ES2450998T3 - Nuevas variantes de proteína de cubierta E1 de rubéola y su utilización en la detección de anticuerpos anti-rubéola - Google Patents
Nuevas variantes de proteína de cubierta E1 de rubéola y su utilización en la detección de anticuerpos anti-rubéolaInfo
- Publication number
- ES2450998T3 ES2450998T3 ES08860033.3T ES08860033T ES2450998T3 ES 2450998 T3 ES2450998 T3 ES 2450998T3 ES 08860033 T ES08860033 T ES 08860033T ES 2450998 T3 ES2450998 T3 ES 2450998T3
- Authority
- ES
- Spain
- Prior art keywords
- rubella
- antigen
- disulfide
- protein
- chaperone
- Prior art date
- 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.)
- Active
Links
- 201000005404 rubella Diseases 0.000 title claims abstract description 297
- 238000001514 detection method Methods 0.000 title claims description 55
- PCDQPRRSZKQHHS-XVFCMESISA-N CTP Chemical compound O=C1N=C(N)C=CN1[C@H]1[C@H](O)[C@H](O)[C@@H](COP(O)(=O)OP(O)(=O)OP(O)(O)=O)O1 PCDQPRRSZKQHHS-XVFCMESISA-N 0.000 title description 2
- 239000000427 antigen Substances 0.000 claims abstract description 289
- 102000036639 antigens Human genes 0.000 claims abstract description 286
- 108091007433 antigens Proteins 0.000 claims abstract description 277
- 150000001413 amino acids Chemical class 0.000 claims abstract description 53
- 108010006519 Molecular Chaperones Proteins 0.000 claims description 93
- 102000037865 fusion proteins Human genes 0.000 claims description 55
- 108020001507 fusion proteins Proteins 0.000 claims description 55
- 238000000034 method Methods 0.000 claims description 29
- 230000014509 gene expression Effects 0.000 claims description 24
- 108020004511 Recombinant DNA Proteins 0.000 claims description 23
- 102000053602 DNA Human genes 0.000 claims description 21
- 239000000203 mixture Substances 0.000 claims description 18
- 102000009658 Peptidylprolyl Isomerase Human genes 0.000 claims description 17
- 108010020062 Peptidylprolyl Isomerase Proteins 0.000 claims description 17
- 238000004519 manufacturing process Methods 0.000 claims description 14
- 230000036046 immunoreaction Effects 0.000 claims description 13
- 239000002773 nucleotide Substances 0.000 claims description 12
- 125000003729 nucleotide group Chemical group 0.000 claims description 12
- 239000003153 chemical reaction reagent Substances 0.000 claims description 10
- 239000013604 expression vector Substances 0.000 claims description 10
- 210000001124 body fluid Anatomy 0.000 claims description 8
- 239000010839 body fluid Substances 0.000 claims description 8
- 238000011144 upstream manufacturing Methods 0.000 claims description 8
- 238000000746 purification Methods 0.000 claims description 6
- 102000007056 Recombinant Fusion Proteins Human genes 0.000 claims description 2
- 108010008281 Recombinant Fusion Proteins Proteins 0.000 claims description 2
- 238000012258 culturing Methods 0.000 claims description 2
- 238000002156 mixing Methods 0.000 claims description 2
- 108090000623 proteins and genes Proteins 0.000 description 81
- 102000004169 proteins and genes Human genes 0.000 description 73
- 235000018102 proteins Nutrition 0.000 description 62
- 235000001014 amino acid Nutrition 0.000 description 52
- 229940024606 amino acid Drugs 0.000 description 50
- 239000012634 fragment Substances 0.000 description 39
- 238000003018 immunoassay Methods 0.000 description 37
- 108090000765 processed proteins & peptides Proteins 0.000 description 33
- 102000005431 Molecular Chaperones Human genes 0.000 description 31
- 210000004027 cell Anatomy 0.000 description 29
- 102000004196 processed proteins & peptides Human genes 0.000 description 27
- 229920001184 polypeptide Polymers 0.000 description 24
- 230000027455 binding Effects 0.000 description 23
- 230000004927 fusion Effects 0.000 description 23
- 239000007790 solid phase Substances 0.000 description 23
- 102000018679 Tacrolimus Binding Proteins Human genes 0.000 description 22
- 108010027179 Tacrolimus Binding Proteins Proteins 0.000 description 22
- 125000000151 cysteine group Chemical group N[C@@H](CS)C(=O)* 0.000 description 22
- 239000000523 sample Substances 0.000 description 20
- 150000002019 disulfides Chemical class 0.000 description 17
- BWGNESOTFCXPMA-UHFFFAOYSA-N Dihydrogen disulfide Chemical compound SS BWGNESOTFCXPMA-UHFFFAOYSA-N 0.000 description 16
- 101710185720 Putative ethidium bromide resistance protein Proteins 0.000 description 16
- 238000003556 assay Methods 0.000 description 16
- YBJHBAHKTGYVGT-ZKWXMUAHSA-N (+)-Biotin Chemical compound N1C(=O)N[C@@H]2[C@H](CCCCC(=O)O)SC[C@@H]21 YBJHBAHKTGYVGT-ZKWXMUAHSA-N 0.000 description 14
- 108060003951 Immunoglobulin Proteins 0.000 description 14
- 210000004899 c-terminal region Anatomy 0.000 description 14
- 102000018358 immunoglobulin Human genes 0.000 description 14
- 230000001900 immune effect Effects 0.000 description 13
- 230000000890 antigenic effect Effects 0.000 description 12
- 239000000543 intermediate Substances 0.000 description 12
- 125000000539 amino acid group Chemical group 0.000 description 11
- 235000018417 cysteine Nutrition 0.000 description 11
- 230000006870 function Effects 0.000 description 11
- 230000001965 increasing effect Effects 0.000 description 11
- 238000012360 testing method Methods 0.000 description 11
- 108020004414 DNA Proteins 0.000 description 10
- 125000003295 alanine group Chemical group N[C@@H](C)C(=O)* 0.000 description 10
- 230000015572 biosynthetic process Effects 0.000 description 10
- 241000588724 Escherichia coli Species 0.000 description 9
- 108091028043 Nucleic acid sequence Proteins 0.000 description 9
- FAPWRFPIFSIZLT-UHFFFAOYSA-M Sodium chloride Chemical compound [Na+].[Cl-] FAPWRFPIFSIZLT-UHFFFAOYSA-M 0.000 description 9
- 125000003275 alpha amino acid group Chemical group 0.000 description 9
- 239000000872 buffer Substances 0.000 description 9
- RAXXELZNTBOGNW-UHFFFAOYSA-N imidazole Natural products C1=CNC=N1 RAXXELZNTBOGNW-UHFFFAOYSA-N 0.000 description 9
- 229940072221 immunoglobulins Drugs 0.000 description 9
- 230000035772 mutation Effects 0.000 description 9
- 230000009257 reactivity Effects 0.000 description 9
- 230000002776 aggregation Effects 0.000 description 8
- 238000004220 aggregation Methods 0.000 description 8
- 239000003550 marker Substances 0.000 description 8
- 230000001590 oxidative effect Effects 0.000 description 8
- 239000000126 substance Substances 0.000 description 8
- 108091026890 Coding region Proteins 0.000 description 7
- 235000020958 biotin Nutrition 0.000 description 7
- 229960002685 biotin Drugs 0.000 description 7
- 239000011616 biotin Substances 0.000 description 7
- 150000001945 cysteines Chemical class 0.000 description 7
- 210000003000 inclusion body Anatomy 0.000 description 7
- 210000002966 serum Anatomy 0.000 description 7
- 108010070675 Glutathione transferase Proteins 0.000 description 6
- 102100029100 Hematopoietic prostaglandin D synthase Human genes 0.000 description 6
- 241000710799 Rubella virus Species 0.000 description 6
- 238000013461 design Methods 0.000 description 6
- 238000002372 labelling Methods 0.000 description 6
- 239000011159 matrix material Substances 0.000 description 6
- 238000005259 measurement Methods 0.000 description 6
- 150000007523 nucleic acids Chemical group 0.000 description 6
- 102000040430 polynucleotide Human genes 0.000 description 6
- 108091033319 polynucleotide Proteins 0.000 description 6
- 239000002157 polynucleotide Substances 0.000 description 6
- 230000011664 signaling Effects 0.000 description 6
- 241000894007 species Species 0.000 description 6
- 239000013598 vector Substances 0.000 description 6
- 241000894006 Bacteria Species 0.000 description 5
- 241000710779 Trina Species 0.000 description 5
- 239000012491 analyte Substances 0.000 description 5
- 238000002820 assay format Methods 0.000 description 5
- 239000003795 chemical substances by application Substances 0.000 description 5
- 238000000338 in vitro Methods 0.000 description 5
- 239000013642 negative control Substances 0.000 description 5
- 230000002285 radioactive effect Effects 0.000 description 5
- 229910052707 ruthenium Inorganic materials 0.000 description 5
- 239000011780 sodium chloride Substances 0.000 description 5
- 239000001488 sodium phosphate Substances 0.000 description 5
- 229910000162 sodium phosphate Inorganic materials 0.000 description 5
- RYFMWSXOAZQYPI-UHFFFAOYSA-K trisodium phosphate Chemical compound [Na+].[Na+].[Na+].[O-]P([O-])([O-])=O RYFMWSXOAZQYPI-UHFFFAOYSA-K 0.000 description 5
- 229960005486 vaccine Drugs 0.000 description 5
- 102000004190 Enzymes Human genes 0.000 description 4
- 108090000790 Enzymes Proteins 0.000 description 4
- 241000206602 Eukaryota Species 0.000 description 4
- 240000004808 Saccharomyces cerevisiae Species 0.000 description 4
- 235000014680 Saccharomyces cerevisiae Nutrition 0.000 description 4
- 101710154918 Trigger factor Proteins 0.000 description 4
- 239000000654 additive Substances 0.000 description 4
- 235000004279 alanine Nutrition 0.000 description 4
- 238000004458 analytical method Methods 0.000 description 4
- 230000001580 bacterial effect Effects 0.000 description 4
- 239000003054 catalyst Substances 0.000 description 4
- XUJNEKJLAYXESH-UHFFFAOYSA-N cysteine Natural products SCC(N)C(O)=O XUJNEKJLAYXESH-UHFFFAOYSA-N 0.000 description 4
- 230000001086 cytosolic effect Effects 0.000 description 4
- 239000012636 effector Substances 0.000 description 4
- 229940088598 enzyme Drugs 0.000 description 4
- 238000011156 evaluation Methods 0.000 description 4
- 102000039446 nucleic acids Human genes 0.000 description 4
- 108020004707 nucleic acids Proteins 0.000 description 4
- 239000013612 plasmid Substances 0.000 description 4
- BASFCYQUMIYNBI-UHFFFAOYSA-N platinum Chemical compound [Pt] BASFCYQUMIYNBI-UHFFFAOYSA-N 0.000 description 4
- 239000000047 product Substances 0.000 description 4
- 230000006337 proteolytic cleavage Effects 0.000 description 4
- 230000008521 reorganization Effects 0.000 description 4
- MTCFGRXMJLQNBG-REOHCLBHSA-N (2S)-2-Amino-3-hydroxypropansäure Chemical group OC[C@H](N)C(O)=O MTCFGRXMJLQNBG-REOHCLBHSA-N 0.000 description 3
- ADHAUWMNDHMUMH-UHFFFAOYSA-L 2-[bis(carboxylatomethyl)amino]acetate;hydron;nickel(2+) Chemical compound [Ni+2].OC(=O)CN(CC([O-])=O)CC([O-])=O ADHAUWMNDHMUMH-UHFFFAOYSA-L 0.000 description 3
- 102100027723 Endogenous retrovirus group K member 6 Rec protein Human genes 0.000 description 3
- 101710091045 Envelope protein Proteins 0.000 description 3
- LFQSCWFLJHTTHZ-UHFFFAOYSA-N Ethanol Chemical compound CCO LFQSCWFLJHTTHZ-UHFFFAOYSA-N 0.000 description 3
- PEDCQBHIVMGVHV-UHFFFAOYSA-N Glycerine Chemical compound OCC(O)CO PEDCQBHIVMGVHV-UHFFFAOYSA-N 0.000 description 3
- QNAYBMKLOCPYGJ-REOHCLBHSA-N L-alanine Chemical compound C[C@H](N)C(O)=O QNAYBMKLOCPYGJ-REOHCLBHSA-N 0.000 description 3
- KDXKERNSBIXSRK-YFKPBYRVSA-N L-lysine Chemical compound NCCCC[C@H](N)C(O)=O KDXKERNSBIXSRK-YFKPBYRVSA-N 0.000 description 3
- -1 N-hydroxy succinimide activated biotin Chemical class 0.000 description 3
- 102000001708 Protein Isoforms Human genes 0.000 description 3
- 108010029485 Protein Isoforms Proteins 0.000 description 3
- 101710188315 Protein X Proteins 0.000 description 3
- KJTLSVCANCCWHF-UHFFFAOYSA-N Ruthenium Chemical compound [Ru] KJTLSVCANCCWHF-UHFFFAOYSA-N 0.000 description 3
- MTCFGRXMJLQNBG-UHFFFAOYSA-N Serine Chemical group OCC(N)C(O)=O MTCFGRXMJLQNBG-UHFFFAOYSA-N 0.000 description 3
- 108010090804 Streptavidin Proteins 0.000 description 3
- 239000012505 Superdex™ Substances 0.000 description 3
- PZBFGYYEXUXCOF-UHFFFAOYSA-N TCEP Chemical compound OC(=O)CCP(CCC(O)=O)CCC(O)=O PZBFGYYEXUXCOF-UHFFFAOYSA-N 0.000 description 3
- 241000700605 Viruses Species 0.000 description 3
- 239000004480 active ingredient Substances 0.000 description 3
- 230000003197 catalytic effect Effects 0.000 description 3
- 238000006243 chemical reaction Methods 0.000 description 3
- 238000010367 cloning Methods 0.000 description 3
- 239000011248 coating agent Substances 0.000 description 3
- 238000000576 coating method Methods 0.000 description 3
- 238000010276 construction Methods 0.000 description 3
- 238000005859 coupling reaction Methods 0.000 description 3
- 210000000172 cytosol Anatomy 0.000 description 3
- 239000003599 detergent Substances 0.000 description 3
- 239000012139 lysis buffer Substances 0.000 description 3
- 230000009871 nonspecific binding Effects 0.000 description 3
- 238000012261 overproduction Methods 0.000 description 3
- 239000002243 precursor Substances 0.000 description 3
- 230000008569 process Effects 0.000 description 3
- 239000000243 solution Substances 0.000 description 3
- 230000009870 specific binding Effects 0.000 description 3
- 238000003786 synthesis reaction Methods 0.000 description 3
- 150000003573 thiols Chemical class 0.000 description 3
- 238000012546 transfer Methods 0.000 description 3
- 238000005406 washing Methods 0.000 description 3
- 208000003606 Congenital Rubella Syndrome Diseases 0.000 description 2
- 241000699800 Cricetinae Species 0.000 description 2
- 230000007023 DNA restriction-modification system Effects 0.000 description 2
- LTMHDMANZUZIPE-AMTYYWEZSA-N Digoxin Natural products O([C@H]1[C@H](C)O[C@H](O[C@@H]2C[C@@H]3[C@@](C)([C@@H]4[C@H]([C@]5(O)[C@](C)([C@H](O)C4)[C@H](C4=CC(=O)OC4)CC5)CC3)CC2)C[C@@H]1O)[C@H]1O[C@H](C)[C@@H](O[C@H]2O[C@@H](C)[C@H](O)[C@@H](O)C2)[C@@H](O)C1 LTMHDMANZUZIPE-AMTYYWEZSA-N 0.000 description 2
- 241000233866 Fungi Species 0.000 description 2
- 241000238631 Hexapoda Species 0.000 description 2
- 101710125507 Integrase/recombinase Proteins 0.000 description 2
- 102000004195 Isomerases Human genes 0.000 description 2
- 108090000769 Isomerases Proteins 0.000 description 2
- 241000235058 Komagataella pastoris Species 0.000 description 2
- 239000004472 Lysine Substances 0.000 description 2
- 241000124008 Mammalia Species 0.000 description 2
- 102000007999 Nuclear Proteins Human genes 0.000 description 2
- 108010089610 Nuclear Proteins Proteins 0.000 description 2
- 241000235648 Pichia Species 0.000 description 2
- 108010076504 Protein Sorting Signals Proteins 0.000 description 2
- 239000012327 Ruthenium complex Substances 0.000 description 2
- 241000235346 Schizosaccharomyces Species 0.000 description 2
- 241000256251 Spodoptera frugiperda Species 0.000 description 2
- 241001495444 Thermococcus sp. Species 0.000 description 2
- 230000009471 action Effects 0.000 description 2
- 238000013459 approach Methods 0.000 description 2
- 239000011324 bead Substances 0.000 description 2
- 230000008901 benefit Effects 0.000 description 2
- 150000001615 biotins Chemical class 0.000 description 2
- 230000000903 blocking effect Effects 0.000 description 2
- 230000006037 cell lysis Effects 0.000 description 2
- 238000005119 centrifugation Methods 0.000 description 2
- 230000003196 chaotropic effect Effects 0.000 description 2
- 239000003638 chemical reducing agent Substances 0.000 description 2
- 210000004978 chinese hamster ovary cell Anatomy 0.000 description 2
- 238000004587 chromatography analysis Methods 0.000 description 2
- 230000000295 complement effect Effects 0.000 description 2
- 230000009918 complex formation Effects 0.000 description 2
- 230000008878 coupling Effects 0.000 description 2
- 238000010168 coupling process Methods 0.000 description 2
- 230000009260 cross reactivity Effects 0.000 description 2
- 238000012217 deletion Methods 0.000 description 2
- 230000037430 deletion Effects 0.000 description 2
- 238000000502 dialysis Methods 0.000 description 2
- LTMHDMANZUZIPE-PUGKRICDSA-N digoxin Chemical compound C1[C@H](O)[C@H](O)[C@@H](C)O[C@H]1O[C@@H]1[C@@H](C)O[C@@H](O[C@@H]2[C@H](O[C@@H](O[C@@H]3C[C@@H]4[C@]([C@@H]5[C@H]([C@]6(CC[C@@H]([C@@]6(C)[C@H](O)C5)C=5COC(=O)C=5)O)CC4)(C)CC3)C[C@@H]2O)C)C[C@@H]1O LTMHDMANZUZIPE-PUGKRICDSA-N 0.000 description 2
- 229960005156 digoxin Drugs 0.000 description 2
- LTMHDMANZUZIPE-UHFFFAOYSA-N digoxine Natural products C1C(O)C(O)C(C)OC1OC1C(C)OC(OC2C(OC(OC3CC4C(C5C(C6(CCC(C6(C)C(O)C5)C=5COC(=O)C=5)O)CC4)(C)CC3)CC2O)C)CC1O LTMHDMANZUZIPE-UHFFFAOYSA-N 0.000 description 2
- 238000010790 dilution Methods 0.000 description 2
- 239000012895 dilution Substances 0.000 description 2
- 239000000539 dimer Substances 0.000 description 2
- 230000000694 effects Effects 0.000 description 2
- 230000008030 elimination Effects 0.000 description 2
- 238000003379 elimination reaction Methods 0.000 description 2
- 238000010828 elution Methods 0.000 description 2
- 230000005284 excitation Effects 0.000 description 2
- 239000013613 expression plasmid Substances 0.000 description 2
- 210000003754 fetus Anatomy 0.000 description 2
- 238000002523 gelfiltration Methods 0.000 description 2
- 230000002068 genetic effect Effects 0.000 description 2
- 238000010324 immunological assay Methods 0.000 description 2
- 230000006698 induction Effects 0.000 description 2
- 230000003834 intracellular effect Effects 0.000 description 2
- 210000003292 kidney cell Anatomy 0.000 description 2
- 239000007788 liquid Substances 0.000 description 2
- 239000007791 liquid phase Substances 0.000 description 2
- 239000012528 membrane Substances 0.000 description 2
- 229910052751 metal Inorganic materials 0.000 description 2
- 239000002184 metal Substances 0.000 description 2
- 230000004048 modification Effects 0.000 description 2
- 238000012986 modification Methods 0.000 description 2
- 239000002245 particle Substances 0.000 description 2
- 239000000049 pigment Substances 0.000 description 2
- 229910052697 platinum Inorganic materials 0.000 description 2
- 229920000642 polymer Polymers 0.000 description 2
- 230000012846 protein folding Effects 0.000 description 2
- 108020001775 protein parts Proteins 0.000 description 2
- 238000004153 renaturation Methods 0.000 description 2
- 230000003252 repetitive effect Effects 0.000 description 2
- FGDZQCVHDSGLHJ-UHFFFAOYSA-M rubidium chloride Chemical compound [Cl-].[Rb+] FGDZQCVHDSGLHJ-UHFFFAOYSA-M 0.000 description 2
- 238000000926 separation method Methods 0.000 description 2
- 238000007086 side reaction Methods 0.000 description 2
- 238000001542 size-exclusion chromatography Methods 0.000 description 2
- 125000006850 spacer group Chemical group 0.000 description 2
- 230000000087 stabilizing effect Effects 0.000 description 2
- 230000004936 stimulating effect Effects 0.000 description 2
- 238000006467 substitution reaction Methods 0.000 description 2
- 239000000725 suspension Substances 0.000 description 2
- 230000014616 translation Effects 0.000 description 2
- LWIHDJKSTIGBAC-UHFFFAOYSA-K tripotassium phosphate Chemical compound [K+].[K+].[K+].[O-]P([O-])([O-])=O LWIHDJKSTIGBAC-UHFFFAOYSA-K 0.000 description 2
- 108020005087 unfolded proteins Proteins 0.000 description 2
- 210000003501 vero cell Anatomy 0.000 description 2
- 230000003612 virological effect Effects 0.000 description 2
- 108091032973 (ribonucleotides)n+m Proteins 0.000 description 1
- BCHZICNRHXRCHY-UHFFFAOYSA-N 2h-oxazine Chemical compound N1OC=CC=C1 BCHZICNRHXRCHY-UHFFFAOYSA-N 0.000 description 1
- GOLORTLGFDVFDW-UHFFFAOYSA-N 3-(1h-benzimidazol-2-yl)-7-(diethylamino)chromen-2-one Chemical compound C1=CC=C2NC(C3=CC4=CC=C(C=C4OC3=O)N(CC)CC)=NC2=C1 GOLORTLGFDVFDW-UHFFFAOYSA-N 0.000 description 1
- DEQPBRIACBATHE-FXQIFTODSA-N 5-[(3as,4s,6ar)-2-oxo-1,3,3a,4,6,6a-hexahydrothieno[3,4-d]imidazol-4-yl]-2-iminopentanoic acid Chemical compound N1C(=O)N[C@@H]2[C@H](CCCC(=N)C(=O)O)SC[C@@H]21 DEQPBRIACBATHE-FXQIFTODSA-N 0.000 description 1
- 206010000234 Abortion spontaneous Diseases 0.000 description 1
- 241000567147 Aeropyrum Species 0.000 description 1
- 108010032595 Antibody Binding Sites Proteins 0.000 description 1
- 241000893512 Aquifex aeolicus Species 0.000 description 1
- DCXYFEDJOCDNAF-UHFFFAOYSA-N Asparagine Natural products OC(=O)C(N)CC(N)=O DCXYFEDJOCDNAF-UHFFFAOYSA-N 0.000 description 1
- 108090001008 Avidin Proteins 0.000 description 1
- 244000063299 Bacillus subtilis Species 0.000 description 1
- 108091032955 Bacterial small RNA Proteins 0.000 description 1
- 101710117545 C protein Proteins 0.000 description 1
- UXVMQQNJUSDDNG-UHFFFAOYSA-L Calcium chloride Chemical compound [Cl-].[Cl-].[Ca+2] UXVMQQNJUSDDNG-UHFFFAOYSA-L 0.000 description 1
- 101800001603 Capsid protein C Proteins 0.000 description 1
- 208000002177 Cataract Diseases 0.000 description 1
- 241000282693 Cercopithecidae Species 0.000 description 1
- 108020004705 Codon Proteins 0.000 description 1
- 108700010070 Codon Usage Proteins 0.000 description 1
- 101800001847 Core protein precursor Proteins 0.000 description 1
- 241000699802 Cricetulus griseus Species 0.000 description 1
- 241000938605 Crocodylia Species 0.000 description 1
- 239000004971 Cross linker Substances 0.000 description 1
- 235000019750 Crude protein Nutrition 0.000 description 1
- 206010011878 Deafness Diseases 0.000 description 1
- 229920002307 Dextran Polymers 0.000 description 1
- SHIBSTMRCDJXLN-UHFFFAOYSA-N Digoxigenin Natural products C1CC(C2C(C3(C)CCC(O)CC3CC2)CC2O)(O)C2(C)C1C1=CC(=O)OC1 SHIBSTMRCDJXLN-UHFFFAOYSA-N 0.000 description 1
- BVTJGGGYKAMDBN-UHFFFAOYSA-N Dioxetane Chemical class C1COO1 BVTJGGGYKAMDBN-UHFFFAOYSA-N 0.000 description 1
- KCXVZYZYPLLWCC-UHFFFAOYSA-N EDTA Chemical compound OC(=O)CN(CC(O)=O)CCN(CC(O)=O)CC(O)=O KCXVZYZYPLLWCC-UHFFFAOYSA-N 0.000 description 1
- 238000002965 ELISA Methods 0.000 description 1
- 241001198387 Escherichia coli BL21(DE3) Species 0.000 description 1
- 150000000918 Europium Chemical class 0.000 description 1
- 206010055690 Foetal death Diseases 0.000 description 1
- 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 1
- 208000031886 HIV Infections Diseases 0.000 description 1
- 101710154606 Hemagglutinin Proteins 0.000 description 1
- 108010093488 His-His-His-His-His-His Proteins 0.000 description 1
- 101000881168 Homo sapiens SPARC Proteins 0.000 description 1
- 241000713772 Human immunodeficiency virus 1 Species 0.000 description 1
- 241000713340 Human immunodeficiency virus 2 Species 0.000 description 1
- 235000019766 L-Lysine Nutrition 0.000 description 1
- DCXYFEDJOCDNAF-REOHCLBHSA-N L-asparagine Chemical compound OC(=O)[C@@H](N)CC(N)=O DCXYFEDJOCDNAF-REOHCLBHSA-N 0.000 description 1
- HNDVDQJCIGZPNO-YFKPBYRVSA-N L-histidine Chemical compound OC(=O)[C@@H](N)CC1=CN=CN1 HNDVDQJCIGZPNO-YFKPBYRVSA-N 0.000 description 1
- 241000186660 Lactobacillus Species 0.000 description 1
- 241000194036 Lactococcus Species 0.000 description 1
- 102000004856 Lectins Human genes 0.000 description 1
- 108090001090 Lectins Proteins 0.000 description 1
- 208000008771 Lymphadenopathy Diseases 0.000 description 1
- KDXKERNSBIXSRK-UHFFFAOYSA-N Lysine Natural products NCCCCC(N)C(O)=O KDXKERNSBIXSRK-UHFFFAOYSA-N 0.000 description 1
- 101710175625 Maltose/maltodextrin-binding periplasmic protein Proteins 0.000 description 1
- 241001465754 Metazoa Species 0.000 description 1
- 241000203407 Methanocaldococcus jannaschii Species 0.000 description 1
- 241000203382 Methanothermococcus thermolithotrophicus Species 0.000 description 1
- 230000004988 N-glycosylation Effects 0.000 description 1
- 241001195348 Nusa Species 0.000 description 1
- 241000320412 Ogataea angusta Species 0.000 description 1
- 241000283973 Oryctolagus cuniculus Species 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
- 241000606856 Pasteurella multocida Species 0.000 description 1
- 101000621511 Potato virus M (strain German) RNA silencing suppressor Proteins 0.000 description 1
- 101710176177 Protein A56 Proteins 0.000 description 1
- 208000003251 Pruritus Diseases 0.000 description 1
- 206010037660 Pyrexia Diseases 0.000 description 1
- 241000522615 Pyrococcus horikoshii Species 0.000 description 1
- 102000001218 Rec A Recombinases Human genes 0.000 description 1
- 108010055016 Rec A Recombinases Proteins 0.000 description 1
- 241000710801 Rubivirus Species 0.000 description 1
- 102100037599 SPARC Human genes 0.000 description 1
- 241000235070 Saccharomyces Species 0.000 description 1
- 241001123227 Saccharomyces pastorianus Species 0.000 description 1
- 241000607142 Salmonella Species 0.000 description 1
- 101000582398 Staphylococcus aureus Replication initiation protein Proteins 0.000 description 1
- 241000194017 Streptococcus Species 0.000 description 1
- 241000187747 Streptomyces Species 0.000 description 1
- 101710172711 Structural protein Proteins 0.000 description 1
- 239000004098 Tetracycline Substances 0.000 description 1
- 241000589596 Thermus Species 0.000 description 1
- 241000589499 Thermus thermophilus Species 0.000 description 1
- 102100036407 Thioredoxin Human genes 0.000 description 1
- 241000710924 Togaviridae Species 0.000 description 1
- 101800000385 Transmembrane protein Proteins 0.000 description 1
- 101800001690 Transmembrane protein gp41 Proteins 0.000 description 1
- 241000589884 Treponema pallidum Species 0.000 description 1
- 241000607626 Vibrio cholerae Species 0.000 description 1
- 108010067390 Viral Proteins Proteins 0.000 description 1
- 241000607479 Yersinia pestis Species 0.000 description 1
- 241000235017 Zygosaccharomyces Species 0.000 description 1
- 230000005856 abnormality Effects 0.000 description 1
- 206010000210 abortion Diseases 0.000 description 1
- 231100000176 abortion Toxicity 0.000 description 1
- 238000010521 absorption reaction Methods 0.000 description 1
- 238000009825 accumulation Methods 0.000 description 1
- DZBUGLKDJFMEHC-UHFFFAOYSA-O acridine;hydron Chemical compound C1=CC=CC2=CC3=CC=CC=C3[NH+]=C21 DZBUGLKDJFMEHC-UHFFFAOYSA-O 0.000 description 1
- 230000000996 additive effect Effects 0.000 description 1
- 229960000723 ampicillin Drugs 0.000 description 1
- 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 description 1
- 230000003321 amplification Effects 0.000 description 1
- 239000003242 anti bacterial agent Substances 0.000 description 1
- 230000000840 anti-viral effect Effects 0.000 description 1
- 229940088710 antibiotic agent Drugs 0.000 description 1
- 235000009582 asparagine Nutrition 0.000 description 1
- 229960001230 asparagine Drugs 0.000 description 1
- 210000003719 b-lymphocyte Anatomy 0.000 description 1
- 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 1
- LWISPDYGRSGXME-YDHLFZDLSA-N biotin peg2 amine Chemical compound N1C(=O)N[C@@H]2[C@H](CCCCC(=O)NCCOCCOCCN)SC[C@@H]21 LWISPDYGRSGXME-YDHLFZDLSA-N 0.000 description 1
- 210000004369 blood Anatomy 0.000 description 1
- 239000008280 blood Substances 0.000 description 1
- 239000001110 calcium chloride Substances 0.000 description 1
- 229910001628 calcium chloride Inorganic materials 0.000 description 1
- 239000001506 calcium phosphate Substances 0.000 description 1
- 229910000389 calcium phosphate Inorganic materials 0.000 description 1
- 235000011010 calcium phosphates Nutrition 0.000 description 1
- 230000015556 catabolic process Effects 0.000 description 1
- 230000001413 cellular effect Effects 0.000 description 1
- 239000013522 chelant Substances 0.000 description 1
- 238000010382 chemical cross-linking Methods 0.000 description 1
- 238000007385 chemical modification Methods 0.000 description 1
- 230000001010 compromised effect Effects 0.000 description 1
- 208000028831 congenital heart disease Diseases 0.000 description 1
- 210000000805 cytoplasm Anatomy 0.000 description 1
- 210000005220 cytoplasmic tail Anatomy 0.000 description 1
- 231100000895 deafness Toxicity 0.000 description 1
- 230000007812 deficiency Effects 0.000 description 1
- 238000006731 degradation reaction Methods 0.000 description 1
- 230000001419 dependent effect Effects 0.000 description 1
- 238000011161 development Methods 0.000 description 1
- 239000008121 dextrose Substances 0.000 description 1
- 238000002405 diagnostic procedure Methods 0.000 description 1
- 238000010586 diagram Methods 0.000 description 1
- QONQRTHLHBTMGP-UHFFFAOYSA-N digitoxigenin Natural products CC12CCC(C3(CCC(O)CC3CC3)C)C3C11OC1CC2C1=CC(=O)OC1 QONQRTHLHBTMGP-UHFFFAOYSA-N 0.000 description 1
- SHIBSTMRCDJXLN-KCZCNTNESA-N digoxigenin Chemical compound C1([C@@H]2[C@@]3([C@@](CC2)(O)[C@H]2[C@@H]([C@@]4(C)CC[C@H](O)C[C@H]4CC2)C[C@H]3O)C)=CC(=O)OC1 SHIBSTMRCDJXLN-KCZCNTNESA-N 0.000 description 1
- 201000010099 disease Diseases 0.000 description 1
- 208000037265 diseases, disorders, signs and symptoms Diseases 0.000 description 1
- 230000006334 disulfide bridging Effects 0.000 description 1
- 125000002228 disulfide group Chemical group 0.000 description 1
- 241001493065 dsRNA viruses Species 0.000 description 1
- 238000005516 engineering process Methods 0.000 description 1
- 210000003527 eukaryotic cell Anatomy 0.000 description 1
- 230000002349 favourable effect Effects 0.000 description 1
- 238000001914 filtration Methods 0.000 description 1
- GNBHRKFJIUUOQI-UHFFFAOYSA-N fluorescein Chemical compound O1C(=O)C2=CC=CC=C2C21C1=CC=C(O)C=C1OC1=CC(O)=CC=C21 GNBHRKFJIUUOQI-UHFFFAOYSA-N 0.000 description 1
- 230000002538 fungal effect Effects 0.000 description 1
- 230000007274 generation of a signal involved in cell-cell signaling Effects 0.000 description 1
- 238000010353 genetic engineering Methods 0.000 description 1
- 108091005608 glycosylated proteins Proteins 0.000 description 1
- 230000012010 growth Effects 0.000 description 1
- 208000016354 hearing loss disease Diseases 0.000 description 1
- 239000000185 hemagglutinin Substances 0.000 description 1
- 206010073071 hepatocellular carcinoma Diseases 0.000 description 1
- HNDVDQJCIGZPNO-UHFFFAOYSA-N histidine Natural products OC(=O)C(N)CC1=CN=CN1 HNDVDQJCIGZPNO-UHFFFAOYSA-N 0.000 description 1
- 239000012456 homogeneous solution Substances 0.000 description 1
- 238000002744 homologous recombination Methods 0.000 description 1
- 230000006801 homologous recombination Effects 0.000 description 1
- 239000005556 hormone Substances 0.000 description 1
- 229940088597 hormone Drugs 0.000 description 1
- 244000052637 human pathogen Species 0.000 description 1
- 230000028996 humoral immune response Effects 0.000 description 1
- 230000002209 hydrophobic effect Effects 0.000 description 1
- 230000008105 immune reaction Effects 0.000 description 1
- 230000002163 immunogen Effects 0.000 description 1
- 230000001976 improved effect Effects 0.000 description 1
- 238000007901 in situ hybridization Methods 0.000 description 1
- 238000001727 in vivo Methods 0.000 description 1
- 230000001939 inductive effect Effects 0.000 description 1
- 239000012678 infectious agent Substances 0.000 description 1
- 208000015181 infectious disease Diseases 0.000 description 1
- 230000002458 infectious effect Effects 0.000 description 1
- 238000002347 injection Methods 0.000 description 1
- 239000007924 injection Substances 0.000 description 1
- 238000003780 insertion Methods 0.000 description 1
- 230000037431 insertion Effects 0.000 description 1
- 231100001046 intrauterine death Toxicity 0.000 description 1
- 150000002500 ions Chemical class 0.000 description 1
- 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 1
- 125000001449 isopropyl group Chemical group [H]C([H])([H])C([H])(*)C([H])([H])[H] 0.000 description 1
- 229960000318 kanamycin Drugs 0.000 description 1
- 229930027917 kanamycin Natural products 0.000 description 1
- 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 description 1
- 229930182823 kanamycin A Natural products 0.000 description 1
- 210000003734 kidney Anatomy 0.000 description 1
- 229940039696 lactobacillus Drugs 0.000 description 1
- 239000002523 lectin Substances 0.000 description 1
- 239000003446 ligand Substances 0.000 description 1
- 239000006194 liquid suspension Substances 0.000 description 1
- 238000011068 loading method Methods 0.000 description 1
- 208000018555 lymphatic system disease Diseases 0.000 description 1
- 239000006166 lysate Substances 0.000 description 1
- 235000018977 lysine Nutrition 0.000 description 1
- 230000013011 mating Effects 0.000 description 1
- 108020004999 messenger RNA Proteins 0.000 description 1
- 238000013508 migration Methods 0.000 description 1
- 230000005012 migration Effects 0.000 description 1
- 238000010369 molecular cloning Methods 0.000 description 1
- 238000003199 nucleic acid amplification method Methods 0.000 description 1
- 235000015097 nutrients Nutrition 0.000 description 1
- 238000005457 optimization Methods 0.000 description 1
- 210000000056 organ Anatomy 0.000 description 1
- 201000008968 osteosarcoma Diseases 0.000 description 1
- 230000002018 overexpression Effects 0.000 description 1
- 229940051027 pasteurella multocida Drugs 0.000 description 1
- 239000008188 pellet Substances 0.000 description 1
- 125000001151 peptidyl group Chemical group 0.000 description 1
- 210000001322 periplasm Anatomy 0.000 description 1
- 239000000546 pharmaceutical excipient Substances 0.000 description 1
- 239000008363 phosphate buffer Substances 0.000 description 1
- 108091005981 phosphorylated proteins Proteins 0.000 description 1
- 230000035790 physiological processes and functions Effects 0.000 description 1
- 210000002381 plasma Anatomy 0.000 description 1
- 231100000614 poison Toxicity 0.000 description 1
- 230000008092 positive effect Effects 0.000 description 1
- 108091005626 post-translationally modified proteins Proteins 0.000 description 1
- 102000035123 post-translationally modified proteins Human genes 0.000 description 1
- 229910000160 potassium phosphate Inorganic materials 0.000 description 1
- 235000011009 potassium phosphates Nutrition 0.000 description 1
- 230000035935 pregnancy Effects 0.000 description 1
- 230000002028 premature Effects 0.000 description 1
- 238000002360 preparation method Methods 0.000 description 1
- 238000012545 processing Methods 0.000 description 1
- 210000001236 prokaryotic cell Anatomy 0.000 description 1
- 229960000856 protein c Drugs 0.000 description 1
- 238000011002 quantification Methods 0.000 description 1
- 239000011535 reaction buffer Substances 0.000 description 1
- 239000011541 reaction mixture Substances 0.000 description 1
- 102000005962 receptors Human genes 0.000 description 1
- 108020003175 receptors Proteins 0.000 description 1
- 238000003259 recombinant expression Methods 0.000 description 1
- 238000009877 rendering Methods 0.000 description 1
- 230000010076 replication Effects 0.000 description 1
- 125000006853 reporter group Chemical group 0.000 description 1
- 238000011160 research Methods 0.000 description 1
- HSSLDCABUXLXKM-UHFFFAOYSA-N resorufin Chemical compound C1=CC(=O)C=C2OC3=CC(O)=CC=C3N=C21 HSSLDCABUXLXKM-UHFFFAOYSA-N 0.000 description 1
- PYWVYCXTNDRMGF-UHFFFAOYSA-N rhodamine B Chemical compound [Cl-].C=12C=CC(=[N+](CC)CC)C=C2OC2=CC(N(CC)CC)=CC=C2C=1C1=CC=CC=C1C(O)=O PYWVYCXTNDRMGF-UHFFFAOYSA-N 0.000 description 1
- 229940102127 rubidium chloride Drugs 0.000 description 1
- 210000003296 saliva Anatomy 0.000 description 1
- 150000003839 salts Chemical class 0.000 description 1
- 230000028327 secretion Effects 0.000 description 1
- 230000035945 sensitivity Effects 0.000 description 1
- 230000000405 serological effect Effects 0.000 description 1
- 238000002741 site-directed mutagenesis Methods 0.000 description 1
- 238000002415 sodium dodecyl sulfate polyacrylamide gel electrophoresis Methods 0.000 description 1
- 238000005063 solubilization Methods 0.000 description 1
- 230000007928 solubilization Effects 0.000 description 1
- 239000002904 solvent Substances 0.000 description 1
- 238000011895 specific detection Methods 0.000 description 1
- 229940043517 specific immunoglobulins Drugs 0.000 description 1
- 208000000995 spontaneous abortion Diseases 0.000 description 1
- 230000002269 spontaneous effect Effects 0.000 description 1
- 230000006641 stabilisation Effects 0.000 description 1
- 238000011105 stabilization Methods 0.000 description 1
- 239000012086 standard solution Substances 0.000 description 1
- 239000003270 steroid hormone Substances 0.000 description 1
- 108020003113 steroid hormone receptors Proteins 0.000 description 1
- 102000005969 steroid hormone receptors Human genes 0.000 description 1
- 239000000758 substrate Substances 0.000 description 1
- 125000004434 sulfur atom Chemical group 0.000 description 1
- 239000006228 supernatant Substances 0.000 description 1
- 230000004083 survival effect Effects 0.000 description 1
- 230000009897 systematic effect Effects 0.000 description 1
- 229960002180 tetracycline Drugs 0.000 description 1
- 229930101283 tetracycline Natural products 0.000 description 1
- 235000019364 tetracycline Nutrition 0.000 description 1
- 150000003522 tetracyclines Chemical class 0.000 description 1
- ANRHNWWPFJCPAZ-UHFFFAOYSA-M thionine Chemical compound [Cl-].C1=CC(N)=CC2=[S+]C3=CC(N)=CC=C3N=C21 ANRHNWWPFJCPAZ-UHFFFAOYSA-M 0.000 description 1
- 108060008226 thioredoxin Proteins 0.000 description 1
- 229940094937 thioredoxin Drugs 0.000 description 1
- 210000001519 tissue Anatomy 0.000 description 1
- 239000003440 toxic substance Substances 0.000 description 1
- 238000013518 transcription Methods 0.000 description 1
- 230000035897 transcription Effects 0.000 description 1
- 238000001890 transfection Methods 0.000 description 1
- 238000013519 translation Methods 0.000 description 1
- QORWJWZARLRLPR-UHFFFAOYSA-H tricalcium bis(phosphate) Chemical compound [Ca+2].[Ca+2].[Ca+2].[O-]P([O-])([O-])=O.[O-]P([O-])([O-])=O QORWJWZARLRLPR-UHFFFAOYSA-H 0.000 description 1
- 241000701447 unidentified baculovirus Species 0.000 description 1
- 210000002700 urine Anatomy 0.000 description 1
- 238000002255 vaccination Methods 0.000 description 1
- 229940118696 vibrio cholerae Drugs 0.000 description 1
- 230000009385 viral infection Effects 0.000 description 1
- 210000002845 virion Anatomy 0.000 description 1
- 239000011534 wash buffer Substances 0.000 description 1
- XLYOFNOQVPJJNP-UHFFFAOYSA-N water Substances O XLYOFNOQVPJJNP-UHFFFAOYSA-N 0.000 description 1
Classifications
-
- 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
- G01N33/56983—Viruses
-
- C—CHEMISTRY; METALLURGY
- C07—ORGANIC CHEMISTRY
- C07K—PEPTIDES
- C07K14/00—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof
- C07K14/005—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof from viruses
-
- C—CHEMISTRY; METALLURGY
- C07—ORGANIC CHEMISTRY
- C07K—PEPTIDES
- C07K2319/00—Fusion polypeptide
- C07K2319/35—Fusion polypeptide containing a fusion for enhanced stability/folding during expression, e.g. fusions with chaperones or thioredoxin
-
- 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
- C12N2770/00—MICROORGANISMS OR ENZYMES; COMPOSITIONS THEREOF; PROPAGATING, PRESERVING, OR MAINTAINING MICROORGANISMS; MUTATION OR GENETIC ENGINEERING; CULTURE MEDIA ssRNA viruses positive-sense
- C12N2770/00011—Details
- C12N2770/36011—Togaviridae
- C12N2770/36211—Rubivirus, e.g. rubella virus
- C12N2770/36222—New viral proteins or individual genes, new structural or functional aspects of known viral proteins or genes
-
- 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
- G01N2333/005—Assays involving biological materials from specific organisms or of a specific nature from viruses
- G01N2333/08—RNA viruses
- G01N2333/18—Togaviridae; Flaviviridae
- G01N2333/19—Rubella virus
-
- G—PHYSICS
- G01—MEASURING; TESTING
- G01N—INVESTIGATING OR ANALYSING MATERIALS BY DETERMINING THEIR CHEMICAL OR PHYSICAL PROPERTIES
- G01N2469/00—Immunoassays for the detection of microorganisms
- G01N2469/20—Detection of antibodies in sample from host which are directed against antigens from microorganisms
-
- Y—GENERAL TAGGING OF NEW TECHNOLOGICAL DEVELOPMENTS; GENERAL TAGGING OF CROSS-SECTIONAL TECHNOLOGIES SPANNING OVER SEVERAL SECTIONS OF THE IPC; TECHNICAL SUBJECTS COVERED BY FORMER USPC CROSS-REFERENCE ART COLLECTIONS [XRACs] AND DIGESTS
- Y02—TECHNOLOGIES OR APPLICATIONS FOR MITIGATION OR ADAPTATION AGAINST CLIMATE CHANGE
- Y02A—TECHNOLOGIES FOR ADAPTATION TO CLIMATE CHANGE
- Y02A50/00—TECHNOLOGIES FOR ADAPTATION TO CLIMATE CHANGE in human health protection, e.g. against extreme weather
- Y02A50/30—Against vector-borne diseases, e.g. mosquito-borne, fly-borne, tick-borne or waterborne diseases whose impact is exacerbated by climate change
Landscapes
- Health & Medical Sciences (AREA)
- Life Sciences & Earth Sciences (AREA)
- Chemical & Material Sciences (AREA)
- Virology (AREA)
- Engineering & Computer Science (AREA)
- Immunology (AREA)
- Molecular Biology (AREA)
- General Health & Medical Sciences (AREA)
- Biochemistry (AREA)
- Medicinal Chemistry (AREA)
- Urology & Nephrology (AREA)
- Hematology (AREA)
- Organic Chemistry (AREA)
- Biomedical Technology (AREA)
- Cell Biology (AREA)
- Biophysics (AREA)
- Tropical Medicine & Parasitology (AREA)
- Biotechnology (AREA)
- Genetics & Genomics (AREA)
- Proteomics, Peptides & Aminoacids (AREA)
- Microbiology (AREA)
- Gastroenterology & Hepatology (AREA)
- Food Science & Technology (AREA)
- Physics & Mathematics (AREA)
- Analytical Chemistry (AREA)
- General Physics & Mathematics (AREA)
- Pathology (AREA)
- Peptides Or Proteins (AREA)
- Preparation Of Compounds By Using Micro-Organisms (AREA)
- Micro-Organisms Or Cultivation Processes Thereof (AREA)
Applications Claiming Priority (3)
| Application Number | Priority Date | Filing Date | Title |
|---|---|---|---|
| EP07024190 | 2007-12-13 | ||
| EP07024190 | 2007-12-13 | ||
| PCT/EP2008/010532 WO2009074318A2 (en) | 2007-12-13 | 2008-12-11 | Novel rubella e1 envelope protein variants and their use in the detection of anti-rubella antibodies |
Publications (1)
| Publication Number | Publication Date |
|---|---|
| ES2450998T3 true ES2450998T3 (es) | 2014-03-26 |
Family
ID=40671057
Family Applications (1)
| Application Number | Title | Priority Date | Filing Date |
|---|---|---|---|
| ES08860033.3T Active ES2450998T3 (es) | 2007-12-13 | 2008-12-11 | Nuevas variantes de proteína de cubierta E1 de rubéola y su utilización en la detección de anticuerpos anti-rubéola |
Country Status (7)
| Country | Link |
|---|---|
| US (1) | US8551696B2 (enExample) |
| EP (1) | EP2222694B1 (enExample) |
| JP (1) | JP5461423B2 (enExample) |
| CN (1) | CN101939330B (enExample) |
| CA (1) | CA2705716C (enExample) |
| ES (1) | ES2450998T3 (enExample) |
| WO (1) | WO2009074318A2 (enExample) |
Families Citing this family (8)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| EP2706115A1 (en) | 2012-09-06 | 2014-03-12 | Roche Diagnostics GmbH | Chaperone-chaperone fusion polypeptides for reduction of interference and stabilization of immunoassays |
| EA201500503A1 (ru) | 2012-11-08 | 2015-10-30 | Ф.Хоффманн-Ля Рош Аг | Анти-her3/her4 антигенсвязывающие белки, связывающиеся с бета-шпилькой her3 и бета-шпилькой her4 |
| MX2016014862A (es) | 2014-05-14 | 2017-02-27 | Hoffmann La Roche | Her3 / her2 anticuerpos biespecificos que se unen a la horquilla beta de her3 y al dominio ii de her2. |
| CN108136000B (zh) * | 2015-09-30 | 2022-11-08 | 勃林格殷格翰动物保健有限公司 | 经改良的模块化抗原转运分子及其在动物中的用途 |
| BR112018012055A2 (pt) * | 2015-12-15 | 2018-12-04 | Hoffmann La Roche | substrato de transglutaminase (tg) recombinante, método in vitro para marcar uma proteína de interesse, composição farmacêutica ou de diagnóstico e kit de diagnóstico |
| WO2020010009A1 (en) * | 2018-07-02 | 2020-01-09 | Siemens Healthcare Diagnostics Inc. | Direct immunoassay measurement of autoantibodies |
| DE102019004812B4 (de) | 2019-07-10 | 2021-03-18 | Institut Virion-Serion GmbH Würzburg | Rubella Virus Spike Konstrukt |
| CN115197941A (zh) * | 2021-04-08 | 2022-10-18 | 中国科学院分子细胞科学卓越创新中心 | 具有分子伴侣功能的rna及其应用 |
Family Cites Families (6)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| AU736670B2 (en) | 1996-09-26 | 2001-08-02 | Medical Research Council | Chaperone fragments |
| ATE289354T1 (de) * | 1999-04-15 | 2005-03-15 | Crucell Holland Bv | Verwendung von adenovirus e1 protein sequenzen kodierenden, zur herstellung von rekombinanten proteinen in menschlichen zellen. |
| EP1103610A1 (en) * | 1999-11-26 | 2001-05-30 | Introgene B.V. | Production of vaccines from immortalised mammalian cell lines |
| PL215170B1 (pl) | 2001-06-22 | 2013-10-31 | Hoffmann La Roche | Sposób wytwarzania rozpuszczalnego kompleksu zawierajacego amyloidogenne bialko docelowe oraz bialko opiekuncze z klasy izomeraz peptydyloprolilowych |
| EP1780282B1 (en) * | 2005-10-26 | 2010-12-08 | Roche Diagnostics GmbH | Recombinant expression of Rubella E1 envelope protein variants as chaperone fusion-proteins, and their use in the detection of anti-Rubella antibodies |
| CA2562738C (en) * | 2005-10-26 | 2011-07-12 | F. Hoffmann-La Roche Ag | Soluble rubella e1 envelope antigens |
-
2008
- 2008-12-11 JP JP2010537314A patent/JP5461423B2/ja active Active
- 2008-12-11 CA CA2705716A patent/CA2705716C/en active Active
- 2008-12-11 EP EP08860033.3A patent/EP2222694B1/en active Active
- 2008-12-11 ES ES08860033.3T patent/ES2450998T3/es active Active
- 2008-12-11 CN CN200880121328.1A patent/CN101939330B/zh active Active
- 2008-12-11 WO PCT/EP2008/010532 patent/WO2009074318A2/en not_active Ceased
-
2010
- 2010-06-03 US US12/793,134 patent/US8551696B2/en active Active
Also Published As
| Publication number | Publication date |
|---|---|
| US20110059552A1 (en) | 2011-03-10 |
| CN101939330B (zh) | 2014-06-04 |
| CA2705716C (en) | 2013-03-19 |
| JP5461423B2 (ja) | 2014-04-02 |
| EP2222694A2 (en) | 2010-09-01 |
| WO2009074318A3 (en) | 2009-07-30 |
| EP2222694B1 (en) | 2014-01-15 |
| CN101939330A (zh) | 2011-01-05 |
| CA2705716A1 (en) | 2009-06-18 |
| HK1148026A1 (en) | 2011-08-26 |
| JP2011505811A (ja) | 2011-03-03 |
| US8551696B2 (en) | 2013-10-08 |
| WO2009074318A2 (en) | 2009-06-18 |
Similar Documents
| Publication | Publication Date | Title |
|---|---|---|
| ES2450998T3 (es) | Nuevas variantes de proteína de cubierta E1 de rubéola y su utilización en la detección de anticuerpos anti-rubéola | |
| JP3945822B2 (ja) | 複数エピトープ融合タンパク質 | |
| CA2667177C (en) | Slpa as a tool for recombinant protein and enzyme technology | |
| EP2267452A1 (en) | A soluble complex comprising a retroviral surface glycoprotein | |
| ES2561462T3 (es) | Antígenos TpN47 de Treponema pallidum inmunorreactivos solubles | |
| US7074555B2 (en) | Detection of West Nile Virus | |
| EP1780282B1 (en) | Recombinant expression of Rubella E1 envelope protein variants as chaperone fusion-proteins, and their use in the detection of anti-Rubella antibodies | |
| EP3110831B1 (en) | Soluble and immunoreactive variants of htlv capsid antigen p24 | |
| US20210349090A1 (en) | Corona nucleocapsid antigen for use in antibody-immunoassays | |
| ES2356383T3 (es) | Expresión recombinante de variantes de proteína de cubierta de rubeola e1 como proteínas de fusión chaperonas, y utilización de las mismas en la detección de anticuerpos anti-rubeola. | |
| ES2949180T3 (es) | Construcción de espícula del virus de la rubéola | |
| HK1148026B (en) | Novel rubella e1 envelope protein variants and their use in the detection of antirubella antibodies | |
| CN115843334A (zh) | 用于抗体免疫测定的冠状核衣壳抗原 | |
| JP2025517121A (ja) | 免疫診断アッセイのためのHIV gp41バリアント | |
| CN106699895A (zh) | 一种新型融合抗原和包含其的检测试剂盒及应用 | |
| HK1138620B (en) | Slpa as a tool for recombinant protein and enzyme technology |