JP2000505306A - ２つまたはそれ以上の相互作用性（ポリ）ペプチドをコードする核酸配列の新規同定方法 - Google Patents

２つまたはそれ以上の相互作用性（ポリ）ペプチドをコードする核酸配列の新規同定方法

Info

Publication number: JP2000505306A
Authority: JP; Japan
Prior art keywords: poly; nucleic acid; peptide; vector; library
Prior art date: 1996-02-26
Legal status (The legal status is an assumption and is not a legal conclusion. Google has not performed a legal analysis and makes no representation as to the accuracy of the status listed.): Pending

Application number

JP9530595A

Other languages

English (en)

Japanese (ja)

Inventor

イラグ，ヴィック

ゲ，リミン

Current Assignee (The listed assignees may be inaccurate. Google has not performed a legal analysis and makes no representation or warranty as to the accuracy of the list.)

Morphosys AG

Original Assignee

Morphosys AG

Priority date (The priority date is an assumption and is not a legal conclusion. Google has not performed a legal analysis and makes no representation as to the accuracy of the date listed.)

1996-02-26

Filing date

1997-02-26

Publication date

2000-05-09

1997-02-26 Application filed by Morphosys AG filed Critical Morphosys AG

2000-05-09 Publication of JP2000505306A publication Critical patent/JP2000505306A/ja

Status Pending legal-status Critical Current

Links

108090000765 processed proteins & peptides Proteins 0.000 title claims abstract description 126
150000007523 nucleic acids Chemical group 0.000 title claims abstract description 107
238000000034 method Methods 0.000 title claims abstract description 98
102000004196 processed proteins & peptides Human genes 0.000 title claims abstract description 42
108090000623 proteins and genes Proteins 0.000 claims abstract description 93
239000013598 vector Substances 0.000 claims description 191
210000004027 cell Anatomy 0.000 claims description 81
230000003993 interaction Effects 0.000 claims description 48
108091028043 Nucleic acid sequence Proteins 0.000 claims description 43
208000015181 infectious disease Diseases 0.000 claims description 34
230000006798 recombination Effects 0.000 claims description 34
238000005215 recombination Methods 0.000 claims description 34
230000027455 binding Effects 0.000 claims description 31
241000588724 Escherichia coli Species 0.000 claims description 30
238000012216 screening Methods 0.000 claims description 29
230000002458 infectious effect Effects 0.000 claims description 24
229960005091 chloramphenicol Drugs 0.000 claims description 20
WIIZWVCIJKGZOK-RKDXNWHRSA-N chloramphenicol Chemical compound ClC(Cl)C(=O)N[C@H](CO)[C@H](O)C1=CC=C([N+]([O-])=O)C=C1 WIIZWVCIJKGZOK-RKDXNWHRSA-N 0.000 claims description 20
230000004927 fusion Effects 0.000 claims description 20
229960000723 ampicillin Drugs 0.000 claims description 17
AVKUERGKIZMTKX-NJBDSQKTSA-N ampicillin Chemical compound C1([C@@H](N)C(=O)N[C@H]2[C@H]3SC([C@@H](N3C2=O)C(O)=O)(C)C)=CC=CC=C1 AVKUERGKIZMTKX-NJBDSQKTSA-N 0.000 claims description 17
108020004707 nucleic acids Proteins 0.000 claims description 16
102000039446 nucleic acids Human genes 0.000 claims description 16
239000003550 marker Substances 0.000 claims description 14
238000000746 purification Methods 0.000 claims description 12
ROHFNLRQFUQHCH-YFKPBYRVSA-N L-leucine Chemical compound CC(C)C[C@H](N)C(O)=O ROHFNLRQFUQHCH-YFKPBYRVSA-N 0.000 claims description 11
230000002068 genetic effect Effects 0.000 claims description 11
239000002253 acid Substances 0.000 claims description 10
238000004519 manufacturing process Methods 0.000 claims description 10
239000002299 complementary DNA Substances 0.000 claims description 9
108010079246 OMPA outer membrane proteins Proteins 0.000 claims description 8
108020001507 fusion proteins Proteins 0.000 claims description 8
102000037865 fusion proteins Human genes 0.000 claims description 8
108091008146 restriction endonucleases Proteins 0.000 claims description 8
229930027917 kanamycin Natural products 0.000 claims description 7
229960000318 kanamycin Drugs 0.000 claims description 7
SBUJHOSQTJFQJX-NOAMYHISSA-N kanamycin Chemical compound O[C@@H]1[C@@H](O)[C@H](O)[C@@H](CN)O[C@@H]1O[C@H]1[C@H](O)[C@@H](O[C@@H]2[C@@H]([C@@H](N)[C@H](O)[C@@H](CO)O2)O)[C@H](N)C[C@@H]1N SBUJHOSQTJFQJX-NOAMYHISSA-N 0.000 claims description 7
229930182823 kanamycin A Natural products 0.000 claims description 7
241000894006 Bacteria Species 0.000 claims description 6
239000003242 anti bacterial agent Substances 0.000 claims description 6
UCSJYZPVAKXKNQ-HZYVHMACSA-N streptomycin Chemical compound CN[C@H]1[C@H](O)[C@@H](O)[C@H](CO)O[C@H]1O[C@@H]1[C@](C=O)(O)[C@H](C)O[C@H]1O[C@@H]1[C@@H](NC(N)=N)[C@H](O)[C@@H](NC(N)=N)[C@H](O)[C@H]1O UCSJYZPVAKXKNQ-HZYVHMACSA-N 0.000 claims description 6
230000003115 biocidal effect Effects 0.000 claims description 5
210000003495 flagella Anatomy 0.000 claims description 5
230000035772 mutation Effects 0.000 claims description 5
108060003951 Immunoglobulin Proteins 0.000 claims description 4
108090001030 Lipoproteins Proteins 0.000 claims description 4
102000004895 Lipoproteins Human genes 0.000 claims description 4
241000700605 Viruses Species 0.000 claims description 4
108010084455 Zeocin Proteins 0.000 claims description 4
108010005774 beta-Galactosidase Proteins 0.000 claims description 4
238000006243 chemical reaction Methods 0.000 claims description 4
102000018358 immunoglobulin Human genes 0.000 claims description 4
230000001404 mediated effect Effects 0.000 claims description 4
230000004048 modification Effects 0.000 claims description 4
238000012986 modification Methods 0.000 claims description 4
108010091748 peptide A Proteins 0.000 claims description 4
CWCMIVBLVUHDHK-ZSNHEYEWSA-N phleomycin D1 Chemical compound N([C@H](C(=O)N[C@H](C)[C@@H](O)[C@H](C)C(=O)N[C@@H]([C@H](O)C)C(=O)NCCC=1SC[C@@H](N=1)C=1SC=C(N=1)C(=O)NCCCCNC(N)=N)[C@@H](O[C@H]1[C@H]([C@@H](O)[C@H](O)[C@H](CO)O1)O[C@@H]1[C@H]([C@@H](OC(N)=O)[C@H](O)[C@@H](CO)O1)O)C=1N=CNC=1)C(=O)C1=NC([C@H](CC(N)=O)NC[C@H](N)C(N)=O)=NC(N)=C1C CWCMIVBLVUHDHK-ZSNHEYEWSA-N 0.000 claims description 4
230000001737 promoting effect Effects 0.000 claims description 4
108010052285 Membrane Proteins Proteins 0.000 claims description 3
241000588652 Neisseria gonorrhoeae Species 0.000 claims description 3
229930193140 Neomycin Natural products 0.000 claims description 3
240000004808 Saccharomyces cerevisiae Species 0.000 claims description 3
239000004098 Tetracycline Substances 0.000 claims description 3
229940088710 antibiotic agent Drugs 0.000 claims description 3
229960004927 neomycin Drugs 0.000 claims description 3
229960005322 streptomycin Drugs 0.000 claims description 3
229960002180 tetracycline Drugs 0.000 claims description 3
229930101283 tetracycline Natural products 0.000 claims description 3
235000019364 tetracycline Nutrition 0.000 claims description 3
150000003522 tetracyclines Chemical class 0.000 claims description 3
238000013518 transcription Methods 0.000 claims description 3
230000035897 transcription Effects 0.000 claims description 3
241000710929 Alphavirus Species 0.000 claims description 2
241000702374 Enterobacteria phage fd Species 0.000 claims description 2
101150009006 HIS3 gene Proteins 0.000 claims description 2
241001112471 Lambdavirus Species 0.000 claims description 2
MSFSPUZXLOGKHJ-UHFFFAOYSA-N Muraminsaeure Natural products OC(=O)C(C)OC1C(N)C(O)OC(CO)C1O MSFSPUZXLOGKHJ-UHFFFAOYSA-N 0.000 claims description 2
101150054516 PRD1 gene Proteins 0.000 claims description 2
108091005804 Peptidases Proteins 0.000 claims description 2
108010013639 Peptidoglycan Proteins 0.000 claims description 2
239000004365 Protease Substances 0.000 claims description 2
241000702227 Pseudomonas phage Pf1 Species 0.000 claims description 2
241000702212 Pseudomonas phage Pf3 Species 0.000 claims description 2
241000702263 Reovirus sp. Species 0.000 claims description 2
101100394989 Rhodopseudomonas palustris (strain ATCC BAA-98 / CGA009) hisI gene Proteins 0.000 claims description 2
101100459905 Saccharomyces cerevisiae (strain ATCC 204508 / S288c) NCP1 gene Proteins 0.000 claims description 2
108010090804 Streptavidin Proteins 0.000 claims description 2
241001091925 Xanthomonas phage Xf Species 0.000 claims description 2
238000003776 cleavage reaction Methods 0.000 claims description 2
230000013595 glycosylation Effects 0.000 claims description 2
238000006206 glycosylation reaction Methods 0.000 claims description 2
230000029226 lipidation Effects 0.000 claims description 2
230000007246 mechanism Effects 0.000 claims description 2
230000011987 methylation Effects 0.000 claims description 2
238000007069 methylation reaction Methods 0.000 claims description 2
235000016709 nutrition Nutrition 0.000 claims description 2
230000026731 phosphorylation Effects 0.000 claims description 2
238000006366 phosphorylation reaction Methods 0.000 claims description 2
230000023603 positive regulation of transcription initiation, DNA-dependent Effects 0.000 claims description 2
230000007017 scission Effects 0.000 claims description 2
241000701447 unidentified baculovirus Species 0.000 claims description 2
102000005936 beta-Galactosidase Human genes 0.000 claims 2
101100390951 Caenorhabditis elegans flp-22 gene Proteins 0.000 claims 1
102000000584 Calmodulin Human genes 0.000 claims 1
108010041952 Calmodulin Proteins 0.000 claims 1
102000035195 Peptidases Human genes 0.000 claims 1
102000004160 Phosphoric Monoester Hydrolases Human genes 0.000 claims 1
108090000608 Phosphoric Monoester Hydrolases Proteins 0.000 claims 1
102400000368 Surface protein Human genes 0.000 claims 1
241000711517 Torovirus Species 0.000 claims 1
230000000694 effects Effects 0.000 claims 1
230000006126 farnesylation Effects 0.000 claims 1
102000004169 proteins and genes Human genes 0.000 abstract description 43
235000018102 proteins Nutrition 0.000 description 42
239000012634 fragment Substances 0.000 description 34
108020004414 DNA Proteins 0.000 description 28
238000003752 polymerase chain reaction Methods 0.000 description 27
239000006137 Luria-Bertani broth Substances 0.000 description 19
230000029087 digestion Effects 0.000 description 18
239000000126 substance Substances 0.000 description 15
102100036220 PC4 and SFRS1-interacting protein Human genes 0.000 description 14
238000010361 transduction Methods 0.000 description 14
239000002245 particle Substances 0.000 description 13
239000013612 plasmid Substances 0.000 description 13
239000000047 product Substances 0.000 description 13
239000006228 supernatant Substances 0.000 description 12
238000010561 standard procedure Methods 0.000 description 11
150000001413 amino acids Chemical class 0.000 description 10
210000004899 c-terminal region Anatomy 0.000 description 10
238000002474 experimental method Methods 0.000 description 10
239000002609 medium Substances 0.000 description 10
ROHFNLRQFUQHCH-UHFFFAOYSA-N Leucine Natural products CC(C)CC(N)C(O)=O ROHFNLRQFUQHCH-UHFFFAOYSA-N 0.000 description 9
238000002823 phage display Methods 0.000 description 9
238000012163 sequencing technique Methods 0.000 description 9
238000010276 construction Methods 0.000 description 8
238000005516 engineering process Methods 0.000 description 8
238000001727 in vivo Methods 0.000 description 8
239000000725 suspension Substances 0.000 description 8
WQZGKKKJIJFFOK-GASJEMHNSA-N Glucose Natural products OC[C@H]1OC(O)[C@H](O)[C@@H](O)[C@@H]1O WQZGKKKJIJFFOK-GASJEMHNSA-N 0.000 description 7
101800003050 Interleukin-16 Proteins 0.000 description 7
102000049772 Interleukin-16 Human genes 0.000 description 7
108010025020 Nerve Growth Factor Proteins 0.000 description 7
102000015336 Nerve Growth Factor Human genes 0.000 description 7
230000003321 amplification Effects 0.000 description 7
238000004458 analytical method Methods 0.000 description 7
238000013459 approach Methods 0.000 description 7
230000015572 biosynthetic process Effects 0.000 description 7
238000010367 cloning Methods 0.000 description 7
239000008103 glucose Substances 0.000 description 7
229940053128 nerve growth factor Drugs 0.000 description 7
238000003199 nucleic acid amplification method Methods 0.000 description 7
102000001189 Cyclic Peptides Human genes 0.000 description 6
108010069514 Cyclic Peptides Proteins 0.000 description 6
241000724791 Filamentous phage Species 0.000 description 6
108010067902 Peptide Library Proteins 0.000 description 6
FAPWRFPIFSIZLT-UHFFFAOYSA-M Sodium chloride Chemical compound [Na+].[Cl-] FAPWRFPIFSIZLT-UHFFFAOYSA-M 0.000 description 6
230000003834 intracellular effect Effects 0.000 description 6
239000000203 mixture Substances 0.000 description 6
230000010076 replication Effects 0.000 description 6
102000004190 Enzymes Human genes 0.000 description 5
108090000790 Enzymes Proteins 0.000 description 5
239000000427 antigen Substances 0.000 description 5
239000000872 buffer Substances 0.000 description 5
238000005119 centrifugation Methods 0.000 description 5
239000000499 gel Substances 0.000 description 5
BPHPUYQFMNQIOC-NXRLNHOXSA-N isopropyl beta-D-thiogalactopyranoside Chemical compound CC(C)S[C@@H]1O[C@H](CO)[C@H](O)[C@H](O)[C@H]1O BPHPUYQFMNQIOC-NXRLNHOXSA-N 0.000 description 5
239000008188 pellet Substances 0.000 description 5
230000004850 protein–protein interaction Effects 0.000 description 5
101100129922 Caenorhabditis elegans pig-1 gene Proteins 0.000 description 4
101100520057 Drosophila melanogaster Pig1 gene Proteins 0.000 description 4
108091034117 Oligonucleotide Proteins 0.000 description 4
238000012408 PCR amplification Methods 0.000 description 4
108091007433 antigens Proteins 0.000 description 4
102000036639 antigens Human genes 0.000 description 4
230000001580 bacterial effect Effects 0.000 description 4
238000010168 coupling process Methods 0.000 description 4
238000001514 detection method Methods 0.000 description 4
230000009870 specific binding Effects 0.000 description 4
238000012360 testing method Methods 0.000 description 4
238000012546 transfer Methods 0.000 description 4
241001515965 unidentified phage Species 0.000 description 4
108010011170 Ala-Trp-Arg-His-Pro-Gln-Phe-Gly-Gly Proteins 0.000 description 3
101100364969 Dictyostelium discoideum scai gene Proteins 0.000 description 3
239000006142 Luria-Bertani Agar Substances 0.000 description 3
101100364971 Mus musculus Scai gene Proteins 0.000 description 3
102000002933 Thioredoxin Human genes 0.000 description 3
108091023040 Transcription factor Proteins 0.000 description 3
102000040945 Transcription factor Human genes 0.000 description 3
230000008901 benefit Effects 0.000 description 3
239000011230 binding agent Substances 0.000 description 3
238000004440 column chromatography Methods 0.000 description 3
230000008878 coupling Effects 0.000 description 3
238000005859 coupling reaction Methods 0.000 description 3
239000013604 expression vector Substances 0.000 description 3
230000006870 function Effects 0.000 description 3
239000000833 heterodimer Substances 0.000 description 3
238000002156 mixing Methods 0.000 description 3
238000002360 preparation method Methods 0.000 description 3
102000005962 receptors Human genes 0.000 description 3
108020003175 receptors Proteins 0.000 description 3
239000011780 sodium chloride Substances 0.000 description 3
108060008226 thioredoxin Proteins 0.000 description 3
229940094937 thioredoxin Drugs 0.000 description 3
230000026683 transduction Effects 0.000 description 3
102000002260 Alkaline Phosphatase Human genes 0.000 description 2
108020004774 Alkaline Phosphatase Proteins 0.000 description 2
102100026189 Beta-galactosidase Human genes 0.000 description 2
108020004705 Codon Proteins 0.000 description 2
102000053602 DNA Human genes 0.000 description 2
108010017826 DNA Polymerase I Proteins 0.000 description 2
102000004594 DNA Polymerase I Human genes 0.000 description 2
108010002231 IgA-specific serine endopeptidase Proteins 0.000 description 2
102000018697 Membrane Proteins Human genes 0.000 description 2
DYUQAZSOFZSPHD-UHFFFAOYSA-N Phenylpropanol Chemical compound CCC(O)C1=CC=CC=C1 DYUQAZSOFZSPHD-UHFFFAOYSA-N 0.000 description 2
OAICVXFJPJFONN-UHFFFAOYSA-N Phosphorus Chemical compound [P] OAICVXFJPJFONN-UHFFFAOYSA-N 0.000 description 2
108091000080 Phosphotransferase Proteins 0.000 description 2
208000035415 Reinfection Diseases 0.000 description 2
239000007984 Tris EDTA buffer Substances 0.000 description 2
239000011543 agarose gel Substances 0.000 description 2
WQZGKKKJIJFFOK-VFUOTHLCSA-N beta-D-glucose Chemical compound OC[C@H]1O[C@@H](O)[C@H](O)[C@@H](O)[C@@H]1O WQZGKKKJIJFFOK-VFUOTHLCSA-N 0.000 description 2
230000031018 biological processes and functions Effects 0.000 description 2
101150055766 cat gene Proteins 0.000 description 2
210000000078 claw Anatomy 0.000 description 2
238000007796 conventional method Methods 0.000 description 2
238000005520 cutting process Methods 0.000 description 2
238000000605 extraction Methods 0.000 description 2
238000000338 in vitro Methods 0.000 description 2
238000003780 insertion Methods 0.000 description 2
230000037431 insertion Effects 0.000 description 2
239000000463 material Substances 0.000 description 2
239000012528 membrane Substances 0.000 description 2
229910052698 phosphorus Inorganic materials 0.000 description 2
239000011574 phosphorus Substances 0.000 description 2
102000020233 phosphotransferase Human genes 0.000 description 2
239000013600 plasmid vector Substances 0.000 description 2
238000007747 plating Methods 0.000 description 2
230000008569 process Effects 0.000 description 2
238000011084 recovery Methods 0.000 description 2
239000013589 supplement Substances 0.000 description 2
238000001086 yeast two-hybrid system Methods 0.000 description 2
YRMCBQLZVBXOSJ-PCFSSPOYSA-N (e)-3-[(6r,6as)-4-hydroxy-6-methoxy-3-methyl-11-oxo-5,6,6a,7-tetrahydropyrrolo[2,1-c][1,4]benzodiazepin-8-yl]prop-2-enamide Chemical group CO[C@H]1NC2=C(O)C(C)=CC=C2C(=O)N2C=C(\C=C\C(N)=O)C[C@@H]12 YRMCBQLZVBXOSJ-PCFSSPOYSA-N 0.000 description 1
WIIZWVCIJKGZOK-IUCAKERBSA-N 2,2-dichloro-n-[(1s,2s)-1,3-dihydroxy-1-(4-nitrophenyl)propan-2-yl]acetamide Chemical compound ClC(Cl)C(=O)N[C@@H](CO)[C@@H](O)C1=CC=C([N+]([O-])=O)C=C1 WIIZWVCIJKGZOK-IUCAKERBSA-N 0.000 description 1
DLZKEQQWXODGGZ-KCJUWKMLSA-N 2-[[(2r)-2-[[(2s)-2-amino-3-(4-hydroxyphenyl)propanoyl]amino]propanoyl]amino]acetic acid Chemical compound OC(=O)CNC(=O)[C@@H](C)NC(=O)[C@@H](N)CC1=CC=C(O)C=C1 DLZKEQQWXODGGZ-KCJUWKMLSA-N 0.000 description 1
101710132601 Capsid protein Proteins 0.000 description 1
101710094648 Coat protein Proteins 0.000 description 1
108010051219 Cre recombinase Proteins 0.000 description 1
238000001712 DNA sequencing Methods 0.000 description 1
230000006820 DNA synthesis Effects 0.000 description 1
102000016928 DNA-directed DNA polymerase Human genes 0.000 description 1
108010014303 DNA-directed DNA polymerase Proteins 0.000 description 1
101100453511 Danio rerio kazna gene Proteins 0.000 description 1
108090000204 Dipeptidase 1 Proteins 0.000 description 1
241000255925 Diptera Species 0.000 description 1
102100021181 Golgi phosphoprotein 3 Human genes 0.000 description 1
HVLSXIKZNLPZJJ-TXZCQADKSA-N HA peptide Chemical compound C([C@@H](C(=O)N[C@@H](CC(O)=O)C(=O)N[C@@H](C(C)C)C(=O)N1[C@@H](CCC1)C(=O)N[C@@H](CC(O)=O)C(=O)N[C@@H](CC=1C=CC(O)=CC=1)C(=O)N[C@@H](C)C(O)=O)NC(=O)[C@H]1N(CCC1)C(=O)[C@@H](N)CC=1C=CC(O)=CC=1)C1=CC=C(O)C=C1 HVLSXIKZNLPZJJ-TXZCQADKSA-N 0.000 description 1
101710154606 Hemagglutinin Proteins 0.000 description 1
241000238631 Hexapoda Species 0.000 description 1
101000617823 Homo sapiens Solute carrier organic anion transporter family member 6A1 Proteins 0.000 description 1
101150102236 IL16 gene Proteins 0.000 description 1
235000019687 Lamb Nutrition 0.000 description 1
101710125418 Major capsid protein Proteins 0.000 description 1
108091008604 NGF receptors Proteins 0.000 description 1
101710141454 Nucleoprotein Proteins 0.000 description 1
108700026244 Open Reading Frames Proteins 0.000 description 1
101710093908 Outer capsid protein VP4 Proteins 0.000 description 1
101710135467 Outer capsid protein sigma-1 Proteins 0.000 description 1
102000004316 Oxidoreductases Human genes 0.000 description 1
108090000854 Oxidoreductases Proteins 0.000 description 1
229910019142 PO4 Inorganic materials 0.000 description 1
101710083689 Probable capsid protein Proteins 0.000 description 1
101710176177 Protein A56 Proteins 0.000 description 1
108010076504 Protein Sorting Signals Proteins 0.000 description 1
101000702488 Rattus norvegicus High affinity cationic amino acid transporter 1 Proteins 0.000 description 1
108700008625 Reporter Genes Proteins 0.000 description 1
102100037486 Reverse transcriptase/ribonuclease H Human genes 0.000 description 1
241000277331 Salmonidae Species 0.000 description 1
108020004682 Single-Stranded DNA Proteins 0.000 description 1
102100033725 Tumor necrosis factor receptor superfamily member 16 Human genes 0.000 description 1
241000607626 Vibrio cholerae Species 0.000 description 1
JLCPHMBAVCMARE-UHFFFAOYSA-N [3-[[3-[[3-[[3-[[3-[[3-[[3-[[3-[[3-[[3-[[3-[[5-(2-amino-6-oxo-1H-purin-9-yl)-3-[[3-[[3-[[3-[[3-[[3-[[5-(2-amino-6-oxo-1H-purin-9-yl)-3-[[5-(2-amino-6-oxo-1H-purin-9-yl)-3-hydroxyoxolan-2-yl]methoxy-hydroxyphosphoryl]oxyoxolan-2-yl]methoxy-hydroxyphosphoryl]oxy-5-(5-methyl-2,4-dioxopyrimidin-1-yl)oxolan-2-yl]methoxy-hydroxyphosphoryl]oxy-5-(6-aminopurin-9-yl)oxolan-2-yl]methoxy-hydroxyphosphoryl]oxy-5-(6-aminopurin-9-yl)oxolan-2-yl]methoxy-hydroxyphosphoryl]oxy-5-(6-aminopurin-9-yl)oxolan-2-yl]methoxy-hydroxyphosphoryl]oxy-5-(6-aminopurin-9-yl)oxolan-2-yl]methoxy-hydroxyphosphoryl]oxyoxolan-2-yl]methoxy-hydroxyphosphoryl]oxy-5-(5-methyl-2,4-dioxopyrimidin-1-yl)oxolan-2-yl]methoxy-hydroxyphosphoryl]oxy-5-(4-amino-2-oxopyrimidin-1-yl)oxolan-2-yl]methoxy-hydroxyphosphoryl]oxy-5-(5-methyl-2,4-dioxopyrimidin-1-yl)oxolan-2-yl]methoxy-hydroxyphosphoryl]oxy-5-(5-methyl-2,4-dioxopyrimidin-1-yl)oxolan-2-yl]methoxy-hydroxyphosphoryl]oxy-5-(6-aminopurin-9-yl)oxolan-2-yl]methoxy-hydroxyphosphoryl]oxy-5-(6-aminopurin-9-yl)oxolan-2-yl]methoxy-hydroxyphosphoryl]oxy-5-(4-amino-2-oxopyrimidin-1-yl)oxolan-2-yl]methoxy-hydroxyphosphoryl]oxy-5-(4-amino-2-oxopyrimidin-1-yl)oxolan-2-yl]methoxy-hydroxyphosphoryl]oxy-5-(4-amino-2-oxopyrimidin-1-yl)oxolan-2-yl]methoxy-hydroxyphosphoryl]oxy-5-(6-aminopurin-9-yl)oxolan-2-yl]methoxy-hydroxyphosphoryl]oxy-5-(4-amino-2-oxopyrimidin-1-yl)oxolan-2-yl]methyl [5-(6-aminopurin-9-yl)-2-(hydroxymethyl)oxolan-3-yl] hydrogen phosphate Polymers Cc1cn(C2CC(OP(O)(=O)OCC3OC(CC3OP(O)(=O)OCC3OC(CC3O)n3cnc4c3nc(N)[nH]c4=O)n3cnc4c3nc(N)[nH]c4=O)C(COP(O)(=O)OC3CC(OC3COP(O)(=O)OC3CC(OC3COP(O)(=O)OC3CC(OC3COP(O)(=O)OC3CC(OC3COP(O)(=O)OC3CC(OC3COP(O)(=O)OC3CC(OC3COP(O)(=O)OC3CC(OC3COP(O)(=O)OC3CC(OC3COP(O)(=O)OC3CC(OC3COP(O)(=O)OC3CC(OC3COP(O)(=O)OC3CC(OC3COP(O)(=O)OC3CC(OC3COP(O)(=O)OC3CC(OC3COP(O)(=O)OC3CC(OC3COP(O)(=O)OC3CC(OC3COP(O)(=O)OC3CC(OC3COP(O)(=O)OC3CC(OC3CO)n3cnc4c(N)ncnc34)n3ccc(N)nc3=O)n3cnc4c(N)ncnc34)n3ccc(N)nc3=O)n3ccc(N)nc3=O)n3ccc(N)nc3=O)n3cnc4c(N)ncnc34)n3cnc4c(N)ncnc34)n3cc(C)c(=O)[nH]c3=O)n3cc(C)c(=O)[nH]c3=O)n3ccc(N)nc3=O)n3cc(C)c(=O)[nH]c3=O)n3cnc4c3nc(N)[nH]c4=O)n3cnc4c(N)ncnc34)n3cnc4c(N)ncnc34)n3cnc4c(N)ncnc34)n3cnc4c(N)ncnc34)O2)c(=O)[nH]c1=O JLCPHMBAVCMARE-UHFFFAOYSA-N 0.000 description 1
101150063325 ab gene Proteins 0.000 description 1
230000004308 accommodation Effects 0.000 description 1
150000007513 acids Chemical class 0.000 description 1
230000009471 action Effects 0.000 description 1
238000001042 affinity chromatography Methods 0.000 description 1
238000000246 agarose gel electrophoresis Methods 0.000 description 1
238000000137 annealing Methods 0.000 description 1
238000007845 assembly PCR Methods 0.000 description 1
230000000468 autoproteolytic effect Effects 0.000 description 1
102000006635 beta-lactamase Human genes 0.000 description 1
239000008280 blood Substances 0.000 description 1
210000004369 blood Anatomy 0.000 description 1
238000004113 cell culture Methods 0.000 description 1
238000004140 cleaning Methods 0.000 description 1
230000000295 complement effect Effects 0.000 description 1
238000004132 cross linking Methods 0.000 description 1
125000004122 cyclic group Chemical group 0.000 description 1
238000013461 design Methods 0.000 description 1
238000011161 development Methods 0.000 description 1
238000009826 distribution Methods 0.000 description 1
239000003814 drug Substances 0.000 description 1
238000004520 electroporation Methods 0.000 description 1
238000011049 filling Methods 0.000 description 1
239000000706 filtrate Substances 0.000 description 1
238000001943 fluorescence-activated cell sorting Methods 0.000 description 1
150000004676 glycans Chemical class 0.000 description 1
239000000185 hemagglutinin Substances 0.000 description 1
230000001939 inductive effect Effects 0.000 description 1
230000010354 integration Effects 0.000 description 1
238000002955 isolation Methods 0.000 description 1
238000004898 kneading Methods 0.000 description 1
210000003127 knee Anatomy 0.000 description 1
239000003446 ligand Substances 0.000 description 1
230000033001 locomotion Effects 0.000 description 1
210000004962 mammalian cell Anatomy 0.000 description 1
238000004949 mass spectrometry Methods 0.000 description 1
230000002906 microbiologic effect Effects 0.000 description 1
238000010369 molecular cloning Methods 0.000 description 1
230000000877 morphologic effect Effects 0.000 description 1
239000013642 negative control Substances 0.000 description 1
235000015097 nutrients Nutrition 0.000 description 1
230000035764 nutrition Effects 0.000 description 1
238000004806 packaging method and process Methods 0.000 description 1
235000021317 phosphate Nutrition 0.000 description 1
150000003013 phosphoric acid derivatives Chemical class 0.000 description 1
229920001184 polypeptide Polymers 0.000 description 1
239000002244 precipitate Substances 0.000 description 1
238000001556 precipitation Methods 0.000 description 1
239000002243 precursor Substances 0.000 description 1
235000004252 protein component Nutrition 0.000 description 1
238000002005 protein protein interaction detection Methods 0.000 description 1
230000003362 replicative effect Effects 0.000 description 1
238000011160 research Methods 0.000 description 1
239000004576 sand Substances 0.000 description 1
238000010187 selection method Methods 0.000 description 1
230000035945 sensitivity Effects 0.000 description 1
238000013207 serial dilution Methods 0.000 description 1
239000000243 solution Substances 0.000 description 1
238000000638 solvent extraction Methods 0.000 description 1
230000003068 static effect Effects 0.000 description 1
230000001629 suppression Effects 0.000 description 1
238000007862 touchdown PCR Methods 0.000 description 1
238000011144 upstream manufacturing Methods 0.000 description 1

Classifications

- C—CHEMISTRY; METALLURGY
- C40—COMBINATORIAL TECHNOLOGY
- C40B—COMBINATORIAL CHEMISTRY; LIBRARIES, e.g. CHEMICAL LIBRARIES
- C40B40/00—Libraries per se, e.g. arrays, mixtures
- C40B40/02—Libraries contained in or displayed by microorganisms, e.g. bacteria or animal cells; Libraries contained in or displayed by vectors, e.g. plasmids; Libraries containing only microorganisms or vectors
- C—CHEMISTRY; METALLURGY
- C12—BIOCHEMISTRY; BEER; SPIRITS; WINE; VINEGAR; MICROBIOLOGY; ENZYMOLOGY; MUTATION OR GENETIC ENGINEERING
- C12N—MICROORGANISMS OR ENZYMES; COMPOSITIONS THEREOF; PROPAGATING, PRESERVING, OR MAINTAINING MICROORGANISMS; MUTATION OR GENETIC ENGINEERING; CULTURE MEDIA
- C12N15/00—Mutation or genetic engineering; DNA or RNA concerning genetic engineering, vectors, e.g. plasmids, or their isolation, preparation or purification; Use of hosts therefor
- C12N15/09—Recombinant DNA-technology
- C12N15/10—Processes for the isolation, preparation or purification of DNA or RNA
- C12N15/1034—Isolating an individual clone by screening libraries
- C12N15/1037—Screening libraries presented on the surface of microorganisms, e.g. phage display, E. coli display
- C—CHEMISTRY; METALLURGY
- C12—BIOCHEMISTRY; BEER; SPIRITS; WINE; VINEGAR; MICROBIOLOGY; ENZYMOLOGY; MUTATION OR GENETIC ENGINEERING
- C12N—MICROORGANISMS OR ENZYMES; COMPOSITIONS THEREOF; PROPAGATING, PRESERVING, OR MAINTAINING MICROORGANISMS; MUTATION OR GENETIC ENGINEERING; CULTURE MEDIA
- C12N15/00—Mutation or genetic engineering; DNA or RNA concerning genetic engineering, vectors, e.g. plasmids, or their isolation, preparation or purification; Use of hosts therefor
- C12N15/09—Recombinant DNA-technology
- C12N15/10—Processes for the isolation, preparation or purification of DNA or RNA
- C12N15/1034—Isolating an individual clone by screening libraries
- C12N15/1055—Protein x Protein interaction, e.g. two hybrid selection

Landscapes

Life Sciences & Earth Sciences (AREA)
Chemical & Material Sciences (AREA)
Health & Medical Sciences (AREA)
Organic Chemistry (AREA)
Engineering & Computer Science (AREA)
Genetics & Genomics (AREA)
Zoology (AREA)
Wood Science & Technology (AREA)
Biomedical Technology (AREA)
Bioinformatics & Cheminformatics (AREA)
Biotechnology (AREA)
General Engineering & Computer Science (AREA)
Molecular Biology (AREA)
Microbiology (AREA)
Biochemistry (AREA)
General Health & Medical Sciences (AREA)
Physics & Mathematics (AREA)
Crystallography & Structural Chemistry (AREA)
Biophysics (AREA)
Plant Pathology (AREA)
Virology (AREA)
Chemical Kinetics & Catalysis (AREA)
General Chemical & Material Sciences (AREA)
Medicinal Chemistry (AREA)
Bioinformatics & Computational Biology (AREA)
Measuring Or Testing Involving Enzymes Or Micro-Organisms (AREA)

JP9530595A 1996-02-26 1997-02-26 ２つまたはそれ以上の相互作用性（ポリ）ペプチドをコードする核酸配列の新規同定方法 Pending JP2000505306A (ja)

Applications Claiming Priority (3)

Application Number	Priority Date	Filing Date	Title
EP96102852.9		1996-02-26
EP96102852		1996-02-26
PCT/EP1997/000931 WO1997032017A1 (fr)	1996-02-26	1997-02-26	Nouvelle methode pour l'identification de sequences d'acides nucleiques codant pour deux (poly)peptides interactifs, ou plus

Publications (1)

Publication Number	Publication Date
JP2000505306A true JP2000505306A (ja)	2000-05-09

Family

ID=8222506

Family Applications (1)

Application Number	Title	Priority Date	Filing Date
JP9530595A Pending JP2000505306A (ja)	1996-02-26	1997-02-26	２つまたはそれ以上の相互作用性（ポリ）ペプチドをコードする核酸配列の新規同定方法

Country Status (3)

Country	Link
EP (1)	EP0883686A1 (fr)
JP (1)	JP2000505306A (fr)
WO (1)	WO1997032017A1 (fr)

Cited By (1)

* Cited by examiner, † Cited by third party
Publication number	Priority date	Publication date	Assignee	Title
JP2007501007A (ja) *	2003-08-06	2007-01-25	リナネッツヴェルクエルエヌアー−テクノローギエンゲゼルシャフトミットベグレンツターハフトゥング	無細胞タンパク質生合成用溶解物の産生法

Families Citing this family (38)

* Cited by examiner, † Cited by third party
Publication number	Priority date	Publication date	Assignee	Title
EP0866805A1 (fr)	1995-12-12	1998-09-30	Karolinska Innovations AB	PEPTIDE FIXANT LA SEQUENCE KLVFF DE L'AMYLOIDE $g(b)
CA2297070A1 (fr)	1997-08-01	1999-02-11	Morphosys Ag	Nouvelle methode et nouveau phage d'identification d'une sequence d'acide nucleique
US6913745B1 (en)	1997-12-02	2005-07-05	Neuralab Limited	Passive immunization of Alzheimer's disease
US7588766B1 (en)	2000-05-26	2009-09-15	Elan Pharma International Limited	Treatment of amyloidogenic disease
US20080050367A1 (en)	1998-04-07	2008-02-28	Guriq Basi	Humanized antibodies that recognize beta amyloid peptide
US7964192B1 (en)	1997-12-02	2011-06-21	Janssen Alzheimer Immunotherapy	Prevention and treatment of amyloidgenic disease
US6905686B1 (en)	1997-12-02	2005-06-14	Neuralab Limited	Active immunization for treatment of alzheimer's disease
US7790856B2 (en)	1998-04-07	2010-09-07	Janssen Alzheimer Immunotherapy	Humanized antibodies that recognize beta amyloid peptide
US6761888B1 (en)	2000-05-26	2004-07-13	Neuralab Limited	Passive immunization treatment of Alzheimer's disease
US7179892B2 (en)	2000-12-06	2007-02-20	Neuralab Limited	Humanized antibodies that recognize beta amyloid peptide
TWI239847B (en)	1997-12-02	2005-09-21	Elan Pharm Inc	N-terminal fragment of Abeta peptide and an adjuvant for preventing and treating amyloidogenic disease
ATE282717T1 (de) *	1998-04-30	2004-12-15	Max Planck Gesellschaft	Neuartiges verfahren zur identifizierung von klonen mit einer gewünschten biologischen eigenschaft, ausgehend von einer expressionsgenbank
US7060670B1 (en)	1999-05-05	2006-06-13	Neurochem (International) Limited	Stereoselective antifibrillogenic peptides and peptidomimetics thereof
WO2001042454A2 (fr) *	1999-12-09	2001-06-14	Select Therapeutics Inc.	Procedes de detection des interactions de composes par l'expression phagique
EP1252319A2 (fr) *	2000-02-03	2002-10-30	Domantis Limited	Domaine de prot ines combinatoire
EP1612221A3 (fr)	2000-05-22	2008-07-23	Vlaams Interuniversitair Instituut voor Biotechnologie vzw.	Piège à interaction basé sur un récepteur
WO2002012277A2 (fr) *	2000-08-07	2002-02-14	Domantis Limited	Nouvelles proteines
US6830885B1 (en)	2000-08-18	2004-12-14	Phenogene Therapeutiques Inc.	Nucleic acid molecule, method and kit for selecting a nucleic acid having a desired feature
PE20020574A1 (es)	2000-12-06	2002-07-02	Wyeth Corp	Anticuerpos humanizados que reconocen el peptido amiloideo beta
US7700751B2 (en)	2000-12-06	2010-04-20	Janssen Alzheimer Immunotherapy	Humanized antibodies that recognize β-amyloid peptide
WO2003004643A2 (fr)	2001-07-03	2003-01-16	Vlaams Interuniversitair Instituut Voor Biotechnologie Vzw	Piege a interaction proteine-proteine de mammifere inverse
US7175983B2 (en) *	2001-11-02	2007-02-13	Abmaxis, Inc.	Adapter-directed display systems
MY139983A (en)	2002-03-12	2009-11-30	Janssen Alzheimer Immunotherap	Humanized antibodies that recognize beta amyloid peptide
DE10256669B4 (de) *	2002-12-04	2006-03-09	Universitätsklinikum Charité an der Humboldt-Universität zu Berlin Technologietransferstelle	Gemisch mindestens zweier Fusionsproteine sowie ihre Herstellung und Verwendung
TWI306458B (en)	2003-05-30	2009-02-21	Elan Pharma Int Ltd	Humanized antibodies that recognize beta amyloid peptide
US20040248323A1 (en)	2003-06-09	2004-12-09	Protometrix, Inc.	Methods for conducting assays for enzyme activity on protein microarrays
TW200636066A (en)	2004-12-15	2006-10-16	Elan Pharm Inc	Humanized antibodies that recognize beta amyloid peptide
AR052051A1 (es)	2004-12-15	2007-02-28	Neuralab Ltd	Anticuerpos ab humanizados usados en mejorar la cognicion
US8784810B2 (en)	2006-04-18	2014-07-22	Janssen Alzheimer Immunotherapy	Treatment of amyloidogenic diseases
WO2009017467A1 (fr)	2007-07-27	2009-02-05	Elan Pharma International Limited	Traitement de maladies amyloïdogéniques
US8003097B2 (en)	2007-04-18	2011-08-23	Janssen Alzheimer Immunotherapy	Treatment of cerebral amyloid angiopathy
JO3076B1 (ar)	2007-10-17	2017-03-15	Janssen Alzheimer Immunotherap	نظم العلاج المناعي المعتمد على حالة apoe
US8637435B2 (en)	2007-11-16	2014-01-28	Merck Sharp & Dohme Corp.	Eukaryotic cell display systems
US9067981B1 (en)	2008-10-30	2015-06-30	Janssen Sciences Ireland Uc	Hybrid amyloid-beta antibodies
GB201103453D0 (en)	2011-03-01	2011-04-13	Vib Vzw	Kinase substrate sensor
CA2866097C (fr)	2012-03-06	2021-02-02	Vib Vzw	Proteine de fusion transmembranaire-kinase et les utilisations de celle-ci
WO2013174999A1 (fr)	2012-05-24	2013-11-28	Vib Vzw	Particule de type viral sur la base d'une interaction protéine-protéine
GB201504859D0 (en)	2015-03-23	2015-05-06	Vib Vzw	Viral particle based small molecule-protein interaction trap

Family Cites Families (4)

* Cited by examiner, † Cited by third party
Publication number	Priority date	Publication date	Assignee	Title
DE4122598C1 (fr) *	1991-07-08	1992-07-30	Deutsches Krebsforschungszentrum Stiftung Des Oeffentlichen Rechts, 6900 Heidelberg, De
WO1993019172A1 (fr) *	1992-03-24	1993-09-30	Cambridge Antibody Technology Limited	Procedes de production d'elements de paires de liaison specifiques
EP0614989A1 (fr) *	1993-02-17	1994-09-14	MorphoSys AG	Procédé de sélection in vivo des protéines attachées des ligands
SE9503151D0 (sv) *	1995-09-13	1995-09-13	Bioinvent Internatioal Ab	Combined ligand and receptor display

1997
- 1997-02-26 JP JP9530595A patent/JP2000505306A/ja active Pending
- 1997-02-26 WO PCT/EP1997/000931 patent/WO1997032017A1/fr not_active Application Discontinuation
- 1997-02-26 EP EP97905095A patent/EP0883686A1/fr not_active Withdrawn

Cited By (2)

* Cited by examiner, † Cited by third party
Publication number	Priority date	Publication date	Assignee	Title
JP2007501007A (ja) *	2003-08-06	2007-01-25	リナネッツヴェルクエルエヌアー−テクノローギエンゲゼルシャフトミットベグレンツターハフトゥング	無細胞タンパク質生合成用溶解物の産生法
JP4850064B2 (ja) *	2003-08-06	2012-01-11	キアゲンゲーエムベーハー	無細胞タンパク質生合成用溶解物の産生法

Also Published As

Publication number	Publication date
WO1997032017A1 (fr)	1997-09-04
EP0883686A1 (fr)	1998-12-16

Publication	Publication Date	Title
JP2000505306A (ja)	2000-05-09	２つまたはそれ以上の相互作用性（ポリ）ペプチドをコードする核酸配列の新規同定方法
Jaroszewicz et al.	2022	Phage display and other peptide display technologies
US11078479B2 (en)	2021-08-03	Polypeptide display libraries and methods of making and using thereof
Kay et al.	1996	Phage display of peptides and proteins: a laboratory manual
Hufton et al.	1999	Phage display of cDNA repertoires: the pVI display system and its applications for the selection of immunogenic ligands
Krebber et al.	1997	Selectively-infective phage (SIP): a mechanistic dissection of a novel in vivo selection for protein-ligand interactions
Crameri et al.	1993	Display of biologically active proteins on the surface of filamentous phages: a cDNA cloning system for selection of functional gene products linked to the genetic information responsible for their production
US5844076A (en)	1998-12-01	Totally synthetic affinity reagents
US7049135B2 (en)	2006-05-23	Method and phage for the identification of nucleic acid sequences encoding members of a multimeric (poly)peptide complex
JPH0739381A (ja)	1995-02-10	リガンド結合性タンパク質の生体内選別のための方法
EP0575410B1 (fr)	1999-05-19	Selection de proteins specifiques par une methode biologique
Crameri	2023	pJuFo: a phage surface display system for cloning genes based on protein-ligand interaction
Mersich et al.	2008	Generation of bioactive peptides by biological libraries
Petrenko et al.	2005	Vectors and modes of display
Dani	2001	Biological libraries
EP1817591A2 (fr)	2007-08-15	Procedes et compositions pour la detection ex vivo a haut rendement d'interactions proteines/proteines
CA2244838A1 (fr)	1997-09-04	Nouvelle methode pour l'identification de sequences d'acides nucleiques codant pour deux (poly)peptides interactifs, ou plus
Brown	2004	Genetic approaches to programmed assembly
Ku	1995	A combinatorial approach towards molecular recognition
Miertus et al.	2005	Biological Libraries Maria Dani
Dani	2005	16 Biological Libraries