DK172619B1 - Fremgangsmåde til isolering af immunogene præparater af herpes simplex virus type 1 og type 2, fremgangsmåde til fremstill - Google Patents
Fremgangsmåde til isolering af immunogene præparater af herpes simplex virus type 1 og type 2, fremgangsmåde til fremstill Download PDFInfo
- Publication number
- DK172619B1 DK172619B1 DK198304790A DK479083A DK172619B1 DK 172619 B1 DK172619 B1 DK 172619B1 DK 198304790 A DK198304790 A DK 198304790A DK 479083 A DK479083 A DK 479083A DK 172619 B1 DK172619 B1 DK 172619B1
- Authority
- DK
- Denmark
- Prior art keywords
- amino acid
- herpes simplex
- simplex virus
- asp
- leu
- Prior art date
Links
- 238000000034 method Methods 0.000 title claims description 64
- 238000002360 preparation method Methods 0.000 title claims description 44
- 241000700588 Human alphaherpesvirus 1 Species 0.000 title claims description 42
- 241000701074 Human alphaherpesvirus 2 Species 0.000 title claims description 11
- 230000002163 immunogen Effects 0.000 title claims description 10
- 241000700584 Simplexvirus Species 0.000 claims description 62
- 108090000288 Glycoproteins Proteins 0.000 claims description 53
- 102000003886 Glycoproteins Human genes 0.000 claims description 53
- 108090000765 processed proteins & peptides Proteins 0.000 claims description 48
- 102000004196 processed proteins & peptides Human genes 0.000 claims description 41
- 229920001184 polypeptide Polymers 0.000 claims description 39
- 150000001413 amino acids Chemical class 0.000 claims description 27
- 125000003275 alpha amino acid group Chemical group 0.000 claims description 21
- 125000000539 amino acid group Chemical group 0.000 claims description 21
- 239000012634 fragment Substances 0.000 claims description 19
- 230000028993 immune response Effects 0.000 claims description 18
- 208000037265 diseases, disorders, signs and symptoms Diseases 0.000 claims description 17
- 201000010099 disease Diseases 0.000 claims description 16
- 238000002255 vaccination Methods 0.000 claims description 13
- 239000012530 fluid Substances 0.000 claims description 12
- 101710121417 Envelope glycoprotein Proteins 0.000 claims description 11
- 239000007788 liquid Substances 0.000 claims description 10
- 229910052739 hydrogen Inorganic materials 0.000 claims description 9
- 239000001257 hydrogen Substances 0.000 claims description 9
- 125000004435 hydrogen atom Chemical group [H]* 0.000 claims description 9
- 125000002887 hydroxy group Chemical group [H]O* 0.000 claims description 8
- 238000009739 binding Methods 0.000 claims description 7
- 239000000032 diagnostic agent Substances 0.000 claims description 7
- 229940039227 diagnostic agent Drugs 0.000 claims description 7
- 230000002441 reversible effect Effects 0.000 claims description 7
- 238000002955 isolation Methods 0.000 claims description 6
- 238000001514 detection method Methods 0.000 claims description 5
- 238000010668 complexation reaction Methods 0.000 claims description 4
- 238000010494 dissociation reaction Methods 0.000 claims description 4
- 230000005593 dissociations Effects 0.000 claims description 4
- 108010003533 Viral Envelope Proteins Proteins 0.000 claims description 3
- 239000002253 acid Substances 0.000 claims description 2
- 102100021696 Syncytin-1 Human genes 0.000 claims 4
- 210000004027 cell Anatomy 0.000 description 44
- 229960005486 vaccine Drugs 0.000 description 40
- 108090000623 proteins and genes Proteins 0.000 description 31
- 208000015181 infectious disease Diseases 0.000 description 30
- 235000018102 proteins Nutrition 0.000 description 30
- 102000004169 proteins and genes Human genes 0.000 description 30
- 241001465754 Metazoa Species 0.000 description 28
- 241000700605 Viruses Species 0.000 description 28
- 235000001014 amino acid Nutrition 0.000 description 26
- 229940024606 amino acid Drugs 0.000 description 26
- 210000002966 serum Anatomy 0.000 description 26
- 101100016593 Encephalitozoon cuniculi (strain GB-M1) HD-1 gene Proteins 0.000 description 21
- FAPWRFPIFSIZLT-UHFFFAOYSA-M Sodium chloride Chemical compound [Na+].[Cl-] FAPWRFPIFSIZLT-UHFFFAOYSA-M 0.000 description 21
- 230000000694 effects Effects 0.000 description 20
- 239000000203 mixture Substances 0.000 description 20
- 239000000427 antigen Substances 0.000 description 17
- 102000036639 antigens Human genes 0.000 description 17
- 108091007433 antigens Proteins 0.000 description 17
- ROHFNLRQFUQHCH-YFKPBYRVSA-N L-leucine Chemical compound CC(C)C[C@H](N)C(O)=O ROHFNLRQFUQHCH-YFKPBYRVSA-N 0.000 description 16
- 230000003472 neutralizing effect Effects 0.000 description 16
- 238000004458 analytical method Methods 0.000 description 15
- 230000001086 cytosolic effect Effects 0.000 description 15
- 239000000284 extract Substances 0.000 description 15
- 241000699670 Mus sp. Species 0.000 description 13
- 230000000890 antigenic effect Effects 0.000 description 13
- 230000001900 immune effect Effects 0.000 description 12
- 238000000746 purification Methods 0.000 description 11
- 239000000523 sample Substances 0.000 description 11
- 102100038132 Endogenous retrovirus group K member 6 Pro protein Human genes 0.000 description 10
- 230000015572 biosynthetic process Effects 0.000 description 10
- 229960004452 methionine Drugs 0.000 description 10
- ROHFNLRQFUQHCH-UHFFFAOYSA-N Leucine Natural products CC(C)CC(N)C(O)=O ROHFNLRQFUQHCH-UHFFFAOYSA-N 0.000 description 9
- 238000002372 labelling Methods 0.000 description 9
- 238000003156 radioimmunoprecipitation Methods 0.000 description 9
- 239000004475 Arginine Substances 0.000 description 8
- FFEARJCKVFRZRR-BYPYZUCNSA-N L-methionine Chemical compound CSCC[C@H](N)C(O)=O FFEARJCKVFRZRR-BYPYZUCNSA-N 0.000 description 8
- 238000003556 assay Methods 0.000 description 8
- 230000015556 catabolic process Effects 0.000 description 8
- 238000010790 dilution Methods 0.000 description 8
- 239000012895 dilution Substances 0.000 description 8
- 238000000338 in vitro Methods 0.000 description 8
- 238000004519 manufacturing process Methods 0.000 description 8
- 229930182817 methionine Natural products 0.000 description 8
- 238000006386 neutralization reaction Methods 0.000 description 8
- 230000001681 protective effect Effects 0.000 description 8
- 239000011780 sodium chloride Substances 0.000 description 8
- 238000002415 sodium dodecyl sulfate polyacrylamide gel electrophoresis Methods 0.000 description 8
- 125000003295 alanine group Chemical group N[C@@H](C)C(=O)* 0.000 description 7
- ODKSFYDXXFIFQN-UHFFFAOYSA-N arginine Natural products OC(=O)C(N)CCCNC(N)=N ODKSFYDXXFIFQN-UHFFFAOYSA-N 0.000 description 7
- 238000005755 formation reaction Methods 0.000 description 7
- 210000004379 membrane Anatomy 0.000 description 7
- 239000012528 membrane Substances 0.000 description 7
- 125000001360 methionine group Chemical group N[C@@H](CCSC)C(=O)* 0.000 description 7
- 241001529453 unidentified herpesvirus Species 0.000 description 7
- 230000003612 virological effect Effects 0.000 description 7
- CSCPPACGZOOCGX-UHFFFAOYSA-N Acetone Chemical compound CC(C)=O CSCPPACGZOOCGX-UHFFFAOYSA-N 0.000 description 6
- 108020004414 DNA Proteins 0.000 description 6
- 241000282412 Homo Species 0.000 description 6
- 241000699666 Mus <mouse, genus> Species 0.000 description 6
- 239000002671 adjuvant Substances 0.000 description 6
- 230000027455 binding Effects 0.000 description 6
- 238000002474 experimental method Methods 0.000 description 6
- 230000003053 immunization Effects 0.000 description 6
- 239000003547 immunosorbent Substances 0.000 description 6
- 239000002245 particle Substances 0.000 description 6
- YBYRMVIVWMBXKQ-UHFFFAOYSA-N phenylmethanesulfonyl fluoride Chemical compound FS(=O)(=O)CC1=CC=CC=C1 YBYRMVIVWMBXKQ-UHFFFAOYSA-N 0.000 description 6
- 239000000047 product Substances 0.000 description 6
- 230000002285 radioactive effect Effects 0.000 description 6
- XLYOFNOQVPJJNP-UHFFFAOYSA-N water Chemical compound O XLYOFNOQVPJJNP-UHFFFAOYSA-N 0.000 description 6
- 208000009889 Herpes Simplex Diseases 0.000 description 5
- VEXZGXHMUGYJMC-UHFFFAOYSA-N Hydrochloric acid Chemical compound Cl VEXZGXHMUGYJMC-UHFFFAOYSA-N 0.000 description 5
- QNAYBMKLOCPYGJ-REOHCLBHSA-N L-alanine Chemical compound C[C@H](N)C(O)=O QNAYBMKLOCPYGJ-REOHCLBHSA-N 0.000 description 5
- ODKSFYDXXFIFQN-BYPYZUCNSA-P L-argininium(2+) Chemical compound NC(=[NH2+])NCCC[C@H]([NH3+])C(O)=O ODKSFYDXXFIFQN-BYPYZUCNSA-P 0.000 description 5
- KDXKERNSBIXSRK-YFKPBYRVSA-N L-lysine Chemical compound NCCCC[C@H](N)C(O)=O KDXKERNSBIXSRK-YFKPBYRVSA-N 0.000 description 5
- 208000035415 Reinfection Diseases 0.000 description 5
- 239000007983 Tris buffer Substances 0.000 description 5
- 235000004279 alanine Nutrition 0.000 description 5
- 231100000518 lethal Toxicity 0.000 description 5
- 230000001665 lethal effect Effects 0.000 description 5
- 239000002609 medium Substances 0.000 description 5
- 150000007523 nucleic acids Chemical class 0.000 description 5
- ZNNZYHKDIALBAK-UHFFFAOYSA-M potassium thiocyanate Chemical compound [K+].[S-]C#N ZNNZYHKDIALBAK-UHFFFAOYSA-M 0.000 description 5
- 239000002243 precursor Substances 0.000 description 5
- 238000012360 testing method Methods 0.000 description 5
- YNJBWRMUSHSURL-UHFFFAOYSA-N trichloroacetic acid Chemical compound OC(=O)C(Cl)(Cl)Cl YNJBWRMUSHSURL-UHFFFAOYSA-N 0.000 description 5
- 206010003445 Ascites Diseases 0.000 description 4
- 101800000594 Capsid protein 1 Proteins 0.000 description 4
- 239000004472 Lysine Substances 0.000 description 4
- KDXKERNSBIXSRK-UHFFFAOYSA-N Lysine Natural products NCCCCC(N)C(O)=O KDXKERNSBIXSRK-UHFFFAOYSA-N 0.000 description 4
- 101800000838 Neutrophil cationic peptide 1 Proteins 0.000 description 4
- 241000283973 Oryctolagus cuniculus Species 0.000 description 4
- 125000000613 asparagine group Chemical group N[C@@H](CC(N)=O)C(=O)* 0.000 description 4
- 230000000903 blocking effect Effects 0.000 description 4
- 239000000872 buffer Substances 0.000 description 4
- 150000001720 carbohydrates Chemical class 0.000 description 4
- 238000004587 chromatography analysis Methods 0.000 description 4
- 125000000151 cysteine group Chemical group N[C@@H](CS)C(=O)* 0.000 description 4
- 230000036039 immunity Effects 0.000 description 4
- 238000002649 immunization Methods 0.000 description 4
- 238000001727 in vivo Methods 0.000 description 4
- 239000007924 injection Substances 0.000 description 4
- 238000002347 injection Methods 0.000 description 4
- 238000011081 inoculation Methods 0.000 description 4
- 230000004048 modification Effects 0.000 description 4
- 238000012986 modification Methods 0.000 description 4
- 108020004707 nucleic acids Proteins 0.000 description 4
- 102000039446 nucleic acids Human genes 0.000 description 4
- 230000009257 reactivity Effects 0.000 description 4
- 230000000306 recurrent effect Effects 0.000 description 4
- 230000004044 response Effects 0.000 description 4
- LENZDBCJOHFCAS-UHFFFAOYSA-N tris Chemical compound OCC(N)(CO)CO LENZDBCJOHFCAS-UHFFFAOYSA-N 0.000 description 4
- 108091032973 (ribonucleotides)n+m Proteins 0.000 description 3
- 102000014914 Carrier Proteins Human genes 0.000 description 3
- 108010078791 Carrier Proteins Proteins 0.000 description 3
- 208000035473 Communicable disease Diseases 0.000 description 3
- 102000004190 Enzymes Human genes 0.000 description 3
- 108090000790 Enzymes Proteins 0.000 description 3
- XEKOWRVHYACXOJ-UHFFFAOYSA-N Ethyl acetate Chemical compound CCOC(C)=O XEKOWRVHYACXOJ-UHFFFAOYSA-N 0.000 description 3
- DHMQDGOQFOQNFH-UHFFFAOYSA-N Glycine Chemical compound NCC(O)=O DHMQDGOQFOQNFH-UHFFFAOYSA-N 0.000 description 3
- XQFRJNBWHJMXHO-RRKCRQDMSA-N IDUR Chemical compound C1[C@H](O)[C@@H](CO)O[C@H]1N1C(=O)NC(=O)C(I)=C1 XQFRJNBWHJMXHO-RRKCRQDMSA-N 0.000 description 3
- 108091028043 Nucleic acid sequence Proteins 0.000 description 3
- 229920002684 Sepharose Polymers 0.000 description 3
- HEMHJVSKTPXQMS-UHFFFAOYSA-M Sodium hydroxide Chemical compound [OH-].[Na+] HEMHJVSKTPXQMS-UHFFFAOYSA-M 0.000 description 3
- 229940037003 alum Drugs 0.000 description 3
- 238000010171 animal model Methods 0.000 description 3
- 125000000637 arginyl group Chemical group N[C@@H](CCCNC(N)=N)C(=O)* 0.000 description 3
- 230000002238 attenuated effect Effects 0.000 description 3
- 210000001124 body fluid Anatomy 0.000 description 3
- 239000010839 body fluid Substances 0.000 description 3
- 244000309464 bull Species 0.000 description 3
- 235000014633 carbohydrates Nutrition 0.000 description 3
- 238000006243 chemical reaction Methods 0.000 description 3
- 235000018417 cysteine Nutrition 0.000 description 3
- XUJNEKJLAYXESH-UHFFFAOYSA-N cysteine Natural products SCC(N)C(O)=O XUJNEKJLAYXESH-UHFFFAOYSA-N 0.000 description 3
- 230000034994 death Effects 0.000 description 3
- 238000006731 degradation reaction Methods 0.000 description 3
- 239000003599 detergent Substances 0.000 description 3
- 238000000502 dialysis Methods 0.000 description 3
- 239000003085 diluting agent Substances 0.000 description 3
- 230000001747 exhibiting effect Effects 0.000 description 3
- 230000004927 fusion Effects 0.000 description 3
- 239000000499 gel Substances 0.000 description 3
- 210000004408 hybridoma Anatomy 0.000 description 3
- 239000012133 immunoprecipitate Substances 0.000 description 3
- 238000010348 incorporation Methods 0.000 description 3
- 230000026045 iodination Effects 0.000 description 3
- 238000006192 iodination reaction Methods 0.000 description 3
- 239000002244 precipitate Substances 0.000 description 3
- 230000002265 prevention Effects 0.000 description 3
- 238000010814 radioimmunoprecipitation assay Methods 0.000 description 3
- 230000009467 reduction Effects 0.000 description 3
- 238000012163 sequencing technique Methods 0.000 description 3
- 125000003607 serino group Chemical group [H]N([H])[C@]([H])(C(=O)[*])C(O[H])([H])[H] 0.000 description 3
- 229940031626 subunit vaccine Drugs 0.000 description 3
- 238000003786 synthesis reaction Methods 0.000 description 3
- 229940126577 synthetic vaccine Drugs 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
- HZAXFHJVJLSVMW-UHFFFAOYSA-N 2-Aminoethan-1-ol Chemical compound NCCO HZAXFHJVJLSVMW-UHFFFAOYSA-N 0.000 description 2
- HCZXHQADHZIEJD-CIUDSAMLSA-N Ala-Leu-Ala Chemical compound C[C@H](N)C(=O)N[C@@H](CC(C)C)C(=O)N[C@@H](C)C(O)=O HCZXHQADHZIEJD-CIUDSAMLSA-N 0.000 description 2
- DCXYFEDJOCDNAF-UHFFFAOYSA-N Asparagine Natural products OC(=O)C(N)CC(N)=O DCXYFEDJOCDNAF-UHFFFAOYSA-N 0.000 description 2
- WSFSSNUMVMOOMR-UHFFFAOYSA-N Formaldehyde Chemical compound O=C WSFSSNUMVMOOMR-UHFFFAOYSA-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
- 108010076504 Protein Sorting Signals Proteins 0.000 description 2
- MTCFGRXMJLQNBG-UHFFFAOYSA-N Serine Natural products OCC(N)C(O)=O MTCFGRXMJLQNBG-UHFFFAOYSA-N 0.000 description 2
- CDBYLPFSWZWCQE-UHFFFAOYSA-L Sodium Carbonate Chemical compound [Na+].[Na+].[O-]C([O-])=O CDBYLPFSWZWCQE-UHFFFAOYSA-L 0.000 description 2
- 230000024932 T cell mediated immunity Effects 0.000 description 2
- 241000029668 Uriurana virus Species 0.000 description 2
- 108020005202 Viral DNA Proteins 0.000 description 2
- 229960001230 asparagine Drugs 0.000 description 2
- 235000009582 asparagine Nutrition 0.000 description 2
- 230000009286 beneficial effect Effects 0.000 description 2
- 230000004071 biological effect Effects 0.000 description 2
- 125000003178 carboxy group Chemical group [H]OC(*)=O 0.000 description 2
- 210000000170 cell membrane Anatomy 0.000 description 2
- 108091092356 cellular DNA Proteins 0.000 description 2
- 239000003795 chemical substances by application Substances 0.000 description 2
- VDQQXEISLMTGAB-UHFFFAOYSA-N chloramine T Chemical compound [Na+].CC1=CC=C(S(=O)(=O)[N-]Cl)C=C1 VDQQXEISLMTGAB-UHFFFAOYSA-N 0.000 description 2
- 210000000805 cytoplasm Anatomy 0.000 description 2
- 238000011161 development Methods 0.000 description 2
- 238000001914 filtration Methods 0.000 description 2
- 239000012737 fresh medium Substances 0.000 description 2
- 210000000609 ganglia Anatomy 0.000 description 2
- 230000013595 glycosylation Effects 0.000 description 2
- 238000006206 glycosylation reaction Methods 0.000 description 2
- 230000005802 health problem Effects 0.000 description 2
- 210000000987 immune system Anatomy 0.000 description 2
- 238000001114 immunoprecipitation Methods 0.000 description 2
- 230000006872 improvement Effects 0.000 description 2
- 230000002401 inhibitory effect Effects 0.000 description 2
- 238000007912 intraperitoneal administration Methods 0.000 description 2
- 125000003588 lysine group Chemical group [H]N([H])C([H])([H])C([H])([H])C([H])([H])C([H])([H])C([H])(N([H])[H])C(*)=O 0.000 description 2
- 239000000463 material Substances 0.000 description 2
- 238000001466 metabolic labeling Methods 0.000 description 2
- SVOIKXSQIWJDHA-HNNXBMFYSA-N n-[(2s)-5-chloro-3,4-dioxo-1-phenylpentan-2-yl]-2-methylbenzenesulfonamide Chemical compound CC1=CC=CC=C1S(=O)(=O)N[C@H](C(=O)C(=O)CCl)CC1=CC=CC=C1 SVOIKXSQIWJDHA-HNNXBMFYSA-N 0.000 description 2
- 231100000590 oncogenic Toxicity 0.000 description 2
- 230000002246 oncogenic effect Effects 0.000 description 2
- -1 phenylethyl ethyl sulfonyl fluoride Chemical compound 0.000 description 2
- 230000007505 plaque formation Effects 0.000 description 2
- 125000002924 primary amino group Chemical group [H]N([H])* 0.000 description 2
- 125000001500 prolyl group Chemical group [H]N1C([H])(C(=O)[*])C([H])([H])C([H])([H])C1([H])[H] 0.000 description 2
- 238000011084 recovery Methods 0.000 description 2
- 239000000243 solution Substances 0.000 description 2
- 238000001179 sorption measurement Methods 0.000 description 2
- 210000000278 spinal cord Anatomy 0.000 description 2
- 239000000126 substance Substances 0.000 description 2
- 239000004094 surface-active agent Substances 0.000 description 2
- 239000013598 vector Substances 0.000 description 2
- 230000009385 viral infection Effects 0.000 description 2
- 210000000605 viral structure Anatomy 0.000 description 2
- 239000011534 wash buffer Substances 0.000 description 2
- AUXMWYRZQPIXCC-KNIFDHDWSA-N (2s)-2-amino-4-methylpentanoic acid;(2s)-2-aminopropanoic acid Chemical compound C[C@H](N)C(O)=O.CC(C)C[C@H](N)C(O)=O AUXMWYRZQPIXCC-KNIFDHDWSA-N 0.000 description 1
- ODKSFYDXXFIFQN-JQZHSJCGSA-N (2s)-2-amino-5-(diaminomethylideneamino)-2,3-ditritiopentanoic acid Chemical compound OC(=O)[C@@]([3H])(N)C([3H])CCN=C(N)N ODKSFYDXXFIFQN-JQZHSJCGSA-N 0.000 description 1
- HNSDLXPSAYFUHK-UHFFFAOYSA-N 1,4-bis(2-ethylhexyl) sulfosuccinate Chemical compound CCCCC(CC)COC(=O)CC(S(O)(=O)=O)C(=O)OCC(CC)CCCC HNSDLXPSAYFUHK-UHFFFAOYSA-N 0.000 description 1
- VZSRBBMJRBPUNF-UHFFFAOYSA-N 2-(2,3-dihydro-1H-inden-2-ylamino)-N-[3-oxo-3-(2,4,6,7-tetrahydrotriazolo[4,5-c]pyridin-5-yl)propyl]pyrimidine-5-carboxamide Chemical compound C1C(CC2=CC=CC=C12)NC1=NC=C(C=N1)C(=O)NCCC(N1CC2=C(CC1)NN=N2)=O VZSRBBMJRBPUNF-UHFFFAOYSA-N 0.000 description 1
- LJGHYPLBDBRCRZ-UHFFFAOYSA-N 3-(3-aminophenyl)sulfonylaniline Chemical compound NC1=CC=CC(S(=O)(=O)C=2C=C(N)C=CC=2)=C1 LJGHYPLBDBRCRZ-UHFFFAOYSA-N 0.000 description 1
- HRPVXLWXLXDGHG-UHFFFAOYSA-N Acrylamide Chemical compound NC(=O)C=C HRPVXLWXLXDGHG-UHFFFAOYSA-N 0.000 description 1
- YSMPVONNIWLJML-FXQIFTODSA-N Ala-Asp-Pro Chemical compound C[C@H](N)C(=O)N[C@@H](CC(O)=O)C(=O)N1CCC[C@H]1C(O)=O YSMPVONNIWLJML-FXQIFTODSA-N 0.000 description 1
- HUZGPXBILPMCHM-IHRRRGAJSA-N Asn-Arg-Phe Chemical compound [H]N[C@@H](CC(N)=O)C(=O)N[C@@H](CCCNC(N)=N)C(=O)N[C@@H](CC1=CC=CC=C1)C(O)=O HUZGPXBILPMCHM-IHRRRGAJSA-N 0.000 description 1
- DVUFTQLHHHJEMK-IMJSIDKUSA-N Asp-Ala Chemical compound OC(=O)[C@H](C)NC(=O)[C@@H](N)CC(O)=O DVUFTQLHHHJEMK-IMJSIDKUSA-N 0.000 description 1
- IVPNEDNYYYFAGI-GARJFASQSA-N Asp-Leu-Pro Chemical compound CC(C)C[C@@H](C(=O)N1CCC[C@@H]1C(=O)O)NC(=O)[C@H](CC(=O)O)N IVPNEDNYYYFAGI-GARJFASQSA-N 0.000 description 1
- 102100026189 Beta-galactosidase Human genes 0.000 description 1
- 201000004569 Blindness Diseases 0.000 description 1
- 101000782236 Bothrops leucurus Thrombin-like enzyme leucurobin Proteins 0.000 description 1
- 108091003079 Bovine Serum Albumin Proteins 0.000 description 1
- 102100032985 CCR4-NOT transcription complex subunit 7 Human genes 0.000 description 1
- 108050006912 CCR4-NOT transcription complex subunit 7 Proteins 0.000 description 1
- 241001478240 Coccus Species 0.000 description 1
- 108091026890 Coding region Proteins 0.000 description 1
- 108020004705 Codon Proteins 0.000 description 1
- 206010010904 Convulsion Diseases 0.000 description 1
- 241000699800 Cricetinae Species 0.000 description 1
- 206010011732 Cyst Diseases 0.000 description 1
- 102000016911 Deoxyribonucleases Human genes 0.000 description 1
- 108010053770 Deoxyribonucleases Proteins 0.000 description 1
- 239000006145 Eagle's minimal essential medium Substances 0.000 description 1
- 241000588724 Escherichia coli Species 0.000 description 1
- 241000797798 Fermo virus Species 0.000 description 1
- 241000287828 Gallus gallus Species 0.000 description 1
- 208000003098 Ganglion Cysts Diseases 0.000 description 1
- 108010051815 Glutamyl endopeptidase Proteins 0.000 description 1
- 239000004471 Glycine Substances 0.000 description 1
- 208000001688 Herpes Genitalis Diseases 0.000 description 1
- OAKJQQAXSVQMHS-UHFFFAOYSA-N Hydrazine Chemical compound NN OAKJQQAXSVQMHS-UHFFFAOYSA-N 0.000 description 1
- 206010061598 Immunodeficiency Diseases 0.000 description 1
- 208000029462 Immunodeficiency disease Diseases 0.000 description 1
- 108060003951 Immunoglobulin Proteins 0.000 description 1
- AGPKZVBTJJNPAG-WHFBIAKZSA-N L-isoleucine Chemical compound CC[C@H](C)[C@H](N)C(O)=O AGPKZVBTJJNPAG-WHFBIAKZSA-N 0.000 description 1
- AYFVYJQAPQTCCC-GBXIJSLDSA-N L-threonine Chemical compound C[C@@H](O)[C@H](N)C(O)=O AYFVYJQAPQTCCC-GBXIJSLDSA-N 0.000 description 1
- KZSNJWFQEVHDMF-BYPYZUCNSA-N L-valine Chemical compound CC(C)[C@H](N)C(O)=O KZSNJWFQEVHDMF-BYPYZUCNSA-N 0.000 description 1
- 208000032420 Latent Infection Diseases 0.000 description 1
- 102000004856 Lectins Human genes 0.000 description 1
- 108090001090 Lectins Proteins 0.000 description 1
- ICYRCNICGBJLGM-HJGDQZAQSA-N Leu-Thr-Asp Chemical compound CC(C)C[C@H](N)C(=O)N[C@@H]([C@@H](C)O)C(=O)N[C@H](C(O)=O)CC(O)=O ICYRCNICGBJLGM-HJGDQZAQSA-N 0.000 description 1
- 241000712079 Measles morbillivirus Species 0.000 description 1
- 102100030856 Myoglobin Human genes 0.000 description 1
- 108010062374 Myoglobin Proteins 0.000 description 1
- ZRKLEAHGBNDKHM-UHFFFAOYSA-N N,n'-diallyl-2,3-dihydroxysuccinamide Chemical compound C=CCNC(=O)C(O)C(O)C(=O)NCC=C ZRKLEAHGBNDKHM-UHFFFAOYSA-N 0.000 description 1
- 125000001429 N-terminal alpha-amino-acid group Chemical group 0.000 description 1
- 208000012902 Nervous system disease Diseases 0.000 description 1
- 208000025966 Neurological disease Diseases 0.000 description 1
- 102000011931 Nucleoproteins Human genes 0.000 description 1
- 108010061100 Nucleoproteins Proteins 0.000 description 1
- 108700026244 Open Reading Frames Proteins 0.000 description 1
- 241000609499 Palicourea Species 0.000 description 1
- 241000237988 Patellidae Species 0.000 description 1
- 108010038988 Peptide Hormones Proteins 0.000 description 1
- 102000015731 Peptide Hormones Human genes 0.000 description 1
- 102100030852 Run domain Beclin-1-interacting and cysteine-rich domain-containing protein Human genes 0.000 description 1
- 229920005654 Sephadex Polymers 0.000 description 1
- 239000012507 Sephadex™ Substances 0.000 description 1
- 238000012300 Sequence Analysis Methods 0.000 description 1
- VMHLLURERBWHNL-UHFFFAOYSA-M Sodium acetate Chemical compound [Na+].CC([O-])=O VMHLLURERBWHNL-UHFFFAOYSA-M 0.000 description 1
- 208000005400 Synovial Cyst Diseases 0.000 description 1
- AYFVYJQAPQTCCC-UHFFFAOYSA-N Threonine Natural products CC(O)C(N)C(O)=O AYFVYJQAPQTCCC-UHFFFAOYSA-N 0.000 description 1
- 239000004473 Threonine Substances 0.000 description 1
- 108090000631 Trypsin Proteins 0.000 description 1
- 102000004142 Trypsin Human genes 0.000 description 1
- 206010053613 Type IV hypersensitivity reaction Diseases 0.000 description 1
- AGXGCFSECFQMKB-NHCYSSNCSA-N Val-Leu-Asp Chemical compound CC(C)C[C@@H](C(=O)N[C@@H](CC(=O)O)C(=O)O)NC(=O)[C@H](C(C)C)N AGXGCFSECFQMKB-NHCYSSNCSA-N 0.000 description 1
- KZSNJWFQEVHDMF-UHFFFAOYSA-N Valine Natural products CC(C)C(N)C(O)=O KZSNJWFQEVHDMF-UHFFFAOYSA-N 0.000 description 1
- 108010065667 Viral Matrix Proteins Proteins 0.000 description 1
- 208000036142 Viral infection Diseases 0.000 description 1
- 230000002411 adverse Effects 0.000 description 1
- 238000001042 affinity chromatography Methods 0.000 description 1
- 230000004520 agglutination Effects 0.000 description 1
- 238000007818 agglutination assay Methods 0.000 description 1
- 238000003277 amino acid sequence analysis Methods 0.000 description 1
- BFNBIHQBYMNNAN-UHFFFAOYSA-N ammonium sulfate Chemical class N.N.OS(O)(=O)=O BFNBIHQBYMNNAN-UHFFFAOYSA-N 0.000 description 1
- 239000012491 analyte Substances 0.000 description 1
- 238000004873 anchoring Methods 0.000 description 1
- 108010005774 beta-Galactosidase Proteins 0.000 description 1
- 210000004369 blood Anatomy 0.000 description 1
- 239000008280 blood Substances 0.000 description 1
- 230000037396 body weight Effects 0.000 description 1
- 238000009835 boiling Methods 0.000 description 1
- 229910021538 borax Inorganic materials 0.000 description 1
- 229940098773 bovine serum albumin Drugs 0.000 description 1
- 210000004899 c-terminal region Anatomy 0.000 description 1
- 244000309466 calf Species 0.000 description 1
- 239000000969 carrier Substances 0.000 description 1
- 230000001413 cellular effect Effects 0.000 description 1
- 230000007969 cellular immunity Effects 0.000 description 1
- 230000036755 cellular response Effects 0.000 description 1
- 238000005119 centrifugation Methods 0.000 description 1
- 230000008859 change Effects 0.000 description 1
- 238000012512 characterization method Methods 0.000 description 1
- 239000003153 chemical reaction reagent Substances 0.000 description 1
- 238000011210 chromatographic step Methods 0.000 description 1
- 150000001875 compounds Chemical class 0.000 description 1
- 239000012468 concentrated sample Substances 0.000 description 1
- 239000000470 constituent Substances 0.000 description 1
- NKLPQNGYXWVELD-UHFFFAOYSA-M coomassie brilliant blue Chemical compound [Na+].C1=CC(OCC)=CC=C1NC1=CC=C(C(=C2C=CC(C=C2)=[N+](CC)CC=2C=C(C=CC=2)S([O-])(=O)=O)C=2C=CC(=CC=2)N(CC)CC=2C=C(C=CC=2)S([O-])(=O)=O)C=C1 NKLPQNGYXWVELD-UHFFFAOYSA-M 0.000 description 1
- 210000004087 cornea Anatomy 0.000 description 1
- 230000008878 coupling Effects 0.000 description 1
- 238000010168 coupling process Methods 0.000 description 1
- 238000005859 coupling reaction Methods 0.000 description 1
- 230000009260 cross reactivity Effects 0.000 description 1
- 238000012258 culturing Methods 0.000 description 1
- ATDGTVJJHBUTRL-UHFFFAOYSA-N cyanogen bromide Chemical compound BrC#N ATDGTVJJHBUTRL-UHFFFAOYSA-N 0.000 description 1
- 208000031513 cyst Diseases 0.000 description 1
- 230000003247 decreasing effect Effects 0.000 description 1
- 238000004925 denaturation Methods 0.000 description 1
- 230000036425 denaturation Effects 0.000 description 1
- 229960003964 deoxycholic acid Drugs 0.000 description 1
- KXGVEGMKQFWNSR-LLQZFEROSA-N deoxycholic acid Chemical compound C([C@H]1CC2)[C@H](O)CC[C@]1(C)[C@@H]1[C@@H]2[C@@H]2CC[C@H]([C@@H](CCC(O)=O)C)[C@@]2(C)[C@@H](O)C1 KXGVEGMKQFWNSR-LLQZFEROSA-N 0.000 description 1
- 238000002405 diagnostic procedure Methods 0.000 description 1
- 230000029087 digestion Effects 0.000 description 1
- 239000012153 distilled water Substances 0.000 description 1
- 238000001962 electrophoresis Methods 0.000 description 1
- 206010014599 encephalitis Diseases 0.000 description 1
- DNJIEGIFACGWOD-UHFFFAOYSA-N ethyl mercaptane Natural products CCS DNJIEGIFACGWOD-UHFFFAOYSA-N 0.000 description 1
- 238000013213 extrapolation Methods 0.000 description 1
- 230000002349 favourable effect Effects 0.000 description 1
- 210000002950 fibroblast Anatomy 0.000 description 1
- 238000005194 fractionation Methods 0.000 description 1
- 108020001507 fusion proteins Proteins 0.000 description 1
- 102000037865 fusion proteins Human genes 0.000 description 1
- 238000007429 general method Methods 0.000 description 1
- 201000004946 genital herpes Diseases 0.000 description 1
- 210000004392 genitalia Anatomy 0.000 description 1
- 102000018146 globin Human genes 0.000 description 1
- 108060003196 globin Proteins 0.000 description 1
- 108060003552 hemocyanin Proteins 0.000 description 1
- 230000002949 hemolytic effect Effects 0.000 description 1
- 208000002672 hepatitis B Diseases 0.000 description 1
- 229940124725 herpes simplex vaccine Drugs 0.000 description 1
- 238000004128 high performance liquid chromatography Methods 0.000 description 1
- 230000003054 hormonal effect Effects 0.000 description 1
- 210000005260 human cell Anatomy 0.000 description 1
- 230000007062 hydrolysis Effects 0.000 description 1
- 238000006460 hydrolysis reaction Methods 0.000 description 1
- 230000002209 hydrophobic effect Effects 0.000 description 1
- 238000003018 immunoassay Methods 0.000 description 1
- 230000000984 immunochemical effect Effects 0.000 description 1
- 230000007813 immunodeficiency Effects 0.000 description 1
- 102000018358 immunoglobulin Human genes 0.000 description 1
- 230000002621 immunoprecipitating effect Effects 0.000 description 1
- 229940031551 inactivated vaccine Drugs 0.000 description 1
- 238000011534 incubation Methods 0.000 description 1
- 230000001939 inductive effect Effects 0.000 description 1
- 230000002458 infectious effect Effects 0.000 description 1
- 238000013383 initial experiment Methods 0.000 description 1
- 239000002054 inoculum Substances 0.000 description 1
- 238000007918 intramuscular administration Methods 0.000 description 1
- 239000007928 intraperitoneal injection Substances 0.000 description 1
- 238000005342 ion exchange Methods 0.000 description 1
- 229960000310 isoleucine Drugs 0.000 description 1
- AGPKZVBTJJNPAG-UHFFFAOYSA-N isoleucine Natural products CCC(C)C(N)C(O)=O AGPKZVBTJJNPAG-UHFFFAOYSA-N 0.000 description 1
- 206010023332 keratitis Diseases 0.000 description 1
- 239000002523 lectin Substances 0.000 description 1
- 231100000636 lethal dose Toxicity 0.000 description 1
- 125000001909 leucine group Chemical group [H]N(*)C(C(*)=O)C([H])([H])C(C([H])([H])[H])C([H])([H])[H] 0.000 description 1
- 230000002934 lysing effect Effects 0.000 description 1
- 239000012139 lysis buffer Substances 0.000 description 1
- 238000012423 maintenance Methods 0.000 description 1
- 210000001161 mammalian embryo Anatomy 0.000 description 1
- 239000011159 matrix material Substances 0.000 description 1
- 210000004779 membrane envelope Anatomy 0.000 description 1
- 108020004999 messenger RNA Proteins 0.000 description 1
- 230000000813 microbial effect Effects 0.000 description 1
- 210000004400 mucous membrane Anatomy 0.000 description 1
- 210000004897 n-terminal region Anatomy 0.000 description 1
- 210000000944 nerve tissue Anatomy 0.000 description 1
- 210000000653 nervous system Anatomy 0.000 description 1
- 229920001542 oligosaccharide Polymers 0.000 description 1
- 150000002482 oligosaccharides Chemical class 0.000 description 1
- 230000003647 oxidation Effects 0.000 description 1
- 238000007254 oxidation reaction Methods 0.000 description 1
- 230000008506 pathogenesis Effects 0.000 description 1
- 230000001717 pathogenic effect Effects 0.000 description 1
- 239000000813 peptide hormone Substances 0.000 description 1
- 229940023041 peptide vaccine Drugs 0.000 description 1
- 230000002085 persistent effect Effects 0.000 description 1
- 239000000546 pharmaceutical excipient Substances 0.000 description 1
- DDBREPKUVSBGFI-UHFFFAOYSA-N phenobarbital Chemical compound C=1C=CC=CC=1C1(CC)C(=O)NC(=O)NC1=O DDBREPKUVSBGFI-UHFFFAOYSA-N 0.000 description 1
- 108010018625 phenylalanylarginine Proteins 0.000 description 1
- 239000008363 phosphate buffer Substances 0.000 description 1
- 230000003389 potentiating effect Effects 0.000 description 1
- 238000004321 preservation Methods 0.000 description 1
- 230000008569 process Effects 0.000 description 1
- 238000000159 protein binding assay Methods 0.000 description 1
- 230000017854 proteolysis Effects 0.000 description 1
- 230000002797 proteolythic effect Effects 0.000 description 1
- 239000001397 quillaja saponaria molina bark Substances 0.000 description 1
- 238000003127 radioimmunoassay Methods 0.000 description 1
- 238000010188 recombinant method Methods 0.000 description 1
- 230000002829 reductive effect Effects 0.000 description 1
- 230000000284 resting effect Effects 0.000 description 1
- 238000012502 risk assessment Methods 0.000 description 1
- 229930182490 saponin Natural products 0.000 description 1
- 150000007949 saponins Chemical class 0.000 description 1
- 238000003345 scintillation counting Methods 0.000 description 1
- 210000003491 skin Anatomy 0.000 description 1
- 239000001632 sodium acetate Substances 0.000 description 1
- 235000017281 sodium acetate Nutrition 0.000 description 1
- 229910000029 sodium carbonate Inorganic materials 0.000 description 1
- 235000010339 sodium tetraborate Nutrition 0.000 description 1
- 239000007787 solid Substances 0.000 description 1
- 239000007858 starting material Substances 0.000 description 1
- 239000000725 suspension Substances 0.000 description 1
- 238000010189 synthetic method Methods 0.000 description 1
- 101150072448 thrB gene Proteins 0.000 description 1
- 230000009466 transformation Effects 0.000 description 1
- 230000001052 transient effect Effects 0.000 description 1
- BSVBQGMMJUBVOD-UHFFFAOYSA-N trisodium borate Chemical compound [Na+].[Na+].[Na+].[O-]B([O-])[O-] BSVBQGMMJUBVOD-UHFFFAOYSA-N 0.000 description 1
- GPRLSGONYQIRFK-MNYXATJNSA-N triton Chemical compound [3H+] GPRLSGONYQIRFK-MNYXATJNSA-N 0.000 description 1
- 239000012588 trypsin Substances 0.000 description 1
- 230000005951 type IV hypersensitivity Effects 0.000 description 1
- 208000027930 type IV hypersensitivity disease Diseases 0.000 description 1
- OUYCCCASQSFEME-UHFFFAOYSA-N tyrosine Natural products OC(=O)C(N)CC1=CC=C(O)C=C1 OUYCCCASQSFEME-UHFFFAOYSA-N 0.000 description 1
- 125000001493 tyrosinyl group Chemical group [H]OC1=C([H])C([H])=C(C([H])=C1[H])C([H])([H])C([H])(N([H])[H])C(*)=O 0.000 description 1
- 229940125575 vaccine candidate Drugs 0.000 description 1
- 239000004474 valine Substances 0.000 description 1
- 238000012795 verification Methods 0.000 description 1
- DGVVWUTYPXICAM-UHFFFAOYSA-N β‐Mercaptoethanol Chemical compound OCCS DGVVWUTYPXICAM-UHFFFAOYSA-N 0.000 description 1
Classifications
-
- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61K—PREPARATIONS FOR MEDICAL, DENTAL OR TOILETRY PURPOSES
- A61K39/00—Medicinal preparations containing antigens or antibodies
- A61K39/12—Viral antigens
- A61K39/245—Herpetoviridae, e.g. herpes simplex virus
-
- 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
- G01N33/68—Chemical analysis of biological material, e.g. blood, urine; Testing involving biospecific ligand binding methods; Immunological testing involving proteins, peptides or amino acids
- G01N33/6854—Immunoglobulins
-
- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61P—SPECIFIC THERAPEUTIC ACTIVITY OF CHEMICAL COMPOUNDS OR MEDICINAL PREPARATIONS
- A61P31/00—Antiinfectives, i.e. antibiotics, antiseptics, chemotherapeutics
- A61P31/12—Antivirals
-
- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61P—SPECIFIC THERAPEUTIC ACTIVITY OF CHEMICAL COMPOUNDS OR MEDICINAL PREPARATIONS
- A61P31/00—Antiinfectives, i.e. antibiotics, antiseptics, chemotherapeutics
- A61P31/12—Antivirals
- A61P31/20—Antivirals for DNA viruses
- A61P31/22—Antivirals for DNA viruses for herpes 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
-
- 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
-
- 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
- G01N33/56994—Herpetoviridae, e.g. cytomegalovirus, Epstein-Barr virus
-
- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61K—PREPARATIONS FOR MEDICAL, DENTAL OR TOILETRY PURPOSES
- A61K39/00—Medicinal preparations containing antigens or antibodies
-
- 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
- C12N2710/00—MICROORGANISMS OR ENZYMES; COMPOSITIONS THEREOF; PROPAGATING, PRESERVING, OR MAINTAINING MICROORGANISMS; MUTATION OR GENETIC ENGINEERING; CULTURE MEDIA dsDNA viruses
- C12N2710/00011—Details
- C12N2710/16011—Herpesviridae
- C12N2710/16611—Simplexvirus, e.g. human herpesvirus 1, 2
- C12N2710/16622—New viral proteins or individual genes, new structural or functional aspects of known viral proteins or genes
-
- 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
- Y10—TECHNICAL SUBJECTS COVERED BY FORMER USPC
- Y10S—TECHNICAL SUBJECTS COVERED BY FORMER USPC CROSS-REFERENCE ART COLLECTIONS [XRACs] AND DIGESTS
- Y10S530/00—Chemistry: natural resins or derivatives; peptides or proteins; lignins or reaction products thereof
- Y10S530/806—Antigenic peptides or proteins
-
- 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
- Y10—TECHNICAL SUBJECTS COVERED BY FORMER USPC
- Y10S—TECHNICAL SUBJECTS COVERED BY FORMER USPC CROSS-REFERENCE ART COLLECTIONS [XRACs] AND DIGESTS
- Y10S930/00—Peptide or protein sequence
- Y10S930/01—Peptide or protein sequence
- Y10S930/22—Viral peptide or viral protein
- Y10S930/224—Herpes related
Landscapes
- Health & Medical Sciences (AREA)
- Life Sciences & Earth Sciences (AREA)
- Chemical & Material Sciences (AREA)
- Engineering & Computer Science (AREA)
- Immunology (AREA)
- Virology (AREA)
- Molecular Biology (AREA)
- Urology & Nephrology (AREA)
- Hematology (AREA)
- Biomedical Technology (AREA)
- General Health & Medical Sciences (AREA)
- Medicinal Chemistry (AREA)
- Biochemistry (AREA)
- Biotechnology (AREA)
- Microbiology (AREA)
- Analytical Chemistry (AREA)
- Pathology (AREA)
- General Physics & Mathematics (AREA)
- Physics & Mathematics (AREA)
- Organic Chemistry (AREA)
- Food Science & Technology (AREA)
- Cell Biology (AREA)
- Proteomics, Peptides & Aminoacids (AREA)
- Tropical Medicine & Parasitology (AREA)
- Animal Behavior & Ethology (AREA)
- Public Health (AREA)
- Veterinary Medicine (AREA)
- Pharmacology & Pharmacy (AREA)
- Oncology (AREA)
- Gastroenterology & Hepatology (AREA)
- General Chemical & Material Sciences (AREA)
- Nuclear Medicine, Radiotherapy & Molecular Imaging (AREA)
- Genetics & Genomics (AREA)
- Communicable Diseases (AREA)
- Biophysics (AREA)
- Chemical Kinetics & Catalysis (AREA)
- Mycology (AREA)
- Epidemiology (AREA)
- Medicines Containing Antibodies Or Antigens For Use As Internal Diagnostic Agents (AREA)
- Peptides Or Proteins (AREA)
Applications Claiming Priority (6)
| Application Number | Priority Date | Filing Date | Title |
|---|---|---|---|
| US35002182A | 1982-02-18 | 1982-02-18 | |
| US35002182 | 1982-02-18 | ||
| US06/463,141 US4762708A (en) | 1982-02-18 | 1983-02-04 | Materials and methods for herpes simplex virus vaccination |
| US46314183 | 1983-02-04 | ||
| US8300182 | 1983-02-14 | ||
| PCT/US1983/000182 WO1983002897A1 (en) | 1982-02-18 | 1983-02-14 | Materials and methods for herpes simplex virus vaccination |
Publications (3)
| Publication Number | Publication Date |
|---|---|
| DK479083A DK479083A (da) | 1983-10-17 |
| DK479083D0 DK479083D0 (da) | 1983-10-17 |
| DK172619B1 true DK172619B1 (da) | 1999-03-01 |
Family
ID=26996451
Family Applications (1)
| Application Number | Title | Priority Date | Filing Date |
|---|---|---|---|
| DK198304790A DK172619B1 (da) | 1982-02-18 | 1983-10-17 | Fremgangsmåde til isolering af immunogene præparater af herpes simplex virus type 1 og type 2, fremgangsmåde til fremstill |
Country Status (20)
| Country | Link |
|---|---|
| US (1) | US4762708A (es) |
| EP (1) | EP0101506B1 (es) |
| JP (3) | JP2665332B2 (es) |
| KR (1) | KR910006889B1 (es) |
| AR (1) | AR231496A1 (es) |
| AT (1) | ATE54827T1 (es) |
| AU (1) | AU554710B2 (es) |
| CA (1) | CA1236774A (es) |
| DE (1) | DE3381761D1 (es) |
| DK (1) | DK172619B1 (es) |
| ES (1) | ES519875A0 (es) |
| FI (2) | FI73885C (es) |
| GR (1) | GR77900B (es) |
| HU (1) | HU195734B (es) |
| IE (1) | IE56479B1 (es) |
| IL (5) | IL67930A (es) |
| NO (2) | NO162366B (es) |
| NZ (1) | NZ220771A (es) |
| PH (1) | PH25689A (es) |
| WO (1) | WO1983002897A1 (es) |
Families Citing this family (27)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| US4540669A (en) * | 1980-09-11 | 1985-09-10 | Merck & Co., Inc. | Herpes simplex type I subunit vaccine |
| US5149660A (en) * | 1982-02-18 | 1992-09-22 | University Patents, Inc. | Diagnostic reagents relating to herpes simplex virus |
| US7264817B1 (en) | 1983-08-30 | 2007-09-04 | Genentech, Inc. | Immunogenic composition based on a truncated derivative of a membrane bound protein and process for making it |
| NZ209308A (en) * | 1983-08-30 | 1991-08-27 | Genentech Inc | Vaccine against hsv involving a truncated membrane-free derivative of a membrane-bound protein |
| NZ209307A (en) * | 1983-08-30 | 1990-07-26 | Genentech Inc | Diagnostic product: antigenic peptide produced by recombinant dna techniques |
| JPS6051120A (ja) * | 1983-08-31 | 1985-03-22 | Chemo Sero Therapeut Res Inst | 単純ヘルペスサブユニットワクチン |
| US5171568A (en) * | 1984-04-06 | 1992-12-15 | Chiron Corporation | Recombinant herpes simplex gb-gd vaccine |
| US5612041A (en) * | 1984-07-17 | 1997-03-18 | Chiron Corporation | Recombinant herpes simplex gD vaccine |
| JPS6153226A (ja) * | 1984-08-24 | 1986-03-17 | Chemo Sero Therapeut Res Inst | 単純ヘルペスサブユニツトワクチンの精製方法 |
| DE3683688D1 (de) * | 1985-04-19 | 1992-03-12 | Wistar Inst | Impfstoff fuer die erzeugung einer gegen ein virus schuetzenden immunogenen t-zellen-antwort. |
| GB8605390D0 (en) * | 1986-03-05 | 1986-04-09 | Univ Birmingham | Live herpes simplex vaccine |
| EP0471778A1 (en) * | 1989-05-12 | 1992-02-26 | Ciba Corning Diagnostics Corp. | Herpes simplex virus type 2-glycoprotein g proteins and polypeptides |
| GB9105992D0 (en) * | 1991-03-21 | 1991-05-08 | Smithkline Beecham Biolog | Vaccine |
| US5654174A (en) * | 1995-07-07 | 1997-08-05 | Competitive Technologies, Inc. | Herpes simplex virus glycoprotein D variants |
| US20020090382A1 (en) * | 2000-08-01 | 2002-07-11 | University Of Pittsburgh Of The Commonwealth System Of Higher Education | Antiviral compounds and methods |
| US20030219448A1 (en) * | 2002-05-24 | 2003-11-27 | Cedars-Sinai Medical Center | Peptide epitope-based vaccine for treating herpes simplex virus infections and related diseases |
| US7078041B2 (en) | 2002-07-18 | 2006-07-18 | University Of Washington | Rapid, efficient purification of HSV-specific T-lymphocytes and HSV antigens identified via same |
| CA2538794C (en) * | 2003-09-12 | 2016-04-19 | Antigenics, Inc. | Vaccine for treatment and prevention of herpes simplex virus infection |
| US8865185B2 (en) * | 2006-09-08 | 2014-10-21 | The Trustees Of The University Of Pennsylvania | Methods of use for HSV-1 and HSV-2 vaccines |
| EP2059255A4 (en) * | 2006-09-08 | 2011-08-31 | Univ Pennsylvania | VACCINES AGAINST HSV-1 AND HSV-2 AND METHODS OF USE |
| US10478490B2 (en) * | 2006-12-28 | 2019-11-19 | The Trustees Of The University Of Pennsylvania | Herpes simplex virus combined subunit vaccines and methods of use thereof |
| US8057804B2 (en) * | 2006-12-28 | 2011-11-15 | The Trustees Of The University Of Pennsylvania | Herpes simplex virus combined subunit vaccines and methods of use thereof |
| US20130028925A1 (en) * | 2006-12-28 | 2013-01-31 | Harvey Friedman | Herpes simplex virus combined subunit vaccines and methods of use thereof |
| CN101616688B (zh) * | 2006-12-28 | 2013-12-11 | 宾夕法尼亚大学理事会 | 单纯疱疹病毒联合亚单位疫苗及其使用方法 |
| WO2011106607A2 (en) | 2010-02-26 | 2011-09-01 | Juvaris Biotherapeutics, Inc. | Subunit vaccines for herpes viruses and methods of use |
| WO2012139106A2 (en) * | 2011-04-08 | 2012-10-11 | Duke University | Herpes simplex virus |
| US9555099B2 (en) | 2012-05-16 | 2017-01-31 | Immune Design Corp. | Vaccines for HSV-2 |
Family Cites Families (2)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| US4374127A (en) * | 1977-09-19 | 1983-02-15 | Merck & Co., Inc. | Herpes sub unit vaccine |
| DK171727B1 (da) * | 1978-12-22 | 1997-04-14 | Biogen Inc | Rekombinante hepatitis B virus DNA-molekyler, værtsorganismer transformeret hermed, HBV-antigenspecifikke polypeptider, DNA-sekvenser kodende for HBV-antigenspecifikke polypeptider, metoder til påvisning af hepatitis B virus-antistoffer, metoder til fremstilling af nævnte DNA-molekyler, fremgangsmåder til fremstilling af nævnte polypeptider og midler til påvisning af HBV-infektion |
-
1983
- 1983-02-04 US US06/463,141 patent/US4762708A/en not_active Expired - Lifetime
- 1983-02-14 WO PCT/US1983/000182 patent/WO1983002897A1/en not_active Application Discontinuation
- 1983-02-14 AT AT83901021T patent/ATE54827T1/de not_active IP Right Cessation
- 1983-02-14 EP EP83901021A patent/EP0101506B1/en not_active Expired - Lifetime
- 1983-02-14 IE IE332/83A patent/IE56479B1/en not_active IP Right Cessation
- 1983-02-14 NZ NZ220771A patent/NZ220771A/xx unknown
- 1983-02-14 DE DE8383901021T patent/DE3381761D1/de not_active Revoked
- 1983-02-14 HU HU831928A patent/HU195734B/hu not_active IP Right Cessation
- 1983-02-14 JP JP58500988A patent/JP2665332B2/ja not_active Expired - Lifetime
- 1983-02-14 AU AU13396/83A patent/AU554710B2/en not_active Ceased
- 1983-02-16 IL IL67930A patent/IL67930A/xx not_active IP Right Cessation
- 1983-02-16 IL IL80896A patent/IL80896A/xx not_active IP Right Cessation
- 1983-02-16 IL IL80895A patent/IL80895A/xx not_active IP Right Cessation
- 1983-02-16 AR AR292146A patent/AR231496A1/es active
- 1983-02-17 KR KR1019830000640A patent/KR910006889B1/ko not_active IP Right Cessation
- 1983-02-17 CA CA000421874A patent/CA1236774A/en not_active Expired
- 1983-02-17 ES ES519875A patent/ES519875A0/es active Granted
- 1983-02-18 PH PH28533A patent/PH25689A/en unknown
- 1983-02-18 GR GR70545A patent/GR77900B/el unknown
- 1983-10-17 NO NO83833773A patent/NO162366B/no not_active IP Right Cessation
- 1983-10-17 DK DK198304790A patent/DK172619B1/da not_active IP Right Cessation
- 1983-10-17 FI FI833768A patent/FI73885C/fi not_active IP Right Cessation
-
1984
- 1984-07-19 NO NO84842962A patent/NO172745C/no not_active IP Right Cessation
-
1986
- 1986-10-10 FI FI864102A patent/FI83880C/fi not_active IP Right Cessation
- 1986-12-07 IL IL80896A patent/IL80896A0/xx unknown
- 1986-12-07 IL IL80895A patent/IL80895A0/xx unknown
-
1994
- 1994-02-28 JP JP6054572A patent/JP2669594B2/ja not_active Expired - Lifetime
- 1994-02-28 JP JP6052580A patent/JP2567202B2/ja not_active Expired - Lifetime
Also Published As
Similar Documents
| Publication | Publication Date | Title |
|---|---|---|
| DK172619B1 (da) | Fremgangsmåde til isolering af immunogene præparater af herpes simplex virus type 1 og type 2, fremgangsmåde til fremstill | |
| FI114802B (fi) | Epstein-Barr-virukseen liittyviä peptidejä ja nukleiinihapposekvenssejä | |
| Petrovskis et al. | Use of lambda gt11 to isolate genes for two pseudorabies virus glycoproteins with homology to herpes simplex virus and varicella-zoster virus glycoproteins | |
| US4709011A (en) | Materials and methods for herpes simplex virus vaccination | |
| Dietzschold et al. | Antigenic structure of rabies virus glycoprotein: ordering and immunological characterization of the large CNBr cleavage fragments | |
| Oba et al. | Induction of antibodies to the Epstein-Barr virus glycoprotein gp85 with a synthetic peptide corresponding to a sequence in the BXLF2 open reading frame | |
| US7169393B2 (en) | Antigenic peptide fragments of VapA protein, and uses thereof | |
| US5149660A (en) | Diagnostic reagents relating to herpes simplex virus | |
| CA2178057C (en) | Epstein-barr virus peptides and antibodies against these peptides | |
| CA2719041C (en) | A method for identifying polypeptides which comprise a cross-reactive antigenic determinant | |
| DK175072B1 (da) | Rekombinant DNA-molekyle, værtscelle transformeret dermed, fremgangsmåde til fremstilling af et polypeptid ved anvendelse af det rekombinante DNA-molekyle, og diagnostisk sæt omfattende et sådant polypeptid | |
| CA2068654C (en) | Varicella-zoster virus antigen | |
| AU4816293A (en) | Epstein-barr virus peptides and antibodies against these peptides | |
| US20040234542A1 (en) | Recombinant orf2 proteins of the swine hepatitis e virus and their use as a vaccine and as a diagnostic reagent for medical and veterinary applications | |
| AU777145B2 (en) | Antigenic protein LPPQ of Mycoplasma mycoidessubsp.(mycoides)SC., its preparation and use | |
| Sinclair et al. | Detection of antibodies against equine herpesvirus types 1 and 4 by using recombinant protein derived from an immunodominant region of glycoprotein B | |
| WO2010027499A2 (en) | Methods, compositions and vaccines relating to neisseria meningitidis antibodies |
Legal Events
| Date | Code | Title | Description |
|---|---|---|---|
| B1 | Patent granted (law 1993) | ||
| PBP | Patent lapsed |