ES2596952T3 - Péptidos, dispositivos y procedimientos para la detección de anticuerpos de Ehrlichia - Google Patents
Péptidos, dispositivos y procedimientos para la detección de anticuerpos de Ehrlichia Download PDFInfo
- Publication number
- ES2596952T3 ES2596952T3 ES10832262.9T ES10832262T ES2596952T3 ES 2596952 T3 ES2596952 T3 ES 2596952T3 ES 10832262 T ES10832262 T ES 10832262T ES 2596952 T3 ES2596952 T3 ES 2596952T3
- Authority
- ES
- Spain
- Prior art keywords
- peptide
- seq
- sequence
- amino acid
- peptides
- 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
- 108090000765 processed proteins & peptides Proteins 0.000 title abstract description 211
- 102000004196 processed proteins & peptides Human genes 0.000 title abstract description 92
- 241000605314 Ehrlichia Species 0.000 title description 31
- 238000000034 method Methods 0.000 title description 27
- 238000001514 detection method Methods 0.000 title description 21
- 150000001413 amino acids Chemical class 0.000 abstract description 75
- 239000000203 mixture Substances 0.000 abstract description 18
- 101800001415 Bri23 peptide Proteins 0.000 abstract description 14
- 101800000655 C-terminal peptide Proteins 0.000 abstract description 14
- 102400000107 C-terminal peptide Human genes 0.000 abstract description 14
- 125000003275 alpha amino acid group Chemical group 0.000 abstract 2
- 235000001014 amino acid Nutrition 0.000 description 65
- 229940024606 amino acid Drugs 0.000 description 61
- 239000000523 sample Substances 0.000 description 44
- 150000007523 nucleic acids Chemical class 0.000 description 26
- 239000000427 antigen Substances 0.000 description 24
- 108091007433 antigens Proteins 0.000 description 24
- 102000036639 antigens Human genes 0.000 description 24
- 102000039446 nucleic acids Human genes 0.000 description 24
- 108020004707 nucleic acids Proteins 0.000 description 24
- 238000012360 testing method Methods 0.000 description 18
- 101710138624 Otolith matrix protein 1 Proteins 0.000 description 16
- 229920001184 polypeptide Polymers 0.000 description 16
- 210000004027 cell Anatomy 0.000 description 15
- 108090000623 proteins and genes Proteins 0.000 description 14
- 235000018102 proteins Nutrition 0.000 description 13
- 102000004169 proteins and genes Human genes 0.000 description 13
- 239000013598 vector Substances 0.000 description 13
- 102000004190 Enzymes Human genes 0.000 description 12
- 108090000790 Enzymes Proteins 0.000 description 12
- 229940088598 enzyme Drugs 0.000 description 12
- 239000012634 fragment Substances 0.000 description 12
- 125000000539 amino acid group Chemical group 0.000 description 11
- 230000014509 gene expression Effects 0.000 description 11
- 239000003446 ligand Substances 0.000 description 11
- 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 10
- 238000002965 ELISA Methods 0.000 description 10
- 102000040430 polynucleotide Human genes 0.000 description 10
- 108091033319 polynucleotide Proteins 0.000 description 10
- 239000002157 polynucleotide Substances 0.000 description 10
- DHMQDGOQFOQNFH-UHFFFAOYSA-N Glycine Chemical compound NCC(O)=O DHMQDGOQFOQNFH-UHFFFAOYSA-N 0.000 description 9
- 208000015181 infectious disease Diseases 0.000 description 9
- 230000027455 binding Effects 0.000 description 8
- 238000003018 immunoassay Methods 0.000 description 8
- 239000012528 membrane Substances 0.000 description 8
- 108010001336 Horseradish Peroxidase Proteins 0.000 description 7
- 230000004520 agglutination Effects 0.000 description 7
- 210000004899 c-terminal region Anatomy 0.000 description 7
- 239000000562 conjugate Substances 0.000 description 7
- 239000013604 expression vector Substances 0.000 description 7
- 239000002245 particle Substances 0.000 description 7
- 125000006850 spacer group Chemical group 0.000 description 7
- -1 aliphatic amino acids Chemical class 0.000 description 6
- 238000003556 assay Methods 0.000 description 6
- 238000012217 deletion Methods 0.000 description 6
- 230000037430 deletion Effects 0.000 description 6
- 210000002966 serum Anatomy 0.000 description 6
- 239000004471 Glycine Substances 0.000 description 5
- 239000000020 Nitrocellulose Substances 0.000 description 5
- 239000013060 biological fluid Substances 0.000 description 5
- 229960002685 biotin Drugs 0.000 description 5
- 235000020958 biotin Nutrition 0.000 description 5
- 239000011616 biotin Substances 0.000 description 5
- 239000003795 chemical substances by application Substances 0.000 description 5
- 230000002458 infectious effect Effects 0.000 description 5
- 229920001220 nitrocellulos Polymers 0.000 description 5
- 239000000243 solution Substances 0.000 description 5
- 239000000758 substrate Substances 0.000 description 5
- 210000001519 tissue Anatomy 0.000 description 5
- 108090001008 Avidin Proteins 0.000 description 4
- 108020004414 DNA Proteins 0.000 description 4
- 101000918259 Enterobacteria phage T4 Exonuclease subunit 1 Proteins 0.000 description 4
- 101000896152 Escherichia phage Mu Baseplate protein gp47 Proteins 0.000 description 4
- 101710127944 Non-structural polyprotein p200 Proteins 0.000 description 4
- 239000002033 PVDF binder Substances 0.000 description 4
- 101710124413 Portal protein Proteins 0.000 description 4
- 101710083205 SAR-endolysin Proteins 0.000 description 4
- 101710092804 Tail tube protein gp19 Proteins 0.000 description 4
- 101800000385 Transmembrane protein Proteins 0.000 description 4
- 235000004279 alanine Nutrition 0.000 description 4
- 230000000890 antigenic effect Effects 0.000 description 4
- 230000001580 bacterial effect Effects 0.000 description 4
- 239000011324 bead Substances 0.000 description 4
- 230000015572 biosynthetic process Effects 0.000 description 4
- 210000004369 blood Anatomy 0.000 description 4
- 239000008280 blood Substances 0.000 description 4
- 208000000292 ehrlichiosis Diseases 0.000 description 4
- PCHJSUWPFVWCPO-UHFFFAOYSA-N gold Chemical compound [Au] PCHJSUWPFVWCPO-UHFFFAOYSA-N 0.000 description 4
- 230000003287 optical effect Effects 0.000 description 4
- 230000002285 radioactive effect Effects 0.000 description 4
- 230000009870 specific binding Effects 0.000 description 4
- 238000006467 substitution reaction Methods 0.000 description 4
- 102100026189 Beta-galactosidase Human genes 0.000 description 3
- 108091003079 Bovine Serum Albumin Proteins 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
- 241001465754 Metazoa Species 0.000 description 3
- 238000012300 Sequence Analysis Methods 0.000 description 3
- MTCFGRXMJLQNBG-UHFFFAOYSA-N Serine Natural products OCC(N)C(O)=O MTCFGRXMJLQNBG-UHFFFAOYSA-N 0.000 description 3
- AYFVYJQAPQTCCC-UHFFFAOYSA-N Threonine Natural products CC(O)C(N)C(O)=O AYFVYJQAPQTCCC-UHFFFAOYSA-N 0.000 description 3
- 239000004473 Threonine Substances 0.000 description 3
- 108010005774 beta-Galactosidase Proteins 0.000 description 3
- 239000011230 binding agent Substances 0.000 description 3
- 210000001124 body fluid Anatomy 0.000 description 3
- 239000010839 body fluid Substances 0.000 description 3
- 229940098773 bovine serum albumin Drugs 0.000 description 3
- 239000000872 buffer Substances 0.000 description 3
- 230000004927 fusion Effects 0.000 description 3
- 125000003630 glycyl group Chemical group [H]N([H])C([H])([H])C(*)=O 0.000 description 3
- 210000000987 immune system Anatomy 0.000 description 3
- 239000004816 latex Substances 0.000 description 3
- 229920000126 latex Polymers 0.000 description 3
- 230000005693 optoelectronics Effects 0.000 description 3
- 230000001717 pathogenic effect Effects 0.000 description 3
- 229920002981 polyvinylidene fluoride Polymers 0.000 description 3
- 235000004400 serine Nutrition 0.000 description 3
- 239000000126 substance Substances 0.000 description 3
- 235000008521 threonine Nutrition 0.000 description 3
- 230000003612 virological effect Effects 0.000 description 3
- MTCFGRXMJLQNBG-REOHCLBHSA-N (2S)-2-Amino-3-hydroxypropansäure Chemical compound OC[C@H](N)C(O)=O MTCFGRXMJLQNBG-REOHCLBHSA-N 0.000 description 2
- 102000002260 Alkaline Phosphatase Human genes 0.000 description 2
- 108020004774 Alkaline Phosphatase Proteins 0.000 description 2
- DCXYFEDJOCDNAF-UHFFFAOYSA-N Asparagine Natural products OC(=O)C(N)CC(N)=O DCXYFEDJOCDNAF-UHFFFAOYSA-N 0.000 description 2
- 241000282994 Cervidae Species 0.000 description 2
- 102000053602 DNA Human genes 0.000 description 2
- 238000012286 ELISA Assay Methods 0.000 description 2
- 241000605312 Ehrlichia canis Species 0.000 description 2
- 241000605310 Ehrlichia chaffeensis Species 0.000 description 2
- 101001065501 Escherichia phage MS2 Lysis protein Proteins 0.000 description 2
- 108091006027 G proteins Proteins 0.000 description 2
- 108091000058 GTP-Binding Proteins 0.000 description 2
- 241000287828 Gallus gallus Species 0.000 description 2
- 241000238631 Hexapoda Species 0.000 description 2
- 108060003951 Immunoglobulin Proteins 0.000 description 2
- XUJNEKJLAYXESH-REOHCLBHSA-N L-Cysteine Chemical compound SC[C@H](N)C(O)=O XUJNEKJLAYXESH-REOHCLBHSA-N 0.000 description 2
- DCXYFEDJOCDNAF-REOHCLBHSA-N L-asparagine Chemical compound OC(=O)[C@@H](N)CC(N)=O DCXYFEDJOCDNAF-REOHCLBHSA-N 0.000 description 2
- ZDXPYRJPNDTMRX-VKHMYHEASA-N L-glutamine Chemical compound OC(=O)[C@@H](N)CCC(N)=O ZDXPYRJPNDTMRX-VKHMYHEASA-N 0.000 description 2
- AGPKZVBTJJNPAG-WHFBIAKZSA-N L-isoleucine Chemical compound CC[C@H](C)[C@H](N)C(O)=O AGPKZVBTJJNPAG-WHFBIAKZSA-N 0.000 description 2
- FFEARJCKVFRZRR-BYPYZUCNSA-N L-methionine Chemical compound CSCC[C@H](N)C(O)=O FFEARJCKVFRZRR-BYPYZUCNSA-N 0.000 description 2
- COLNVLDHVKWLRT-QMMMGPOBSA-N L-phenylalanine Chemical compound OC(=O)[C@@H](N)CC1=CC=CC=C1 COLNVLDHVKWLRT-QMMMGPOBSA-N 0.000 description 2
- AYFVYJQAPQTCCC-GBXIJSLDSA-N L-threonine Chemical compound C[C@@H](O)[C@H](N)C(O)=O AYFVYJQAPQTCCC-GBXIJSLDSA-N 0.000 description 2
- QIVBCDIJIAJPQS-VIFPVBQESA-N L-tryptophane Chemical compound C1=CC=C2C(C[C@H](N)C(O)=O)=CNC2=C1 QIVBCDIJIAJPQS-VIFPVBQESA-N 0.000 description 2
- OUYCCCASQSFEME-QMMMGPOBSA-N L-tyrosine Chemical compound OC(=O)[C@@H](N)CC1=CC=C(O)C=C1 OUYCCCASQSFEME-QMMMGPOBSA-N 0.000 description 2
- KZSNJWFQEVHDMF-BYPYZUCNSA-N L-valine Chemical compound CC(C)[C@H](N)C(O)=O KZSNJWFQEVHDMF-BYPYZUCNSA-N 0.000 description 2
- 108020004511 Recombinant DNA Proteins 0.000 description 2
- 240000004808 Saccharomyces cerevisiae Species 0.000 description 2
- 101710120037 Toxin CcdB Proteins 0.000 description 2
- QIVBCDIJIAJPQS-UHFFFAOYSA-N Tryptophan Natural products C1=CC=C2C(CC(N)C(O)=O)=CNC2=C1 QIVBCDIJIAJPQS-UHFFFAOYSA-N 0.000 description 2
- KZSNJWFQEVHDMF-UHFFFAOYSA-N Valine Natural products CC(C)C(N)C(O)=O KZSNJWFQEVHDMF-UHFFFAOYSA-N 0.000 description 2
- 238000007792 addition Methods 0.000 description 2
- 125000003295 alanine group Chemical group N[C@@H](C)C(=O)* 0.000 description 2
- 238000004458 analytical method Methods 0.000 description 2
- 235000009582 asparagine Nutrition 0.000 description 2
- 229960001230 asparagine Drugs 0.000 description 2
- 239000012472 biological sample Substances 0.000 description 2
- 230000000903 blocking effect Effects 0.000 description 2
- 239000008366 buffered solution Substances 0.000 description 2
- 230000001413 cellular effect Effects 0.000 description 2
- 210000001175 cerebrospinal fluid Anatomy 0.000 description 2
- 238000006243 chemical reaction Methods 0.000 description 2
- 239000011248 coating agent Substances 0.000 description 2
- 238000000576 coating method Methods 0.000 description 2
- 239000002299 complementary DNA Substances 0.000 description 2
- 150000001875 compounds Chemical class 0.000 description 2
- 238000004590 computer program Methods 0.000 description 2
- XUJNEKJLAYXESH-UHFFFAOYSA-N cysteine Natural products SCC(N)C(O)=O XUJNEKJLAYXESH-UHFFFAOYSA-N 0.000 description 2
- 235000018417 cysteine Nutrition 0.000 description 2
- 230000000694 effects Effects 0.000 description 2
- 238000010353 genetic engineering Methods 0.000 description 2
- ZDXPYRJPNDTMRX-UHFFFAOYSA-N glutamine Natural products OC(=O)C(N)CCC(N)=O ZDXPYRJPNDTMRX-UHFFFAOYSA-N 0.000 description 2
- 235000004554 glutamine Nutrition 0.000 description 2
- 238000004128 high performance liquid chromatography Methods 0.000 description 2
- HNDVDQJCIGZPNO-UHFFFAOYSA-N histidine Natural products OC(=O)C(N)CC1=CN=CN1 HNDVDQJCIGZPNO-UHFFFAOYSA-N 0.000 description 2
- 102000018358 immunoglobulin Human genes 0.000 description 2
- 230000003993 interaction Effects 0.000 description 2
- 229960000310 isoleucine Drugs 0.000 description 2
- AGPKZVBTJJNPAG-UHFFFAOYSA-N isoleucine Natural products CCC(C)C(N)C(O)=O AGPKZVBTJJNPAG-UHFFFAOYSA-N 0.000 description 2
- 235000014705 isoleucine Nutrition 0.000 description 2
- 238000002372 labelling Methods 0.000 description 2
- 238000004811 liquid chromatography Methods 0.000 description 2
- 108010026228 mRNA guanylyltransferase Proteins 0.000 description 2
- 239000002184 metal Substances 0.000 description 2
- 229910052751 metal Inorganic materials 0.000 description 2
- 229930182817 methionine Natural products 0.000 description 2
- 244000005700 microbiome Species 0.000 description 2
- COLNVLDHVKWLRT-UHFFFAOYSA-N phenylalanine Natural products OC(=O)C(N)CC1=CC=CC=C1 COLNVLDHVKWLRT-UHFFFAOYSA-N 0.000 description 2
- 210000002381 plasma Anatomy 0.000 description 2
- 239000013612 plasmid Substances 0.000 description 2
- 238000000746 purification Methods 0.000 description 2
- 239000011541 reaction mixture Substances 0.000 description 2
- 230000001105 regulatory effect Effects 0.000 description 2
- 230000010076 replication Effects 0.000 description 2
- 210000003296 saliva Anatomy 0.000 description 2
- 239000007787 solid Substances 0.000 description 2
- 241000894007 species Species 0.000 description 2
- 238000010561 standard procedure Methods 0.000 description 2
- OUYCCCASQSFEME-UHFFFAOYSA-N tyrosine Natural products OC(=O)C(N)CC1=CC=C(O)C=C1 OUYCCCASQSFEME-UHFFFAOYSA-N 0.000 description 2
- 235000002374 tyrosine Nutrition 0.000 description 2
- 239000004474 valine Substances 0.000 description 2
- 239000011534 wash buffer Substances 0.000 description 2
- 241000710929 Alphavirus Species 0.000 description 1
- 239000004475 Arginine Substances 0.000 description 1
- 235000014469 Bacillus subtilis Nutrition 0.000 description 1
- 241000283690 Bos taurus Species 0.000 description 1
- 108010075254 C-Peptide Proteins 0.000 description 1
- 241000283707 Capra Species 0.000 description 1
- 241000701022 Cytomegalovirus Species 0.000 description 1
- 241000588724 Escherichia coli Species 0.000 description 1
- 241000701959 Escherichia virus Lambda Species 0.000 description 1
- 102000030782 GTP binding Human genes 0.000 description 1
- 108010015776 Glucose oxidase Proteins 0.000 description 1
- 239000004366 Glucose oxidase Substances 0.000 description 1
- 102000005720 Glutathione transferase Human genes 0.000 description 1
- 108010070675 Glutathione transferase Proteins 0.000 description 1
- 206010020429 Human ehrlichiosis Diseases 0.000 description 1
- ONIBWKKTOPOVIA-BYPYZUCNSA-N L-Proline Chemical compound OC(=O)[C@@H]1CCCN1 ONIBWKKTOPOVIA-BYPYZUCNSA-N 0.000 description 1
- ODKSFYDXXFIFQN-BYPYZUCNSA-P L-argininium(2+) Chemical compound NC(=[NH2+])NCCC[C@H]([NH3+])C(O)=O ODKSFYDXXFIFQN-BYPYZUCNSA-P 0.000 description 1
- CKLJMWTZIZZHCS-REOHCLBHSA-N L-aspartic acid Chemical compound OC(=O)[C@@H](N)CC(O)=O CKLJMWTZIZZHCS-REOHCLBHSA-N 0.000 description 1
- WHUUTDBJXJRKMK-VKHMYHEASA-N L-glutamic acid Chemical compound OC(=O)[C@@H](N)CCC(O)=O WHUUTDBJXJRKMK-VKHMYHEASA-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
- ROHFNLRQFUQHCH-YFKPBYRVSA-N L-leucine Chemical compound CC(C)C[C@H](N)C(O)=O ROHFNLRQFUQHCH-YFKPBYRVSA-N 0.000 description 1
- KDXKERNSBIXSRK-YFKPBYRVSA-N L-lysine Chemical compound NCCCC[C@H](N)C(O)=O KDXKERNSBIXSRK-YFKPBYRVSA-N 0.000 description 1
- ROHFNLRQFUQHCH-UHFFFAOYSA-N Leucine Natural products CC(C)CC(N)C(O)=O ROHFNLRQFUQHCH-UHFFFAOYSA-N 0.000 description 1
- KDXKERNSBIXSRK-UHFFFAOYSA-N Lysine Natural products NCCCCC(N)C(O)=O KDXKERNSBIXSRK-UHFFFAOYSA-N 0.000 description 1
- 239000004472 Lysine Substances 0.000 description 1
- 241000829100 Macaca mulatta polyomavirus 1 Species 0.000 description 1
- 241000124008 Mammalia Species 0.000 description 1
- 241000713869 Moloney murine leukemia virus Species 0.000 description 1
- 241000713862 Moloney murine sarcoma virus Species 0.000 description 1
- 241000713333 Mouse mammary tumor virus Species 0.000 description 1
- 108091028043 Nucleic acid sequence Proteins 0.000 description 1
- 108010033276 Peptide Fragments Proteins 0.000 description 1
- 102000007079 Peptide Fragments Human genes 0.000 description 1
- ONIBWKKTOPOVIA-UHFFFAOYSA-N Proline Natural products OC(=O)C1CCCN1 ONIBWKKTOPOVIA-UHFFFAOYSA-N 0.000 description 1
- 108010076504 Protein Sorting Signals Proteins 0.000 description 1
- 241000589516 Pseudomonas Species 0.000 description 1
- 241000714474 Rous sarcoma virus Species 0.000 description 1
- 241000710960 Sindbis virus Species 0.000 description 1
- 108010088160 Staphylococcal Protein A Proteins 0.000 description 1
- 108010090804 Streptavidin Proteins 0.000 description 1
- 241000187747 Streptomyces Species 0.000 description 1
- NINIDFKCEFEMDL-UHFFFAOYSA-N Sulfur Chemical compound [S] NINIDFKCEFEMDL-UHFFFAOYSA-N 0.000 description 1
- 210000001744 T-lymphocyte Anatomy 0.000 description 1
- QPMSXSBEVQLBIL-CZRHPSIPSA-N ac1mix0p Chemical compound C1=CC=C2N(C[C@H](C)CN(C)C)C3=CC(OC)=CC=C3SC2=C1.O([C@H]1[C@]2(OC)C=CC34C[C@@H]2[C@](C)(O)CCC)C2=C5[C@]41CCN(C)[C@@H]3CC5=CC=C2O QPMSXSBEVQLBIL-CZRHPSIPSA-N 0.000 description 1
- 239000002253 acid Substances 0.000 description 1
- 230000002378 acidificating effect Effects 0.000 description 1
- 150000007513 acids Chemical class 0.000 description 1
- 238000001042 affinity chromatography Methods 0.000 description 1
- 238000007818 agglutination assay Methods 0.000 description 1
- 125000001931 aliphatic group Chemical group 0.000 description 1
- 150000001408 amides Chemical class 0.000 description 1
- 230000003321 amplification Effects 0.000 description 1
- 239000002518 antifoaming agent Substances 0.000 description 1
- ODKSFYDXXFIFQN-UHFFFAOYSA-N arginine Natural products OC(=O)C(N)CCCNC(N)=N ODKSFYDXXFIFQN-UHFFFAOYSA-N 0.000 description 1
- 210000004436 artificial bacterial chromosome Anatomy 0.000 description 1
- 210000001106 artificial yeast chromosome Anatomy 0.000 description 1
- 229940009098 aspartate Drugs 0.000 description 1
- 238000002820 assay format Methods 0.000 description 1
- 238000000376 autoradiography Methods 0.000 description 1
- 210000003719 b-lymphocyte Anatomy 0.000 description 1
- 244000052616 bacterial pathogen Species 0.000 description 1
- 239000010836 blood and blood product Substances 0.000 description 1
- 229940125691 blood product Drugs 0.000 description 1
- 238000005251 capillar electrophoresis Methods 0.000 description 1
- 238000005119 centrifugation Methods 0.000 description 1
- 239000013522 chelant Substances 0.000 description 1
- 239000003153 chemical reaction reagent Substances 0.000 description 1
- 238000004587 chromatography analysis Methods 0.000 description 1
- 239000010415 colloidal nanoparticle Substances 0.000 description 1
- 238000007398 colorimetric assay Methods 0.000 description 1
- 238000004440 column chromatography Methods 0.000 description 1
- 238000012875 competitive assay Methods 0.000 description 1
- 230000009137 competitive binding Effects 0.000 description 1
- 230000000536 complexating effect Effects 0.000 description 1
- 230000002153 concerted effect Effects 0.000 description 1
- 238000004624 confocal microscopy Methods 0.000 description 1
- 230000001268 conjugating effect Effects 0.000 description 1
- 239000000412 dendrimer Substances 0.000 description 1
- 229920000736 dendritic polymer Polymers 0.000 description 1
- 231100000676 disease causative agent Toxicity 0.000 description 1
- 229940051998 ehrlichia canis Drugs 0.000 description 1
- 238000001493 electron microscopy Methods 0.000 description 1
- 238000004520 electroporation Methods 0.000 description 1
- 239000003623 enhancer Substances 0.000 description 1
- 230000002255 enzymatic effect Effects 0.000 description 1
- 210000003527 eukaryotic cell Anatomy 0.000 description 1
- 239000011152 fibreglass Substances 0.000 description 1
- 238000000684 flow cytometry 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
- 238000001943 fluorescence-activated cell sorting Methods 0.000 description 1
- 239000007850 fluorescent dye Substances 0.000 description 1
- 238000005194 fractionation Methods 0.000 description 1
- 230000002538 fungal effect Effects 0.000 description 1
- 230000002496 gastric effect Effects 0.000 description 1
- 238000001502 gel electrophoresis Methods 0.000 description 1
- 230000002068 genetic effect Effects 0.000 description 1
- 229940116332 glucose oxidase Drugs 0.000 description 1
- 235000019420 glucose oxidase Nutrition 0.000 description 1
- 229930195712 glutamate Natural products 0.000 description 1
- 239000001963 growth medium Substances 0.000 description 1
- 230000035931 haemagglutination Effects 0.000 description 1
- 238000010820 immunofluorescence microscopy Methods 0.000 description 1
- 230000002163 immunogen Effects 0.000 description 1
- 229940072221 immunoglobulins Drugs 0.000 description 1
- 238000012744 immunostaining Methods 0.000 description 1
- 238000002955 isolation Methods 0.000 description 1
- 150000002632 lipids Chemical class 0.000 description 1
- 239000011159 matrix material Substances 0.000 description 1
- 230000000813 microbial effect Effects 0.000 description 1
- 238000001823 molecular biology technique Methods 0.000 description 1
- 238000010369 molecular cloning Methods 0.000 description 1
- 210000003097 mucus Anatomy 0.000 description 1
- 239000002105 nanoparticle Substances 0.000 description 1
- 108010087904 neutravidin Proteins 0.000 description 1
- 238000003199 nucleic acid amplification method Methods 0.000 description 1
- 239000002773 nucleotide Substances 0.000 description 1
- 125000003729 nucleotide group Chemical group 0.000 description 1
- 238000000399 optical microscopy Methods 0.000 description 1
- 238000007254 oxidation reaction Methods 0.000 description 1
- 239000000863 peptide conjugate Substances 0.000 description 1
- 239000012071 phase Substances 0.000 description 1
- 238000002264 polyacrylamide gel electrophoresis Methods 0.000 description 1
- 239000003755 preservative agent Substances 0.000 description 1
- 230000002335 preservative effect Effects 0.000 description 1
- 210000003705 ribosome Anatomy 0.000 description 1
- 150000003839 salts Chemical class 0.000 description 1
- 239000012488 sample solution Substances 0.000 description 1
- 238000012216 screening Methods 0.000 description 1
- 230000028327 secretion Effects 0.000 description 1
- 238000002864 sequence alignment Methods 0.000 description 1
- 239000013605 shuttle vector Substances 0.000 description 1
- 238000001542 size-exclusion chromatography Methods 0.000 description 1
- 235000020183 skimmed milk Nutrition 0.000 description 1
- 239000007790 solid phase Substances 0.000 description 1
- 229910052717 sulfur Inorganic materials 0.000 description 1
- 239000011593 sulfur Substances 0.000 description 1
- 238000013518 transcription Methods 0.000 description 1
- 230000035897 transcription Effects 0.000 description 1
- 230000002103 transcriptional effect Effects 0.000 description 1
- 238000001890 transfection Methods 0.000 description 1
- 238000012546 transfer Methods 0.000 description 1
- 230000001131 transforming effect Effects 0.000 description 1
- 238000013519 translation Methods 0.000 description 1
- 241000701161 unidentified adenovirus Species 0.000 description 1
- 241001515965 unidentified phage Species 0.000 description 1
- 241001430294 unidentified retrovirus Species 0.000 description 1
- 210000002700 urine Anatomy 0.000 description 1
- 238000011179 visual inspection Methods 0.000 description 1
- 238000012800 visualization Methods 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
- G01N33/543—Immunoassay; Biospecific binding assay; Materials therefor with an insoluble carrier for immobilising immunochemicals
- G01N33/54306—Solid-phase reaction mechanisms
-
- G—PHYSICS
- G01—MEASURING; TESTING
- G01N—INVESTIGATING OR ANALYSING MATERIALS BY DETERMINING THEIR CHEMICAL OR PHYSICAL PROPERTIES
- G01N33/00—Investigating or analysing materials by specific methods not covered by groups G01N1/00 - G01N31/00
- G01N33/48—Biological material, e.g. blood, urine; Haemocytometers
- G01N33/50—Chemical analysis of biological material, e.g. blood, urine; Testing involving biospecific ligand binding methods; Immunological testing
- G01N33/53—Immunoassay; Biospecific binding assay; Materials therefor
- G01N33/569—Immunoassay; Biospecific binding assay; Materials therefor for microorganisms, e.g. protozoa, bacteria, viruses
- G01N33/56911—Bacteria
-
- C—CHEMISTRY; METALLURGY
- C07—ORGANIC CHEMISTRY
- C07K—PEPTIDES
- C07K14/00—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof
- C07K14/195—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof from bacteria
-
- 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
- G01N33/543—Immunoassay; Biospecific binding assay; Materials therefor with an insoluble carrier for immobilising immunochemicals
- G01N33/54353—Immunoassay; Biospecific binding assay; Materials therefor with an insoluble carrier for immobilising immunochemicals with ligand attached to the carrier via a chemical coupling agent
-
- 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
- G01N33/543—Immunoassay; Biospecific binding assay; Materials therefor with an insoluble carrier for immobilising immunochemicals
- G01N33/54366—Apparatus specially adapted for solid-phase testing
-
- G—PHYSICS
- G01—MEASURING; TESTING
- G01N—INVESTIGATING OR ANALYSING MATERIALS BY DETERMINING THEIR CHEMICAL OR PHYSICAL PROPERTIES
- G01N2333/00—Assays involving biological materials from specific organisms or of a specific nature
- G01N2333/195—Assays involving biological materials from specific organisms or of a specific nature from bacteria
- G01N2333/29—Assays involving biological materials from specific organisms or of a specific nature from bacteria from Richettsiales (o)
-
- 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)
- Immunology (AREA)
- Engineering & Computer Science (AREA)
- Molecular Biology (AREA)
- Urology & Nephrology (AREA)
- Hematology (AREA)
- Biomedical Technology (AREA)
- Biochemistry (AREA)
- Medicinal Chemistry (AREA)
- General Health & Medical Sciences (AREA)
- Food Science & Technology (AREA)
- General Physics & Mathematics (AREA)
- Pathology (AREA)
- Analytical Chemistry (AREA)
- Physics & Mathematics (AREA)
- Biotechnology (AREA)
- Cell Biology (AREA)
- Microbiology (AREA)
- Organic Chemistry (AREA)
- Tropical Medicine & Parasitology (AREA)
- Virology (AREA)
- Proteomics, Peptides & Aminoacids (AREA)
- Gastroenterology & Hepatology (AREA)
- Genetics & Genomics (AREA)
- Biophysics (AREA)
- Chemical Kinetics & Catalysis (AREA)
- Peptides Or Proteins (AREA)
- Investigating Or Analysing Biological Materials (AREA)
Applications Claiming Priority (3)
| Application Number | Priority Date | Filing Date | Title |
|---|---|---|---|
| US263329P | 2001-01-19 | ||
| US26332909P | 2009-11-20 | 2009-11-20 | |
| PCT/US2010/057430 WO2011063235A2 (en) | 2009-11-20 | 2010-11-19 | Peptides, devices, and methods for the detection of ehrlichia antibodies |
Publications (1)
| Publication Number | Publication Date |
|---|---|
| ES2596952T3 true ES2596952T3 (es) | 2017-01-13 |
Family
ID=44060369
Family Applications (1)
| Application Number | Title | Priority Date | Filing Date |
|---|---|---|---|
| ES10832262.9T Active ES2596952T3 (es) | 2009-11-20 | 2010-11-19 | Péptidos, dispositivos y procedimientos para la detección de anticuerpos de Ehrlichia |
Country Status (9)
| Country | Link |
|---|---|
| US (2) | US8828675B2 (enExample) |
| EP (1) | EP2501718B1 (enExample) |
| JP (2) | JP6161291B2 (enExample) |
| KR (1) | KR101892182B1 (enExample) |
| CN (2) | CN102834411B (enExample) |
| AU (1) | AU2010321790B2 (enExample) |
| CA (1) | CA2781117C (enExample) |
| ES (1) | ES2596952T3 (enExample) |
| WO (1) | WO2011063235A2 (enExample) |
Families Citing this family (15)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| CA2781117C (en) | 2009-11-20 | 2019-05-28 | Abaxis, Inc. | Peptides, devices, and methods for the detection of ehrlichia antibodies |
| DK3489685T3 (da) | 2011-11-21 | 2023-12-04 | Zoetis Services Llc | Signalforstærkning i sidestrømning og tilsvarende immunoassays |
| ES2668863T3 (es) | 2012-10-11 | 2018-05-22 | Abaxis, Inc. | Péptidos, dispositivos y métodos para la detección de anticuerpos de Ehrlichia |
| US9194870B2 (en) | 2014-01-21 | 2015-11-24 | Abaxis, Inc. | Peptides, devices, and methods for the detection of Anaplasma antibodies |
| US9442112B2 (en) * | 2014-04-04 | 2016-09-13 | Abaxis, Inc. | Compositions and methods for identifying Ehrlichia species |
| TWI691716B (zh) | 2014-08-13 | 2020-04-21 | 美商艾巴希斯公司 | 電漿特異性結合搭配物檢定中之信號放大 |
| CN104360058A (zh) * | 2014-08-18 | 2015-02-18 | 石河子大学 | 一种新型检测人布鲁氏菌病抗体的免疫层析试纸及制备方法 |
| EP4465021A3 (en) | 2015-08-04 | 2025-02-26 | Zoetis Services LLC | Signal amplification in solution-based plasmonic specific-binding partner assays |
| KR102486615B1 (ko) | 2017-01-30 | 2023-01-11 | 조에티스 서비시즈 엘엘씨 | 용액-기반 플라스몬 특이적-결합 파트너 검정 및 금속성 나노구조체 |
| JP2018128408A (ja) * | 2017-02-10 | 2018-08-16 | 東ソー株式会社 | 抗体凝集体形成予測方法 |
| US20180287426A1 (en) * | 2017-03-30 | 2018-10-04 | Qualcomm Incorporated | Wireless power time division transmitter and coil array |
| US20190309422A1 (en) | 2018-04-06 | 2019-10-10 | Versum Materials Us, Llc | Spin-On Metallization |
| EP4226164A4 (en) * | 2020-10-08 | 2024-10-30 | Controlpoint Inc. | Methods and apparatuses for detecting respiratory infections |
| CN116735872B (zh) * | 2020-12-14 | 2025-12-05 | 杭州亿米诺生物科技有限公司 | 一种用于检测犬埃里希体抗体的试剂盒 |
| EP4220166A1 (en) | 2022-02-01 | 2023-08-02 | Universitat Rovira I Virgili (URV) | In vitro method for detecting antibodies in a sample |
Family Cites Families (36)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| US4366246A (en) | 1977-11-08 | 1982-12-28 | Genentech, Inc. | Method for microbial polypeptide expression |
| US6593147B1 (en) | 1996-10-17 | 2003-07-15 | University Of Florida Research Foundation, Inc. | Nucleic acid vaccines against rickettsial diseases and methods of use |
| US6653128B2 (en) * | 1996-10-17 | 2003-11-25 | University Of Florida | Nucleic acid vaccines against rickettsial diseases and methods of use |
| US6207169B1 (en) * | 1997-03-21 | 2001-03-27 | Corixa Corporation | Compounds and methods for the diagnosis and treatment of Ehrlichia infection |
| US6231869B1 (en) * | 1997-03-21 | 2001-05-15 | Corixa Corporation | Compounds and methods for the diagnosis and treatment of ehrlichia infection |
| AU7256398A (en) * | 1997-04-25 | 1998-11-24 | Aquila Biopharmaceuticals, Inc. | Characterization of granulocytic ehrlichia and methods of use |
| EP1026949B1 (en) | 1997-09-19 | 2010-09-15 | The Ohio State University Research Foundation | Outer membrane proteins of ehrlichia chaffeensis |
| US6043085A (en) * | 1998-08-27 | 2000-03-28 | Research Development Foundation | Ehrlichia canis 120-kDa immunodominant antigenic protein and gene |
| US6893640B2 (en) * | 1998-09-18 | 2005-05-17 | The Ohio State University Research Foundation | Outer membrane protein of Ehrlichia canis and Ehrlichia chaffeensis |
| US7888491B2 (en) * | 1998-09-18 | 2011-02-15 | The Ohio State University Research Foundation | Outer membrane protein of Ehrlichia canis and Ehrlichia chaffeensis |
| US6544517B1 (en) * | 1998-09-18 | 2003-04-08 | The Ohio State University Research Foundation | Outer membrane protein of Ehrlichia canis and Ehrlichia chaffeensis |
| US6392023B1 (en) * | 1999-03-03 | 2002-05-21 | Research Development Foundation | Homologous 28-kilodalton immunodominant protein genes of Ehrlicha canis and uses thereof |
| IL147733A0 (en) * | 1999-07-21 | 2002-08-14 | Cornell Res Foundation Inc | Ehrlichia canis genes and vaccines |
| US6355777B1 (en) | 2000-04-28 | 2002-03-12 | Research Development Foundation | P43 antigen for the immunodiagnosis of canine ehrlichiosis and uses thereof |
| US7183060B2 (en) * | 2005-02-22 | 2007-02-27 | Idexx Laboratories, Inc. | Peptides for detection of antibody to Ehrlichia ewingii |
| US20030194756A1 (en) * | 2002-04-12 | 2003-10-16 | O'connor Thomas Patrick | Peptides for detection of antibody to Ehrlichia equi |
| US7087372B2 (en) * | 2001-01-18 | 2006-08-08 | Idexx Laboratories, Inc. | Compositions and methods for detection of Ehrlichia canis and Ehrlichia chaffeensis antibodies |
| US7407770B2 (en) * | 2001-01-18 | 2008-08-05 | Idexx Corporation | Compositions and methods for detection of Ehrlichia canis and Ehrlichia chaffeensis antibodies |
| CA2442074C (en) * | 2001-03-28 | 2014-07-22 | Heska Corporation | Methods of detecting early renal disease in animals |
| US20030129161A1 (en) * | 2001-09-17 | 2003-07-10 | Hsien-Jue Chu | Interleukin-12 as a veterinary vaccine adjuvant |
| EP1581638B1 (en) | 2002-11-04 | 2007-09-05 | Research Development Foundation | P153 and p156 antigens for the immunodiagnosis of canine and human ehrlichioses and uses thereof |
| WO2004084841A2 (en) * | 2003-03-27 | 2004-10-07 | Heska Corporation | Novel anti-feline albumin antibodies and methods of detecting early renal disease |
| US7304139B2 (en) * | 2003-10-28 | 2007-12-04 | University Of Florida Research Foundation, Inc. | Polynucleotides and polypeptides of Anaplasma phagocytophilum and methods of using the same |
| US20060046310A1 (en) | 2004-08-25 | 2006-03-02 | Zong-Li Xia | Amplification method for solid phase immunoassays |
| US7842473B2 (en) * | 2005-04-04 | 2010-11-30 | Idexx Laboratories, Inc. | Ehrlichia canis DIVA (differentiate infected from vaccinated animals) |
| US7842474B2 (en) * | 2005-04-04 | 2010-11-30 | Idexx Laboratories, Inc. | Ehrlichia canis DIVA (differentiate infected from vaccinated animals) |
| MX2007016189A (es) | 2005-06-16 | 2008-03-10 | Res Dev Foundation | Ortologos de proteinas inmunoreactivas de ehrlichia canis y e. chaffeensis. |
| US20090176208A1 (en) * | 2006-01-04 | 2009-07-09 | Simon Brodie | Methods for detecting, identifying and reporting the presence of animal pathological agents |
| US7776618B2 (en) | 2007-03-01 | 2010-08-17 | Church & Dwight Co., Inc. | Diagnostic detection device |
| US7507789B2 (en) * | 2007-04-09 | 2009-03-24 | Idexx Laboratories, Inc. | Detection of Anaplasma platys |
| WO2008137881A2 (en) | 2007-05-04 | 2008-11-13 | The Ohio State University Research Foundation | Ehrlichia ewingii proteins, nucleic acids, and methods of their use |
| CA2700474C (en) * | 2007-09-21 | 2016-10-04 | Idexx Laboratories, Inc. | Methods and compositions for detection of ehrlichia chaffeensis (p120) |
| US7964366B2 (en) * | 2007-09-21 | 2011-06-21 | Idexx Laboratories, Inc. | Methods and compositions for detection of Ehrlichia chaffeensis (VLPT) |
| EP3527221B1 (en) * | 2007-10-31 | 2022-02-23 | Idexx Laboratories, Inc. | Ehrlichia canis diva (differentiate infected from vaccinated animals) |
| CA2781117C (en) | 2009-11-20 | 2019-05-28 | Abaxis, Inc. | Peptides, devices, and methods for the detection of ehrlichia antibodies |
| ES2668863T3 (es) | 2012-10-11 | 2018-05-22 | Abaxis, Inc. | Péptidos, dispositivos y métodos para la detección de anticuerpos de Ehrlichia |
-
2010
- 2010-11-19 CA CA2781117A patent/CA2781117C/en active Active
- 2010-11-19 ES ES10832262.9T patent/ES2596952T3/es active Active
- 2010-11-19 JP JP2012540090A patent/JP6161291B2/ja active Active
- 2010-11-19 CN CN201080061669.1A patent/CN102834411B/zh active Active
- 2010-11-19 US US12/950,707 patent/US8828675B2/en active Active
- 2010-11-19 WO PCT/US2010/057430 patent/WO2011063235A2/en not_active Ceased
- 2010-11-19 EP EP10832262.9A patent/EP2501718B1/en active Active
- 2010-11-19 KR KR1020127015476A patent/KR101892182B1/ko active Active
- 2010-11-19 AU AU2010321790A patent/AU2010321790B2/en active Active
- 2010-11-19 CN CN201510582480.1A patent/CN105203755B/zh active Active
-
2014
- 2014-08-01 US US14/450,154 patent/US9470682B2/en active Active
-
2016
- 2016-04-04 JP JP2016075063A patent/JP2016175908A/ja active Pending
Also Published As
| Publication number | Publication date |
|---|---|
| EP2501718A4 (en) | 2014-02-19 |
| WO2011063235A3 (en) | 2011-10-13 |
| EP2501718B1 (en) | 2016-07-27 |
| US8828675B2 (en) | 2014-09-09 |
| JP2016175908A (ja) | 2016-10-06 |
| EP2501718A2 (en) | 2012-09-26 |
| CA2781117A1 (en) | 2011-05-26 |
| US20110124125A1 (en) | 2011-05-26 |
| CN105203755A (zh) | 2015-12-30 |
| CA2781117C (en) | 2019-05-28 |
| WO2011063235A2 (en) | 2011-05-26 |
| CN105203755B (zh) | 2018-01-05 |
| KR20120117778A (ko) | 2012-10-24 |
| US20150024417A1 (en) | 2015-01-22 |
| AU2010321790A1 (en) | 2012-07-05 |
| CN102834411B (zh) | 2015-10-21 |
| JP2013511546A (ja) | 2013-04-04 |
| JP6161291B2 (ja) | 2017-07-12 |
| AU2010321790B2 (en) | 2016-08-04 |
| CN102834411A (zh) | 2012-12-19 |
| KR101892182B1 (ko) | 2018-08-24 |
| US9470682B2 (en) | 2016-10-18 |
Similar Documents
| Publication | Publication Date | Title |
|---|---|---|
| ES2596952T3 (es) | Péptidos, dispositivos y procedimientos para la detección de anticuerpos de Ehrlichia | |
| ES2967710T3 (es) | Péptidos y procedimientos para la detección de anticuerpos contra la enfermedad de Lyme | |
| US10948487B2 (en) | Peptides, devices, and methods for the detection of Ehrlichia antibodies | |
| US20110136155A1 (en) | Peptides and methods for the detection of lyme disease antibodies | |
| ES2767183T3 (es) | Péptidos, dispositivos y procedimientos para la detección de anticuerpos de Anaplasma |