226812 A1 WO 0226812A1
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WIPO (PCT)
Prior art keywords
polypeptide
polynucleotide
binding protein
cgg repeat
human
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PCT/CN2001/000910
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English (en)
Chinese (zh)
Inventor
Yumin Mao
Yi Xie
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Shanghai Biowindow Gene Development Inc.
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Priority to AU2001289517A priority Critical patent/AU2001289517A1/en
Publication of WO2002026812A1 publication Critical patent/WO2002026812A1/fr

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    • C—CHEMISTRY; METALLURGY
    • C07—ORGANIC CHEMISTRY
    • C07K—PEPTIDES
    • C07K14/00—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof
    • C07K14/435—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof from animals; from humans
    • C07K14/46—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof from animals; from humans from vertebrates
    • C07K14/47—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof from animals; from humans from vertebrates from mammals
    • A—HUMAN NECESSITIES
    • A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
    • A61K—PREPARATIONS FOR MEDICAL, DENTAL OR TOILETRY PURPOSES
    • A61K38/00—Medicinal preparations containing peptides
    • A—HUMAN NECESSITIES
    • A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
    • A61K—PREPARATIONS FOR MEDICAL, DENTAL OR TOILETRY PURPOSES
    • A61K48/00—Medicinal preparations containing genetic material which is inserted into cells of the living body to treat genetic diseases; Gene therapy

Definitions

  • the present invention belongs to the field of biotechnology. Specifically, the present invention describes a new polypeptide ⁇ A-type DNA CGG repeat binding protein 16.17, and a polynucleotide sequence encoding the polypeptide. The invention also relates to a preparation method and application of the polynucleotide and polypeptide.
  • the 5,-(CGG) n -3 'repeat is located in the 5, untranslated region (UTR) of the fragile X syndrome 1 gene (FMR1). If the n value is greater than 200 and the gene is methylated and inactivated, the gene product will be widely expressed in many human tissues, the first being the human nervous system [Devys, D., Lutz, Y., Rouyer, et al. 1993 Nat. Genet. 4, 335-340].
  • the p20 protein is a nuclear protein and is abundantly expressed in mammals [Deissler, H., WUm, M., Genc, et al. 1997. J. Biol. Chem. 272, 16761-16768], and is specific in the human genome Binding to 5,-(CGG) n -3, repeaters.
  • the p20 protein is located in the nucleus and carries nuclear localization signals (NLS) between 80 and 84.
  • An object of the present invention is to provide an isolated novel polypeptide-human DNA CGG repeat binding protein 16.17 and fragments, analogs and derivatives thereof.
  • sequence of the polynucleotide is one selected from the group consisting of: (a) a sequence having positions 511-5954 in SEQ ID NO: 1; and (b) a sequence having 1-1570 in SEQ ID NO: 1 Sequence of bits.
  • the present invention further relates to a vector, particularly an expression vector, containing the polynucleotide of the present invention; a host cell genetically engineered with the vector, including a transformed, transduced or transfected host cell; Host cell and method of preparing the polypeptide of the present invention by recovering the expression product.
  • a “variant" of a protein or polynucleotide refers to an amino acid sequence having one or more amino acids or nucleotide changes or a polynucleotide sequence encoding it.
  • the changes may include deletions, insertions or substitutions of amino acids or nucleotides in the amino acid sequence or nucleotide sequence.
  • Variants can have "conservative" changes, in which the amino acid substituted has a structural or chemical property similar to the original amino acid, such as replacing isoleucine with leucine.
  • Variants can also have non-conservative changes, such as replacing glycine with tryptophan.
  • An "agonist” is a molecule that, when combined with the human DNA CGG repeat binding protein 16.17, can cause the protein to change, thereby regulating the activity of the protein.
  • An agonist may include a protein, a nucleic acid, a carbohydrate, or any other molecule that can bind human DNA CGG repeat binding protein 16.17.
  • isolated human DM CGG repeat binding protein 16. 17 refers to human DNA CGG repeat binding protein 16. 17 which is substantially free of other proteins, lipids, carbohydrates or other substances naturally associated with it. Those skilled in the art can purify human DM CGG repeat binding protein 16.17 using standard protein purification techniques. Substantially pure polypeptides can produce a single main band on a non-reducing polyacrylamide gel. Human DM CGG repeat binding protein 16. 17 The purity of the polypeptide can be analyzed by amino acid sequence.
  • the polynucleotide encoding the mature polypeptide of SEQ ID NO: 2 includes: only the coding sequence of the mature polypeptide; the coding sequence of the mature polypeptide and various additional coding sequences; the coding sequence of the mature polypeptide (and optional additional coding sequences); Coding sequence.
  • polypeptides and polynucleotides in the present invention are preferably provided in an isolated form and are more preferably purified to homogeneity.
  • the specific polynucleotide sequence encoding the human DM CGG repeat binding protein 16.17 of the present invention can be obtained by various methods.
  • polynucleotides are isolated using hybridization techniques well known in the art. These techniques include, but are not limited to: 1) hybridization of probes to genomic or cDNA libraries to detect homologous polynucleotide sequences, and 2) antibody screening of expression libraries to detect cloned polynucleosides with common structural characteristics Acid fragments.
  • the protein product of the human D CGG repeat binding protein 16. 17 gene can be detected by immunological techniques such as Western blotting, radioimmunoprecipitation, and enzyme-linked immunosorbent assay (ELISA).
  • immunological techniques such as Western blotting, radioimmunoprecipitation, and enzyme-linked immunosorbent assay (ELISA).
  • DM sequence can be operably linked to an appropriate promoter in an expression vector to guide the synthesis of raRNA.
  • promoters are: the lac or trp promoter of E.
  • the expression vector also includes a ribosome binding site and a transcription terminator for translation initiation. Insertion of an enhancer sequence into the vector will Its transcription is enhanced in higher eukaryotic cells. Enhancers are cis-acting factors for DNA expression, usually about 10 to 300 base pairs, which act on promoters to enhance gene transcription. Illustrative examples include SV40 enhancers of 100 to 270 base pairs on the late side of the origin of replication, polyoma enhancers on the late side of the origin of replication, and adenoviral enhancers.
  • the medium used in the culture may be selected from various conventional mediums. Culture is performed under conditions suitable for host cell growth. When the host cell has grown to an appropriate cell density, the selected promoter is induced by a suitable method (such as temperature conversion or chemical induction), and The cells are cultured for a period of time.
  • a suitable method such as temperature conversion or chemical induction
  • Repeated DNA is a major component of the human genome.
  • the amplification of these repeats can terminate the expression of adjacent genes or directly affect their amino acid sequence when the repeats are part of the coding sequence.
  • Human DNA CGG repeat-binding protein is a protein that specifically binds to the 5,-(CGG) n -3, repeater in the human genome and is involved in or regulates the expression of certain genes. Abnormal expression in the body can cause abnormal gene expression in the human body, which in turn leads to the occurrence of related diseases.
  • Horizontal absence congenital short limbs: no arms, no forearms, no hands, no fingers, no legs, no toes, etc .; longitudinal absences: radial / ulnar abscess of upper extremity, tibia / fibula absent of lower extremity, etc .;
  • Arrhythmia shock, insanity, epilepsy, chorea, hepatic encephalopathy (norepinephrine, Y-aminobutyric acid, serotonin, glutamine), motion sickness, type I allergic disease (net Measles, hay fever, allergic rhinitis, skin allergies), peptic ulcer (histamine), hypercholesterolemia (taurine), tumors (polyamines), etc .;
  • the present invention provides a method for producing antibodies using polypeptides, and fragments, derivatives, analogs or cells thereof as antigens. These antibodies can be polyclonal or monoclonal antibodies.
  • the invention also provides antibodies against the human DNA CGG repeat binding protein 16.17 epitope. These antibodies include (but are not limited to): polyclonal antibodies, monoclonal antibodies, chimeric antibodies, single chain antibodies, Fab fragments, and fragments produced by Fab expression libraries.
  • the polypeptides, polynucleotides and mimetics, agonists, antagonists and inhibitors of the present invention can be used in combination with a suitable pharmaceutical carrier.
  • suitable pharmaceutical carrier can be water, glucose, ethanol, salts, buffers Liquid, glycerin and their combinations.
  • the composition comprises a safe and effective amount of the polypeptide or antagonist, and carriers and excipients that do not affect the effect of the drug. These compositions can be used as drugs for the treatment of diseases.
  • Primer2 5'- GTAAGGAACATTAATTCTTTAATG -3 '(SEQ ID NO: 4)
  • Pr imer3 5'-CCCCATATGATGCACTTGGGTGCTTTGTTCCCC-3 '(Seq ID No: 5)
  • Pr iraer4 5, -CATGGATCCTCAGATTCGGCCCTGAAGGGCCAC-3, (Seq ID No: 6)
  • Ndel and BamHI restriction sites correspond to the expression vector plasmid pET- 2 8b (+) (Novagen, Cat. No. 69865. 3) Selective endonuclease site.
  • the probes used in this embodiment include two types: the first type of probes are oligonucleotide fragments that are completely the same as or complementary to the polynucleotide SEQ ID NO: 1 of the present invention; the second type of probes are partially related to the present invention
  • the polynucleotide SEQ ID NO: 1 is the same or complementary oligonucleotide fragment.
  • the dot blot method is used to fix the sample on the filter membrane. Under the high-intensity washing conditions, the first type of probe and the sample have the strongest hybridization specificity and are retained.
  • Those that meet the above conditions can be used as primary selection probes, and then further computer sequence analysis, including the primary selection probe and its source sequence region (ie, SEQ ID NO: 1) and other known genomic sequences and their complements Region for homology comparison, if the homology with non-target molecular region is greater than 85% or more than 15 Two consecutive bases are completely the same, the primary probe should generally not be used;

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  • Chemical & Material Sciences (AREA)
  • Health & Medical Sciences (AREA)
  • Life Sciences & Earth Sciences (AREA)
  • Organic Chemistry (AREA)
  • General Health & Medical Sciences (AREA)
  • Gastroenterology & Hepatology (AREA)
  • Biochemistry (AREA)
  • Biophysics (AREA)
  • Zoology (AREA)
  • Genetics & Genomics (AREA)
  • Medicinal Chemistry (AREA)
  • Molecular Biology (AREA)
  • Proteomics, Peptides & Aminoacids (AREA)
  • Toxicology (AREA)
  • Peptides Or Proteins (AREA)
  • Medicines That Contain Protein Lipid Enzymes And Other Medicines (AREA)
  • Micro-Organisms Or Cultivation Processes Thereof (AREA)

Abstract

L'invention concerne un nouveau polypeptide, une protéine de type humain 16.17 de liaison à la répétition ADN CGG, et un polynucléotide codant ce polypeptide ainsi qu'un procédé d'obtention de ce polypeptide par des techniques recombinantes d'ADN. L'invention concerne en outre les applications de ce polypeptide dans le traitement de maladies, notamment de malformations lors du développement de l'embryon, de tumeurs et de maladies liées aux troubles du métabolisme protéique. L'invention concerne aussi l'antagoniste agissant contre le polypeptide et son action thérapeutique ainsi que les applications de ce polynucléotide codant la protéine de type humain 16.17 de liaison à la répétition ADN CGG.
PCT/CN2001/000910 2000-06-07 2001-06-04 Nouveau polypeptide, proteine de type humain 16.17 de liaison a la repetition adn cgg, et polynucleotide codant ce polypeptide WO2002026812A1 (fr)

Priority Applications (1)

Application Number Priority Date Filing Date Title
AU2001289517A AU2001289517A1 (en) 2000-06-07 2001-06-04 A novel peptide---human dna cgg repeated associative protein 16.17 and the polynucleotide coding this novel peptide

Applications Claiming Priority (2)

Application Number Priority Date Filing Date Title
CN 00116383 CN1326990A (zh) 2000-06-07 2000-06-07 一种新的多肽——人类dna cgg重复结合蛋白16.17和编码这种多肽的多核苷酸
CN00116383.3 2000-06-07

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Cited By (10)

* Cited by examiner, † Cited by third party
Publication number Priority date Publication date Assignee Title
US8263760B2 (en) 2008-02-08 2012-09-11 Prosensa Holding Bv Methods and means for treating DNA repeat instability associated genetic disorders
US8304398B2 (en) 2006-04-20 2012-11-06 Academisch Ziekenhuis Leiden Therapeutic intervention in a genetic disease in an individual by modifying expression of an aberrantly or abnormally expressed gene
US8361979B2 (en) 2006-05-19 2013-01-29 Academisch Ziekenhuis Leiden Means and method for inducing exon-skipping
US9139828B2 (en) 2008-05-14 2015-09-22 Prosensa Technologies B.V. Method for efficient exon (44) skipping in duchenne muscular dystrophy and associated means
US9243245B2 (en) 2007-10-26 2016-01-26 Academisch Ziekenhuis Leiden Means and methods for counteracting muscle disorders
US9890379B2 (en) 2006-08-11 2018-02-13 Biomarin Technologies B.V. Treatment of genetic disorders associated with DNA repeat instability
US9896687B2 (en) 2003-03-21 2018-02-20 Academisch Ziekenhuis Leiden Modulation of exon recognition in pre-mRNA by interfering with the secondary RNA structure
US10179912B2 (en) 2012-01-27 2019-01-15 Biomarin Technologies B.V. RNA modulating oligonucleotides with improved characteristics for the treatment of duchenne and becker muscular dystrophy
US10533171B2 (en) 2009-04-24 2020-01-14 Biomarin Technologies B.V. Oligonucleotide comprising an inosine for treating DMD
USRE48468E1 (en) 2007-10-26 2021-03-16 Biomarin Technologies B.V. Means and methods for counteracting muscle disorders

Citations (1)

* Cited by examiner, † Cited by third party
Publication number Priority date Publication date Assignee Title
WO1999041410A1 (fr) * 1998-02-10 1999-08-19 Yeda Research And Development Co. Ltd. Procedes d'amplification et de sequencage d'adn

Patent Citations (1)

* Cited by examiner, † Cited by third party
Publication number Priority date Publication date Assignee Title
WO1999041410A1 (fr) * 1998-02-10 1999-08-19 Yeda Research And Development Co. Ltd. Procedes d'amplification et de sequencage d'adn

Non-Patent Citations (2)

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Title
DATABASE GENBANK [online] 30 March 2000 (2000-03-30), HATTORI M. ET AL., retrieved from GI:7768677 accession no. NCBI Database accession no. (AP001714.1) *
DATABASE PROTEIN [online] 22 February 2000 (2000-02-22), ISOGAI T. ET AL., retrieved from GI:7023290 accession no. NCBI Database accession no. (BAA91915.1) *

Cited By (26)

* Cited by examiner, † Cited by third party
Publication number Priority date Publication date Assignee Title
US10113165B2 (en) 2003-03-21 2018-10-30 Academisch Ziekenhuis Leiden Modulation of exon recognition in pre-mRNA by interfering with the secondary RNA structure
US11208657B2 (en) 2003-03-21 2021-12-28 Academisch Ziekenhuis Leiden Modulation of exon recognition in pre-mRNA by interfering with the secondary RNA structure
US10544416B2 (en) 2003-03-21 2020-01-28 Academisch Ziekenhuis Leiden Modulation of exon recognition in pre-mRNA by interfering with the secondary RNA structure
US9896687B2 (en) 2003-03-21 2018-02-20 Academisch Ziekenhuis Leiden Modulation of exon recognition in pre-mRNA by interfering with the secondary RNA structure
US10190116B2 (en) 2003-03-21 2019-01-29 Academisch Ziekenhuis Leiden Modulation of exon recognition in pre-mRNA by interfering with the secondary RNA structure
US10100304B2 (en) 2003-03-21 2018-10-16 Academisch Ziekenhuis Leiden Modulation of exon recognition in pre-mRNA by interfering with the secondary RNA structure
US8304398B2 (en) 2006-04-20 2012-11-06 Academisch Ziekenhuis Leiden Therapeutic intervention in a genetic disease in an individual by modifying expression of an aberrantly or abnormally expressed gene
US8361979B2 (en) 2006-05-19 2013-01-29 Academisch Ziekenhuis Leiden Means and method for inducing exon-skipping
US11274299B2 (en) 2006-08-11 2022-03-15 Vico Therapeutics B.V. Methods and means for treating DNA repeat instability associated genetic disorders
US10689646B2 (en) 2006-08-11 2020-06-23 Biomarin Technologies B.V. Treatment of genetic disorders associated with DNA repeat instability
US9890379B2 (en) 2006-08-11 2018-02-13 Biomarin Technologies B.V. Treatment of genetic disorders associated with DNA repeat instability
US10876114B2 (en) 2007-10-26 2020-12-29 Biomarin Technologies B.V. Methods and means for efficient skipping of at least one of the following exons of the human Duchenne muscular dystrophy gene: 43, 46, 50-53
US9243245B2 (en) 2007-10-26 2016-01-26 Academisch Ziekenhuis Leiden Means and methods for counteracting muscle disorders
US9926557B2 (en) 2007-10-26 2018-03-27 Biomarin Technologies B.V. Methods and means for efficient skipping of exon 45 in Duchenne muscular dystrophy pre-mRNA
US11427820B2 (en) 2007-10-26 2022-08-30 Biomarin Technologies B.V. Methods and means for efficient skipping of exon 45 in Duchenne muscular dystrophy pre-mRNA
US9528109B2 (en) 2007-10-26 2016-12-27 Biomarin Technologies B.V. Methods and means for efficient skipping of exon 45 in duchenne muscular dystrophy pre-mRNA
US9499818B2 (en) 2007-10-26 2016-11-22 BioMarin Technologies, B.V. Methods and means for efficient skipping of at least one of the exons 51-53, 55, 57 and 59 of the human duchenne muscular dystrophy gene
USRE48468E1 (en) 2007-10-26 2021-03-16 Biomarin Technologies B.V. Means and methods for counteracting muscle disorders
US8263760B2 (en) 2008-02-08 2012-09-11 Prosensa Holding Bv Methods and means for treating DNA repeat instability associated genetic disorders
US10246707B2 (en) 2008-05-14 2019-04-02 Biomarin Technologies B.V. Method for efficient exon (44) skipping in duchenne muscular dystrophy and associated means
US9139828B2 (en) 2008-05-14 2015-09-22 Prosensa Technologies B.V. Method for efficient exon (44) skipping in duchenne muscular dystrophy and associated means
US10533171B2 (en) 2009-04-24 2020-01-14 Biomarin Technologies B.V. Oligonucleotide comprising an inosine for treating DMD
US11034956B2 (en) 2009-04-24 2021-06-15 Biomarin Technologies B.V. Oligonucleotide comprising an inosine for treating DMD
US11634714B2 (en) 2009-04-24 2023-04-25 Biomarin Technologies B.V. Oligonucleotide comprising an inosine for treating DMD
US10913946B2 (en) 2012-01-27 2021-02-09 Biomarin Technologies B.V. RNA modulating oligonucleotides with improved characteristics for the treatment of Duchenne and Becker muscular dystrophy
US10179912B2 (en) 2012-01-27 2019-01-15 Biomarin Technologies B.V. RNA modulating oligonucleotides with improved characteristics for the treatment of duchenne and becker muscular dystrophy

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CN1326990A (zh) 2001-12-19
AU2001289517A1 (en) 2002-04-08

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