WO1998010792A1 - Immune direction therapy - Google Patents
Immune direction therapy Download PDFInfo
- Publication number
- WO1998010792A1 WO1998010792A1 PCT/IB1996/000945 IB9600945W WO9810792A1 WO 1998010792 A1 WO1998010792 A1 WO 1998010792A1 IB 9600945 W IB9600945 W IB 9600945W WO 9810792 A1 WO9810792 A1 WO 9810792A1
- Authority
- WO
- WIPO (PCT)
- Prior art keywords
- glu
- asp
- lys
- arg
- immune
- Prior art date
Links
- 238000002560 therapeutic procedure Methods 0.000 title claims abstract description 7
- 208000015181 infectious disease Diseases 0.000 claims abstract description 38
- 108090000765 processed proteins & peptides Proteins 0.000 claims abstract description 31
- 102000003814 Interleukin-10 Human genes 0.000 claims abstract description 27
- 108090000174 Interleukin-10 Proteins 0.000 claims abstract description 27
- 229940076144 interleukin-10 Drugs 0.000 claims abstract description 24
- 102000004127 Cytokines Human genes 0.000 claims abstract description 18
- 108090000695 Cytokines Proteins 0.000 claims abstract description 18
- 229960005486 vaccine Drugs 0.000 claims abstract description 18
- 102000004196 processed proteins & peptides Human genes 0.000 claims abstract description 17
- 230000003612 virological effect Effects 0.000 claims abstract description 17
- 238000011282 treatment Methods 0.000 claims abstract description 16
- 210000001744 T-lymphocyte Anatomy 0.000 claims abstract description 14
- 230000001506 immunosuppresive effect Effects 0.000 claims abstract description 12
- 230000002209 hydrophobic effect Effects 0.000 claims abstract description 11
- 230000002458 infectious effect Effects 0.000 claims abstract description 9
- 238000003491 array Methods 0.000 claims abstract description 8
- 230000001580 bacterial effect Effects 0.000 claims abstract description 8
- 230000015572 biosynthetic process Effects 0.000 claims abstract description 7
- 201000010099 disease Diseases 0.000 claims abstract description 7
- 208000037265 diseases, disorders, signs and symptoms Diseases 0.000 claims abstract description 7
- 230000000694 effects Effects 0.000 claims abstract description 7
- 230000001225 therapeutic effect Effects 0.000 claims abstract description 7
- 230000002401 inhibitory effect Effects 0.000 claims abstract description 6
- 230000001419 dependent effect Effects 0.000 claims abstract description 5
- 238000003786 synthesis reaction Methods 0.000 claims abstract description 5
- 230000002538 fungal effect Effects 0.000 claims abstract description 3
- 230000008004 immune attack Effects 0.000 claims abstract description 3
- 208000011580 syndromic disease Diseases 0.000 claims abstract description 3
- 201000006417 multiple sclerosis Diseases 0.000 claims abstract 4
- 206010008874 Chronic Fatigue Syndrome Diseases 0.000 claims abstract 3
- 239000003246 corticosteroid Substances 0.000 claims abstract 3
- 206010025135 lupus erythematosus Diseases 0.000 claims abstract 3
- 208000029766 myalgic encephalomeyelitis/chronic fatigue syndrome Diseases 0.000 claims abstract 3
- 208000023275 Autoimmune disease Diseases 0.000 claims abstract 2
- 210000000056 organ Anatomy 0.000 claims abstract 2
- 206010039073 rheumatoid arthritis Diseases 0.000 claims abstract 2
- 210000004027 cell Anatomy 0.000 claims description 25
- 150000001413 amino acids Chemical group 0.000 claims description 19
- 201000004792 malaria Diseases 0.000 claims description 19
- 210000000987 immune system Anatomy 0.000 claims description 18
- 238000000034 method Methods 0.000 claims description 18
- 241000282414 Homo sapiens Species 0.000 claims description 17
- 239000000427 antigen Substances 0.000 claims description 15
- 108091007433 antigens Proteins 0.000 claims description 15
- 102000036639 antigens Human genes 0.000 claims description 15
- 241001465754 Metazoa Species 0.000 claims description 13
- 210000003719 b-lymphocyte Anatomy 0.000 claims description 8
- 239000008194 pharmaceutical composition Substances 0.000 claims description 8
- 230000004044 response Effects 0.000 claims description 8
- 230000001681 protective effect Effects 0.000 claims description 7
- 241000713772 Human immunodeficiency virus 1 Species 0.000 claims description 5
- 206010061598 Immunodeficiency Diseases 0.000 claims description 5
- 208000029462 Immunodeficiency disease Diseases 0.000 claims description 5
- 206010062016 Immunosuppression Diseases 0.000 claims description 5
- 108010026331 alpha-Fetoproteins Proteins 0.000 claims description 5
- 230000007813 immunodeficiency Effects 0.000 claims description 5
- 108090000623 proteins and genes Proteins 0.000 claims description 5
- 208000030852 Parasitic disease Diseases 0.000 claims description 4
- 208000036142 Viral infection Diseases 0.000 claims description 4
- 230000005875 antibody response Effects 0.000 claims description 4
- 238000012217 deletion Methods 0.000 claims description 4
- 230000037430 deletion Effects 0.000 claims description 4
- 230000036039 immunity Effects 0.000 claims description 4
- 241000712461 unidentified influenza virus Species 0.000 claims description 4
- 229940125575 vaccine candidate Drugs 0.000 claims description 4
- 230000000890 antigenic effect Effects 0.000 claims description 3
- 229940124735 malaria vaccine Drugs 0.000 claims description 3
- 102000004169 proteins and genes Human genes 0.000 claims description 3
- 108010076504 Protein Sorting Signals Proteins 0.000 claims description 2
- 210000004369 blood Anatomy 0.000 claims description 2
- 239000008280 blood Substances 0.000 claims description 2
- 230000003828 downregulation Effects 0.000 claims description 2
- 201000008827 tuberculosis Diseases 0.000 claims description 2
- 238000002360 preparation method Methods 0.000 claims 4
- 102000013529 alpha-Fetoproteins Human genes 0.000 claims 3
- 108020004491 Antisense DNA Proteins 0.000 claims 2
- 108020005544 Antisense RNA Proteins 0.000 claims 2
- 239000002253 acid Substances 0.000 claims 2
- 150000007513 acids Chemical class 0.000 claims 2
- 239000003816 antisense DNA Substances 0.000 claims 2
- 238000003556 assay Methods 0.000 claims 2
- 239000003184 complementary RNA Substances 0.000 claims 2
- 230000009385 viral infection Effects 0.000 claims 2
- SSSROGPPPVTHLX-FXQIFTODSA-N Ala-Arg-Asp Chemical compound [H]N[C@@H](C)C(=O)N[C@@H](CCCNC(N)=N)C(=O)N[C@@H](CC(O)=O)C(O)=O SSSROGPPPVTHLX-FXQIFTODSA-N 0.000 claims 1
- SVBXIUDNTRTKHE-CIUDSAMLSA-N Ala-Arg-Glu Chemical compound [H]N[C@@H](C)C(=O)N[C@@H](CCCNC(N)=N)C(=O)N[C@@H](CCC(O)=O)C(O)=O SVBXIUDNTRTKHE-CIUDSAMLSA-N 0.000 claims 1
- PBAMJJXWDQXOJA-FXQIFTODSA-N Ala-Asp-Arg Chemical compound C[C@H](N)C(=O)N[C@@H](CC(O)=O)C(=O)N[C@H](C(O)=O)CCCN=C(N)N PBAMJJXWDQXOJA-FXQIFTODSA-N 0.000 claims 1
- LZRNYBIJOSKKRJ-XVYDVKMFSA-N Ala-Asp-His Chemical compound C[C@@H](C(=O)N[C@@H](CC(=O)O)C(=O)N[C@@H](CC1=CN=CN1)C(=O)O)N LZRNYBIJOSKKRJ-XVYDVKMFSA-N 0.000 claims 1
- LSLIRHLIUDVNBN-CIUDSAMLSA-N Ala-Asp-Lys Chemical compound C[C@H](N)C(=O)N[C@@H](CC(O)=O)C(=O)N[C@H](C(O)=O)CCCCN LSLIRHLIUDVNBN-CIUDSAMLSA-N 0.000 claims 1
- NWVVKQZOVSTDBQ-CIUDSAMLSA-N Ala-Glu-Arg Chemical compound [H]N[C@@H](C)C(=O)N[C@@H](CCC(O)=O)C(=O)N[C@@H](CCCNC(N)=N)C(O)=O NWVVKQZOVSTDBQ-CIUDSAMLSA-N 0.000 claims 1
- BVSGPHDECMJBDE-HGNGGELXSA-N Ala-Glu-His Chemical compound C[C@@H](C(=O)N[C@@H](CCC(=O)O)C(=O)N[C@@H](CC1=CN=CN1)C(=O)O)N BVSGPHDECMJBDE-HGNGGELXSA-N 0.000 claims 1
- HMRWQTHUDVXMGH-GUBZILKMSA-N Ala-Glu-Lys Chemical compound C[C@H](N)C(=O)N[C@@H](CCC(O)=O)C(=O)N[C@H](C(O)=O)CCCCN HMRWQTHUDVXMGH-GUBZILKMSA-N 0.000 claims 1
- FDAZDMAFZYTHGS-XVYDVKMFSA-N Ala-His-Asp Chemical compound [H]N[C@@H](C)C(=O)N[C@@H](CC1=CNC=N1)C(=O)N[C@@H](CC(O)=O)C(O)=O FDAZDMAFZYTHGS-XVYDVKMFSA-N 0.000 claims 1
- GRPHQEMIFDPKOE-HGNGGELXSA-N Ala-His-Glu Chemical compound [H]N[C@@H](C)C(=O)N[C@@H](CC1=CNC=N1)C(=O)N[C@@H](CCC(O)=O)C(O)=O GRPHQEMIFDPKOE-HGNGGELXSA-N 0.000 claims 1
- SDZRIBWEVVRDQI-CIUDSAMLSA-N Ala-Lys-Asp Chemical compound [H]N[C@@H](C)C(=O)N[C@@H](CCCCN)C(=O)N[C@@H](CC(O)=O)C(O)=O SDZRIBWEVVRDQI-CIUDSAMLSA-N 0.000 claims 1
- MFMDKJIPHSWSBM-GUBZILKMSA-N Ala-Lys-Glu Chemical compound [H]N[C@@H](C)C(=O)N[C@@H](CCCCN)C(=O)N[C@@H](CCC(O)=O)C(O)=O MFMDKJIPHSWSBM-GUBZILKMSA-N 0.000 claims 1
- 241001227713 Chiron Species 0.000 claims 1
- 206010017533 Fungal infection Diseases 0.000 claims 1
- SACHLUOUHCVIKI-GMOBBJLQSA-N Ile-Arg-Asp Chemical compound CC[C@H](C)[C@@H](C(=O)N[C@@H](CCCN=C(N)N)C(=O)N[C@@H](CC(=O)O)C(=O)O)N SACHLUOUHCVIKI-GMOBBJLQSA-N 0.000 claims 1
- FVEWRQXNISSYFO-ZPFDUUQYSA-N Ile-Arg-Glu Chemical compound CC[C@H](C)[C@@H](C(=O)N[C@@H](CCCN=C(N)N)C(=O)N[C@@H](CCC(=O)O)C(=O)O)N FVEWRQXNISSYFO-ZPFDUUQYSA-N 0.000 claims 1
- UMYZBHKAVTXWIW-GMOBBJLQSA-N Ile-Asp-Arg Chemical compound CC[C@H](C)[C@@H](C(=O)N[C@@H](CC(=O)O)C(=O)N[C@@H](CCCN=C(N)N)C(=O)O)N UMYZBHKAVTXWIW-GMOBBJLQSA-N 0.000 claims 1
- JQLFYZMEXFNRFS-DJFWLOJKSA-N Ile-Asp-His Chemical compound CC[C@H](C)[C@@H](C(=O)N[C@@H](CC(=O)O)C(=O)N[C@@H](CC1=CN=CN1)C(=O)O)N JQLFYZMEXFNRFS-DJFWLOJKSA-N 0.000 claims 1
- QSPLUJGYOPZINY-ZPFDUUQYSA-N Ile-Asp-Lys Chemical compound CC[C@H](C)[C@@H](C(=O)N[C@@H](CC(=O)O)C(=O)N[C@@H](CCCCN)C(=O)O)N QSPLUJGYOPZINY-ZPFDUUQYSA-N 0.000 claims 1
- JDAWAWXGAUZPNJ-ZPFDUUQYSA-N Ile-Glu-Arg Chemical compound CC[C@H](C)[C@@H](C(=O)N[C@@H](CCC(=O)O)C(=O)N[C@@H](CCCN=C(N)N)C(=O)O)N JDAWAWXGAUZPNJ-ZPFDUUQYSA-N 0.000 claims 1
- IXEFKXAGHRQFAF-HVTMNAMFSA-N Ile-Glu-His Chemical compound CC[C@H](C)[C@@H](C(=O)N[C@@H](CCC(=O)O)C(=O)N[C@@H](CC1=CN=CN1)C(=O)O)N IXEFKXAGHRQFAF-HVTMNAMFSA-N 0.000 claims 1
- DFJJAVZIHDFOGQ-MNXVOIDGSA-N Ile-Glu-Lys Chemical compound CC[C@H](C)[C@@H](C(=O)N[C@@H](CCC(=O)O)C(=O)N[C@@H](CCCCN)C(=O)O)N DFJJAVZIHDFOGQ-MNXVOIDGSA-N 0.000 claims 1
- UQXADIGYEYBJEI-DJFWLOJKSA-N Ile-His-Asp Chemical compound CC[C@H](C)[C@@H](C(=O)N[C@@H](CC1=CN=CN1)C(=O)N[C@@H](CC(=O)O)C(=O)O)N UQXADIGYEYBJEI-DJFWLOJKSA-N 0.000 claims 1
- YKLOMBNBQUTJDT-HVTMNAMFSA-N Ile-His-Glu Chemical compound CC[C@H](C)[C@@H](C(=O)N[C@@H](CC1=CN=CN1)C(=O)N[C@@H](CCC(=O)O)C(=O)O)N YKLOMBNBQUTJDT-HVTMNAMFSA-N 0.000 claims 1
- RMNMUUCYTMLWNA-ZPFDUUQYSA-N Ile-Lys-Asp Chemical compound CC[C@H](C)[C@@H](C(=O)N[C@@H](CCCCN)C(=O)N[C@@H](CC(=O)O)C(=O)O)N RMNMUUCYTMLWNA-ZPFDUUQYSA-N 0.000 claims 1
- ADDYYRVQQZFIMW-MNXVOIDGSA-N Ile-Lys-Glu Chemical compound CC[C@H](C)[C@@H](C(=O)N[C@@H](CCCCN)C(=O)N[C@@H](CCC(=O)O)C(=O)O)N ADDYYRVQQZFIMW-MNXVOIDGSA-N 0.000 claims 1
- REPPKAMYTOJTFC-DCAQKATOSA-N Leu-Arg-Asp Chemical compound [H]N[C@@H](CC(C)C)C(=O)N[C@@H](CCCNC(N)=N)C(=O)N[C@@H](CC(O)=O)C(O)=O REPPKAMYTOJTFC-DCAQKATOSA-N 0.000 claims 1
- HASRFYOMVPJRPU-SRVKXCTJSA-N Leu-Arg-Glu Chemical compound CC(C)C[C@H](N)C(=O)N[C@@H](CCCN=C(N)N)C(=O)N[C@@H](CCC(O)=O)C(O)=O HASRFYOMVPJRPU-SRVKXCTJSA-N 0.000 claims 1
- YKNBJXOJTURHCU-DCAQKATOSA-N Leu-Asp-Arg Chemical compound CC(C)C[C@H](N)C(=O)N[C@@H](CC(O)=O)C(=O)N[C@H](C(O)=O)CCCN=C(N)N YKNBJXOJTURHCU-DCAQKATOSA-N 0.000 claims 1
- ZDSNOSQHMJBRQN-SRVKXCTJSA-N Leu-Asp-His Chemical compound CC(C)C[C@@H](C(=O)N[C@@H](CC(=O)O)C(=O)N[C@@H](CC1=CN=CN1)C(=O)O)N ZDSNOSQHMJBRQN-SRVKXCTJSA-N 0.000 claims 1
- MYGQXVYRZMKRDB-SRVKXCTJSA-N Leu-Asp-Lys Chemical compound CC(C)C[C@H](N)C(=O)N[C@@H](CC(O)=O)C(=O)N[C@H](C(O)=O)CCCCN MYGQXVYRZMKRDB-SRVKXCTJSA-N 0.000 claims 1
- RVVBWTWPNFDYBE-SRVKXCTJSA-N Leu-Glu-Arg Chemical compound [H]N[C@@H](CC(C)C)C(=O)N[C@@H](CCC(O)=O)C(=O)N[C@@H](CCCNC(N)=N)C(O)=O RVVBWTWPNFDYBE-SRVKXCTJSA-N 0.000 claims 1
- IWTBYNQNAPECCS-AVGNSLFASA-N Leu-Glu-His Chemical compound CC(C)C[C@H](N)C(=O)N[C@@H](CCC(O)=O)C(=O)N[C@H](C(O)=O)CC1=CN=CN1 IWTBYNQNAPECCS-AVGNSLFASA-N 0.000 claims 1
- HQUXQAMSWFIRET-AVGNSLFASA-N Leu-Glu-Lys Chemical compound CC(C)C[C@H](N)C(=O)N[C@@H](CCC(O)=O)C(=O)N[C@H](C(O)=O)CCCCN HQUXQAMSWFIRET-AVGNSLFASA-N 0.000 claims 1
- YWYQSLOTVIRCFE-SRVKXCTJSA-N Leu-His-Asp Chemical compound [H]N[C@@H](CC(C)C)C(=O)N[C@@H](CC1=CNC=N1)C(=O)N[C@@H](CC(O)=O)C(O)=O YWYQSLOTVIRCFE-SRVKXCTJSA-N 0.000 claims 1
- KXODZBLFVFSLAI-AVGNSLFASA-N Leu-His-Glu Chemical compound OC(=O)CC[C@@H](C(O)=O)NC(=O)[C@@H](NC(=O)[C@@H](N)CC(C)C)CC1=CN=CN1 KXODZBLFVFSLAI-AVGNSLFASA-N 0.000 claims 1
- RZXLZBIUTDQHJQ-SRVKXCTJSA-N Leu-Lys-Asp Chemical compound [H]N[C@@H](CC(C)C)C(=O)N[C@@H](CCCCN)C(=O)N[C@@H](CC(O)=O)C(O)=O RZXLZBIUTDQHJQ-SRVKXCTJSA-N 0.000 claims 1
- HVHRPWQEQHIQJF-AVGNSLFASA-N Leu-Lys-Glu Chemical compound [H]N[C@@H](CC(C)C)C(=O)N[C@@H](CCCCN)C(=O)N[C@@H](CCC(O)=O)C(O)=O HVHRPWQEQHIQJF-AVGNSLFASA-N 0.000 claims 1
- CWFYZYQMUDWGTI-GUBZILKMSA-N Met-Arg-Asp Chemical compound [H]N[C@@H](CCSC)C(=O)N[C@@H](CCCNC(N)=N)C(=O)N[C@@H](CC(O)=O)C(O)=O CWFYZYQMUDWGTI-GUBZILKMSA-N 0.000 claims 1
- CTVJSFRHUOSCQQ-DCAQKATOSA-N Met-Arg-Glu Chemical compound CSCC[C@H](N)C(=O)N[C@@H](CCCNC(N)=N)C(=O)N[C@@H](CCC(O)=O)C(O)=O CTVJSFRHUOSCQQ-DCAQKATOSA-N 0.000 claims 1
- SQUTUWHAAWJYES-GUBZILKMSA-N Met-Asp-Arg Chemical compound [H]N[C@@H](CCSC)C(=O)N[C@@H](CC(O)=O)C(=O)N[C@@H](CCCNC(N)=N)C(O)=O SQUTUWHAAWJYES-GUBZILKMSA-N 0.000 claims 1
- DRINJBAHUGXNFC-DCAQKATOSA-N Met-Asp-His Chemical compound [H]N[C@@H](CCSC)C(=O)N[C@@H](CC(O)=O)C(=O)N[C@@H](CC1=CNC=N1)C(O)=O DRINJBAHUGXNFC-DCAQKATOSA-N 0.000 claims 1
- WGBMNLCRYKSWAR-DCAQKATOSA-N Met-Asp-Lys Chemical compound CSCC[C@H](N)C(=O)N[C@@H](CC(O)=O)C(=O)N[C@H](C(O)=O)CCCCN WGBMNLCRYKSWAR-DCAQKATOSA-N 0.000 claims 1
- KQBJYJXPZBNEIK-DCAQKATOSA-N Met-Glu-Arg Chemical compound CSCC[C@H](N)C(=O)N[C@@H](CCC(O)=O)C(=O)N[C@H](C(O)=O)CCCNC(N)=N KQBJYJXPZBNEIK-DCAQKATOSA-N 0.000 claims 1
- PQPMMGQTRQFSDA-SRVKXCTJSA-N Met-Glu-His Chemical compound [H]N[C@@H](CCSC)C(=O)N[C@@H](CCC(O)=O)C(=O)N[C@@H](CC1=CNC=N1)C(O)=O PQPMMGQTRQFSDA-SRVKXCTJSA-N 0.000 claims 1
- VZBXCMCHIHEPBL-SRVKXCTJSA-N Met-Glu-Lys Chemical compound CSCC[C@H](N)C(=O)N[C@@H](CCC(O)=O)C(=O)N[C@H](C(O)=O)CCCCN VZBXCMCHIHEPBL-SRVKXCTJSA-N 0.000 claims 1
- OBCRZLRPJFNLAN-DCAQKATOSA-N Met-His-Asp Chemical compound [H]N[C@@H](CCSC)C(=O)N[C@@H](CC1=CNC=N1)C(=O)N[C@@H](CC(O)=O)C(O)=O OBCRZLRPJFNLAN-DCAQKATOSA-N 0.000 claims 1
- RKIIYGUHIQJCBW-SRVKXCTJSA-N Met-His-Glu Chemical compound [H]N[C@@H](CCSC)C(=O)N[C@@H](CC1=CNC=N1)C(=O)N[C@@H](CCC(O)=O)C(O)=O RKIIYGUHIQJCBW-SRVKXCTJSA-N 0.000 claims 1
- YYEIFXZOBZVDPH-DCAQKATOSA-N Met-Lys-Asp Chemical compound CSCC[C@H](N)C(=O)N[C@@H](CCCCN)C(=O)N[C@@H](CC(O)=O)C(O)=O YYEIFXZOBZVDPH-DCAQKATOSA-N 0.000 claims 1
- WPTHAGXMYDRPFD-SRVKXCTJSA-N Met-Lys-Glu Chemical compound CSCC[C@H](N)C(=O)N[C@@H](CCCCN)C(=O)N[C@@H](CCC(O)=O)C(O)=O WPTHAGXMYDRPFD-SRVKXCTJSA-N 0.000 claims 1
- 208000031888 Mycoses Diseases 0.000 claims 1
- VHWOBXIWBDWZHK-IHRRRGAJSA-N Phe-Arg-Asp Chemical compound NC(N)=NCCC[C@@H](C(=O)N[C@@H](CC(O)=O)C(O)=O)NC(=O)[C@@H](N)CC1=CC=CC=C1 VHWOBXIWBDWZHK-IHRRRGAJSA-N 0.000 claims 1
- MPGJIHFJCXTVEX-KKUMJFAQSA-N Phe-Arg-Glu Chemical compound [H]N[C@@H](CC1=CC=CC=C1)C(=O)N[C@@H](CCCNC(N)=N)C(=O)N[C@@H](CCC(O)=O)C(O)=O MPGJIHFJCXTVEX-KKUMJFAQSA-N 0.000 claims 1
- XMPUYNHKEPFERE-IHRRRGAJSA-N Phe-Asp-Arg Chemical compound NC(N)=NCCC[C@@H](C(O)=O)NC(=O)[C@H](CC(O)=O)NC(=O)[C@@H](N)CC1=CC=CC=C1 XMPUYNHKEPFERE-IHRRRGAJSA-N 0.000 claims 1
- VUYCNYVLKACHPA-KKUMJFAQSA-N Phe-Asp-His Chemical compound C1=CC=C(C=C1)C[C@@H](C(=O)N[C@@H](CC(=O)O)C(=O)N[C@@H](CC2=CN=CN2)C(=O)O)N VUYCNYVLKACHPA-KKUMJFAQSA-N 0.000 claims 1
- WIVCOAKLPICYGY-KKUMJFAQSA-N Phe-Asp-Lys Chemical compound C1=CC=C(C=C1)C[C@@H](C(=O)N[C@@H](CC(=O)O)C(=O)N[C@@H](CCCCN)C(=O)O)N WIVCOAKLPICYGY-KKUMJFAQSA-N 0.000 claims 1
- HOYQLNNGMHXZDW-KKUMJFAQSA-N Phe-Glu-Arg Chemical compound [H]N[C@@H](CC1=CC=CC=C1)C(=O)N[C@@H](CCC(O)=O)C(=O)N[C@@H](CCCNC(N)=N)C(O)=O HOYQLNNGMHXZDW-KKUMJFAQSA-N 0.000 claims 1
- AKJAKCBHLJGRBU-JYJNAYRXSA-N Phe-Glu-His Chemical compound C1=CC=C(C=C1)C[C@@H](C(=O)N[C@@H](CCC(=O)O)C(=O)N[C@@H](CC2=CN=CN2)C(=O)O)N AKJAKCBHLJGRBU-JYJNAYRXSA-N 0.000 claims 1
- PSKRILMFHNIUAO-JYJNAYRXSA-N Phe-Glu-Lys Chemical compound C1=CC=C(C=C1)C[C@@H](C(=O)N[C@@H](CCC(=O)O)C(=O)N[C@@H](CCCCN)C(=O)O)N PSKRILMFHNIUAO-JYJNAYRXSA-N 0.000 claims 1
- FXYXBEZMRACDDR-KKUMJFAQSA-N Phe-His-Asp Chemical compound [H]N[C@@H](CC1=CC=CC=C1)C(=O)N[C@@H](CC1=CNC=N1)C(=O)N[C@@H](CC(O)=O)C(O)=O FXYXBEZMRACDDR-KKUMJFAQSA-N 0.000 claims 1
- ISYSEOWLRQKQEQ-JYJNAYRXSA-N Phe-His-Glu Chemical compound [H]N[C@@H](CC1=CC=CC=C1)C(=O)N[C@@H](CC1=CNC=N1)C(=O)N[C@@H](CCC(O)=O)C(O)=O ISYSEOWLRQKQEQ-JYJNAYRXSA-N 0.000 claims 1
- OQTDZEJJWWAGJT-KKUMJFAQSA-N Phe-Lys-Asp Chemical compound [H]N[C@@H](CC1=CC=CC=C1)C(=O)N[C@@H](CCCCN)C(=O)N[C@@H](CC(O)=O)C(O)=O OQTDZEJJWWAGJT-KKUMJFAQSA-N 0.000 claims 1
- WLYPRKLMRIYGPP-JYJNAYRXSA-N Phe-Lys-Glu Chemical compound OC(=O)CC[C@@H](C(O)=O)NC(=O)[C@H](CCCCN)NC(=O)[C@@H](N)CC1=CC=CC=C1 WLYPRKLMRIYGPP-JYJNAYRXSA-N 0.000 claims 1
- 241000224016 Plasmodium Species 0.000 claims 1
- 241000223810 Plasmodium vivax Species 0.000 claims 1
- 206010057244 Post viral fatigue syndrome Diseases 0.000 claims 1
- SSSFPISOZOLQNP-GUBZILKMSA-N Pro-Arg-Asp Chemical compound [H]N1CCC[C@H]1C(=O)N[C@@H](CCCNC(N)=N)C(=O)N[C@@H](CC(O)=O)C(O)=O SSSFPISOZOLQNP-GUBZILKMSA-N 0.000 claims 1
- IHCXPSYCHXFXKT-DCAQKATOSA-N Pro-Arg-Glu Chemical compound [H]N1CCC[C@H]1C(=O)N[C@@H](CCCNC(N)=N)C(=O)N[C@@H](CCC(O)=O)C(O)=O IHCXPSYCHXFXKT-DCAQKATOSA-N 0.000 claims 1
- JARJPEMLQAWNBR-GUBZILKMSA-N Pro-Asp-Arg Chemical compound [H]N1CCC[C@H]1C(=O)N[C@@H](CC(O)=O)C(=O)N[C@@H](CCCNC(N)=N)C(O)=O JARJPEMLQAWNBR-GUBZILKMSA-N 0.000 claims 1
- KIGGUSRFHJCIEJ-DCAQKATOSA-N Pro-Asp-His Chemical compound C1C[C@H](NC1)C(=O)N[C@@H](CC(=O)O)C(=O)N[C@@H](CC2=CN=CN2)C(=O)O KIGGUSRFHJCIEJ-DCAQKATOSA-N 0.000 claims 1
- XKHCJJPNXFBADI-DCAQKATOSA-N Pro-Asp-Lys Chemical compound C1C[C@H](NC1)C(=O)N[C@@H](CC(=O)O)C(=O)N[C@@H](CCCCN)C(=O)O XKHCJJPNXFBADI-DCAQKATOSA-N 0.000 claims 1
- PULPZRAHVFBVTO-DCAQKATOSA-N Pro-Glu-Arg Chemical compound [H]N1CCC[C@H]1C(=O)N[C@@H](CCC(O)=O)C(=O)N[C@@H](CCCNC(N)=N)C(O)=O PULPZRAHVFBVTO-DCAQKATOSA-N 0.000 claims 1
- VPFGPKIWSDVTOY-SRVKXCTJSA-N Pro-Glu-His Chemical compound C1C[C@H](NC1)C(=O)N[C@@H](CCC(=O)O)C(=O)N[C@@H](CC2=CN=CN2)C(=O)O VPFGPKIWSDVTOY-SRVKXCTJSA-N 0.000 claims 1
- VOZIBWWZSBIXQN-SRVKXCTJSA-N Pro-Glu-Lys Chemical compound NCCCC[C@H](NC(=O)[C@H](CCC(O)=O)NC(=O)[C@@H]1CCCN1)C(O)=O VOZIBWWZSBIXQN-SRVKXCTJSA-N 0.000 claims 1
- GBRUQFBAJOKCTF-DCAQKATOSA-N Pro-His-Asp Chemical compound [H]N1CCC[C@H]1C(=O)N[C@@H](CC1=CNC=N1)C(=O)N[C@@H](CC(O)=O)C(O)=O GBRUQFBAJOKCTF-DCAQKATOSA-N 0.000 claims 1
- AJCRQOHDLCBHFA-SRVKXCTJSA-N Pro-His-Glu Chemical compound [H]N1CCC[C@H]1C(=O)N[C@@H](CC1=CNC=N1)C(=O)N[C@@H](CCC(O)=O)C(O)=O AJCRQOHDLCBHFA-SRVKXCTJSA-N 0.000 claims 1
- ZLXKLMHAMDENIO-DCAQKATOSA-N Pro-Lys-Asp Chemical compound [H]N1CCC[C@H]1C(=O)N[C@@H](CCCCN)C(=O)N[C@@H](CC(O)=O)C(O)=O ZLXKLMHAMDENIO-DCAQKATOSA-N 0.000 claims 1
- XQPHBAKJJJZOBX-SRVKXCTJSA-N Pro-Lys-Glu Chemical compound [H]N1CCC[C@H]1C(=O)N[C@@H](CCCCN)C(=O)N[C@@H](CCC(O)=O)C(O)=O XQPHBAKJJJZOBX-SRVKXCTJSA-N 0.000 claims 1
- 206010040070 Septic Shock Diseases 0.000 claims 1
- 208000021386 Sjogren Syndrome Diseases 0.000 claims 1
- 206010052779 Transplant rejections Diseases 0.000 claims 1
- TZNNEYFZZAHLBL-BPUTZDHNSA-N Trp-Arg-Asp Chemical compound [H]N[C@@H](CC1=CNC2=C1C=CC=C2)C(=O)N[C@@H](CCCNC(N)=N)C(=O)N[C@@H](CC(O)=O)C(O)=O TZNNEYFZZAHLBL-BPUTZDHNSA-N 0.000 claims 1
- HYNAKPYFEYJMAS-XIRDDKMYSA-N Trp-Arg-Glu Chemical compound [H]N[C@@H](CC1=CNC2=C1C=CC=C2)C(=O)N[C@@H](CCCNC(N)=N)C(=O)N[C@@H](CCC(O)=O)C(O)=O HYNAKPYFEYJMAS-XIRDDKMYSA-N 0.000 claims 1
- GKUROEIXVURAAO-BPUTZDHNSA-N Trp-Asp-Arg Chemical compound [H]N[C@@H](CC1=CNC2=C1C=CC=C2)C(=O)N[C@@H](CC(O)=O)C(=O)N[C@@H](CCCNC(N)=N)C(O)=O GKUROEIXVURAAO-BPUTZDHNSA-N 0.000 claims 1
- MWHOLXNKRKRQQH-XIRDDKMYSA-N Trp-Asp-His Chemical compound C1=CC=C2C(=C1)C(=CN2)C[C@@H](C(=O)N[C@@H](CC(=O)O)C(=O)N[C@@H](CC3=CN=CN3)C(=O)O)N MWHOLXNKRKRQQH-XIRDDKMYSA-N 0.000 claims 1
- HJTYJQVRIQXMHM-XIRDDKMYSA-N Trp-Asp-Lys Chemical compound C1=CC=C2C(=C1)C(=CN2)C[C@@H](C(=O)N[C@@H](CC(=O)O)C(=O)N[C@@H](CCCCN)C(=O)O)N HJTYJQVRIQXMHM-XIRDDKMYSA-N 0.000 claims 1
- PKUJMYZNJMRHEZ-XIRDDKMYSA-N Trp-Glu-Arg Chemical compound [H]N[C@@H](CC1=CNC2=C1C=CC=C2)C(=O)N[C@@H](CCC(O)=O)C(=O)N[C@@H](CCCNC(N)=N)C(O)=O PKUJMYZNJMRHEZ-XIRDDKMYSA-N 0.000 claims 1
- VISUNEBASWEMCU-SZMVWBNQSA-N Trp-Glu-His Chemical compound C1=CC=C2C(=C1)C(=CN2)C[C@@H](C(=O)N[C@@H](CCC(=O)O)C(=O)N[C@@H](CC3=CN=CN3)C(=O)O)N VISUNEBASWEMCU-SZMVWBNQSA-N 0.000 claims 1
- OBAMASZCXDIXSS-SZMVWBNQSA-N Trp-Glu-Lys Chemical compound C1=CC=C2C(=C1)C(=CN2)C[C@@H](C(=O)N[C@@H](CCC(=O)O)C(=O)N[C@@H](CCCCN)C(=O)O)N OBAMASZCXDIXSS-SZMVWBNQSA-N 0.000 claims 1
- OTWIOROMZLNAQC-XIRDDKMYSA-N Trp-His-Asp Chemical compound [H]N[C@@H](CC1=CNC2=C1C=CC=C2)C(=O)N[C@@H](CC1=CNC=N1)C(=O)N[C@@H](CC(O)=O)C(O)=O OTWIOROMZLNAQC-XIRDDKMYSA-N 0.000 claims 1
- PGPCENKYTLDIFM-SZMVWBNQSA-N Trp-His-Glu Chemical compound [H]N[C@@H](CC1=CNC2=C1C=CC=C2)C(=O)N[C@@H](CC1=CNC=N1)C(=O)N[C@@H](CCC(O)=O)C(O)=O PGPCENKYTLDIFM-SZMVWBNQSA-N 0.000 claims 1
- KRCPXGSWDOGHAM-XIRDDKMYSA-N Trp-Lys-Asp Chemical compound [H]N[C@@H](CC1=CNC2=C1C=CC=C2)C(=O)N[C@@H](CCCCN)C(=O)N[C@@H](CC(O)=O)C(O)=O KRCPXGSWDOGHAM-XIRDDKMYSA-N 0.000 claims 1
- HJXOFWKCWLHYIJ-SZMVWBNQSA-N Trp-Lys-Glu Chemical compound [H]N[C@@H](CC1=CNC2=C1C=CC=C2)C(=O)N[C@@H](CCCCN)C(=O)N[C@@H](CCC(O)=O)C(O)=O HJXOFWKCWLHYIJ-SZMVWBNQSA-N 0.000 claims 1
- NMANTMWGQZASQN-QXEWZRGKSA-N Val-Arg-Asp Chemical compound CC(C)[C@@H](C(=O)N[C@@H](CCCN=C(N)N)C(=O)N[C@@H](CC(=O)O)C(=O)O)N NMANTMWGQZASQN-QXEWZRGKSA-N 0.000 claims 1
- KKHRWGYHBZORMQ-NHCYSSNCSA-N Val-Arg-Glu Chemical compound CC(C)[C@@H](C(=O)N[C@@H](CCCN=C(N)N)C(=O)N[C@@H](CCC(=O)O)C(=O)O)N KKHRWGYHBZORMQ-NHCYSSNCSA-N 0.000 claims 1
- XQVRMLRMTAGSFJ-QXEWZRGKSA-N Val-Asp-Arg Chemical compound CC(C)[C@@H](C(=O)N[C@@H](CC(=O)O)C(=O)N[C@@H](CCCN=C(N)N)C(=O)O)N XQVRMLRMTAGSFJ-QXEWZRGKSA-N 0.000 claims 1
- ZQGPWORGSNRQLN-NHCYSSNCSA-N Val-Asp-His Chemical compound CC(C)[C@@H](C(=O)N[C@@H](CC(=O)O)C(=O)N[C@@H](CC1=CN=CN1)C(=O)O)N ZQGPWORGSNRQLN-NHCYSSNCSA-N 0.000 claims 1
- BMGOFDMKDVVGJG-NHCYSSNCSA-N Val-Asp-Lys Chemical compound CC(C)[C@@H](C(=O)N[C@@H](CC(=O)O)C(=O)N[C@@H](CCCCN)C(=O)O)N BMGOFDMKDVVGJG-NHCYSSNCSA-N 0.000 claims 1
- BRPKEERLGYNCNC-NHCYSSNCSA-N Val-Glu-Arg Chemical compound CC(C)[C@H](N)C(=O)N[C@@H](CCC(O)=O)C(=O)N[C@H](C(O)=O)CCCN=C(N)N BRPKEERLGYNCNC-NHCYSSNCSA-N 0.000 claims 1
- YDPFWRVQHFWBKI-GVXVVHGQSA-N Val-Glu-His Chemical compound CC(C)[C@@H](C(=O)N[C@@H](CCC(=O)O)C(=O)N[C@@H](CC1=CN=CN1)C(=O)O)N YDPFWRVQHFWBKI-GVXVVHGQSA-N 0.000 claims 1
- ZXAGTABZUOMUDO-GVXVVHGQSA-N Val-Glu-Lys Chemical compound CC(C)[C@@H](C(=O)N[C@@H](CCC(=O)O)C(=O)N[C@@H](CCCCN)C(=O)O)N ZXAGTABZUOMUDO-GVXVVHGQSA-N 0.000 claims 1
- WJVLTYSHNXRCLT-NHCYSSNCSA-N Val-His-Asp Chemical compound CC(C)[C@@H](C(=O)N[C@@H](CC1=CN=CN1)C(=O)N[C@@H](CC(=O)O)C(=O)O)N WJVLTYSHNXRCLT-NHCYSSNCSA-N 0.000 claims 1
- RHYOAUJXSRWVJT-GVXVVHGQSA-N Val-His-Glu Chemical compound CC(C)[C@@H](C(=O)N[C@@H](CC1=CN=CN1)C(=O)N[C@@H](CCC(=O)O)C(=O)O)N RHYOAUJXSRWVJT-GVXVVHGQSA-N 0.000 claims 1
- KTEZUXISLQTDDQ-NHCYSSNCSA-N Val-Lys-Asp Chemical compound CC(C)[C@@H](C(=O)N[C@@H](CCCCN)C(=O)N[C@@H](CC(=O)O)C(=O)O)N KTEZUXISLQTDDQ-NHCYSSNCSA-N 0.000 claims 1
- IJGPOONOTBNTFS-GVXVVHGQSA-N Val-Lys-Glu Chemical compound [H]N[C@@H](C(C)C)C(=O)N[C@@H](CCCCN)C(=O)N[C@@H](CCC(O)=O)C(O)=O IJGPOONOTBNTFS-GVXVVHGQSA-N 0.000 claims 1
- 230000001363 autoimmune Effects 0.000 claims 1
- 210000001124 body fluid Anatomy 0.000 claims 1
- 239000010839 body fluid Substances 0.000 claims 1
- 210000000234 capsid Anatomy 0.000 claims 1
- 230000000295 complement effect Effects 0.000 claims 1
- 239000000470 constituent Substances 0.000 claims 1
- 238000003745 diagnosis Methods 0.000 claims 1
- 235000003869 genetically modified organism Nutrition 0.000 claims 1
- 239000005556 hormone Substances 0.000 claims 1
- 229940088597 hormone Drugs 0.000 claims 1
- 230000005965 immune activity Effects 0.000 claims 1
- 229930014626 natural product Natural products 0.000 claims 1
- 230000001613 neoplastic effect Effects 0.000 claims 1
- 238000012809 post-inoculation Methods 0.000 claims 1
- 229940021993 prophylactic vaccine Drugs 0.000 claims 1
- 230000036303 septic shock Effects 0.000 claims 1
- 210000002966 serum Anatomy 0.000 claims 1
- 150000003431 steroids Chemical class 0.000 claims 1
- 125000003275 alpha amino acid group Chemical group 0.000 abstract description 22
- 230000003278 mimic effect Effects 0.000 abstract description 13
- 230000028993 immune response Effects 0.000 abstract description 8
- 230000003472 neutralizing effect Effects 0.000 abstract description 7
- 208000030507 AIDS Diseases 0.000 abstract description 5
- 239000012678 infectious agent Substances 0.000 abstract description 5
- 238000002649 immunization Methods 0.000 abstract description 3
- 238000011081 inoculation Methods 0.000 abstract description 2
- 230000007246 mechanism Effects 0.000 abstract description 2
- 239000003443 antiviral agent Substances 0.000 abstract 2
- 208000009329 Graft vs Host Disease Diseases 0.000 abstract 1
- 108010057464 Prolactin Proteins 0.000 abstract 1
- 102000003946 Prolactin Human genes 0.000 abstract 1
- 102000007056 Recombinant Fusion Proteins Human genes 0.000 abstract 1
- 108010008281 Recombinant Fusion Proteins Proteins 0.000 abstract 1
- 238000002648 combination therapy Methods 0.000 abstract 1
- 239000006071 cream Substances 0.000 abstract 1
- FMGSKLZLMKYGDP-USOAJAOKSA-N dehydroepiandrosterone Chemical compound C1[C@@H](O)CC[C@]2(C)[C@H]3CC[C@](C)(C(CC4)=O)[C@@H]4[C@@H]3CC=C21 FMGSKLZLMKYGDP-USOAJAOKSA-N 0.000 abstract 1
- 206010012601 diabetes mellitus Diseases 0.000 abstract 1
- 208000024908 graft versus host disease Diseases 0.000 abstract 1
- 230000008102 immune modulation Effects 0.000 abstract 1
- 210000003563 lymphoid tissue Anatomy 0.000 abstract 1
- 230000007257 malfunction Effects 0.000 abstract 1
- 238000004519 manufacturing process Methods 0.000 abstract 1
- 239000002674 ointment Substances 0.000 abstract 1
- 229940097325 prolactin Drugs 0.000 abstract 1
- 238000001243 protein synthesis Methods 0.000 abstract 1
- 208000024891 symptom Diseases 0.000 abstract 1
- 230000009885 systemic effect Effects 0.000 abstract 1
- 230000014616 translation Effects 0.000 abstract 1
- 102100023635 Alpha-fetoprotein Human genes 0.000 description 16
- 241000725303 Human immunodeficiency virus Species 0.000 description 16
- 108091008874 T cell receptors Proteins 0.000 description 10
- 102000016266 T-Cell Antigen Receptors Human genes 0.000 description 10
- 241000204031 Mycoplasma Species 0.000 description 6
- 244000045947 parasite Species 0.000 description 6
- 208000031886 HIV Infections Diseases 0.000 description 5
- 230000010056 antibody-dependent cellular cytotoxicity Effects 0.000 description 5
- 210000000170 cell membrane Anatomy 0.000 description 5
- 230000012202 endocytosis Effects 0.000 description 5
- 230000001965 increasing effect Effects 0.000 description 5
- 210000002540 macrophage Anatomy 0.000 description 5
- 230000003844 B-cell-activation Effects 0.000 description 4
- 108700018351 Major Histocompatibility Complex Proteins 0.000 description 4
- 241000700605 Viruses Species 0.000 description 4
- 230000004913 activation Effects 0.000 description 4
- 238000006243 chemical reaction Methods 0.000 description 4
- 230000003993 interaction Effects 0.000 description 4
- 239000012528 membrane Substances 0.000 description 4
- 241000894006 Bacteria Species 0.000 description 3
- 210000004366 CD4-positive T-lymphocyte Anatomy 0.000 description 3
- 108010015899 Glycopeptides Proteins 0.000 description 3
- 102000002068 Glycopeptides Human genes 0.000 description 3
- 102000003886 Glycoproteins Human genes 0.000 description 3
- 108090000288 Glycoproteins Proteins 0.000 description 3
- 241000282412 Homo Species 0.000 description 3
- 102000008070 Interferon-gamma Human genes 0.000 description 3
- 108010074328 Interferon-gamma Proteins 0.000 description 3
- 102000000588 Interleukin-2 Human genes 0.000 description 3
- 108010002350 Interleukin-2 Proteins 0.000 description 3
- 208000001388 Opportunistic Infections Diseases 0.000 description 3
- 206010053613 Type IV hypersensitivity reaction Diseases 0.000 description 3
- 230000036755 cellular response Effects 0.000 description 3
- 229940044627 gamma-interferon Drugs 0.000 description 3
- 230000036737 immune function Effects 0.000 description 3
- 230000003834 intracellular effect Effects 0.000 description 3
- 230000001404 mediated effect Effects 0.000 description 3
- 210000001616 monocyte Anatomy 0.000 description 3
- 210000003819 peripheral blood mononuclear cell Anatomy 0.000 description 3
- 230000020382 suppression by virus of host antigen processing and presentation of peptide antigen via MHC class I Effects 0.000 description 3
- 210000001519 tissue Anatomy 0.000 description 3
- 230000005951 type IV hypersensitivity Effects 0.000 description 3
- 208000027930 type IV hypersensitivity disease Diseases 0.000 description 3
- 108090000565 Capsid Proteins Proteins 0.000 description 2
- 101001033233 Homo sapiens Interleukin-10 Proteins 0.000 description 2
- 102000000589 Interleukin-1 Human genes 0.000 description 2
- 108010002352 Interleukin-1 Proteins 0.000 description 2
- 208000007766 Kaposi sarcoma Diseases 0.000 description 2
- 241000222722 Leishmania <genus> Species 0.000 description 2
- 230000003213 activating effect Effects 0.000 description 2
- 239000003795 chemical substances by application Substances 0.000 description 2
- 231100000433 cytotoxic Toxicity 0.000 description 2
- 230000001472 cytotoxic effect Effects 0.000 description 2
- 230000006378 damage Effects 0.000 description 2
- 231100000673 dose–response relationship Toxicity 0.000 description 2
- 102000052620 human IL10 Human genes 0.000 description 2
- 230000004727 humoral immunity Effects 0.000 description 2
- 208000026278 immune system disease Diseases 0.000 description 2
- 230000006028 immune-suppresssive effect Effects 0.000 description 2
- 238000001990 intravenous administration Methods 0.000 description 2
- 230000003902 lesion Effects 0.000 description 2
- 230000002503 metabolic effect Effects 0.000 description 2
- 230000035772 mutation Effects 0.000 description 2
- 230000003071 parasitic effect Effects 0.000 description 2
- 230000003334 potential effect Effects 0.000 description 2
- 230000008569 process Effects 0.000 description 2
- 230000009257 reactivity Effects 0.000 description 2
- 108020003175 receptors Proteins 0.000 description 2
- 102000005962 receptors Human genes 0.000 description 2
- 230000009467 reduction Effects 0.000 description 2
- 230000010076 replication Effects 0.000 description 2
- 230000011664 signaling Effects 0.000 description 2
- 238000002255 vaccination Methods 0.000 description 2
- 102100031126 6-phosphogluconolactonase Human genes 0.000 description 1
- 108010029731 6-phosphogluconolactonase Proteins 0.000 description 1
- 208000035143 Bacterial infection Diseases 0.000 description 1
- 102000004506 Blood Proteins Human genes 0.000 description 1
- 108010017384 Blood Proteins Proteins 0.000 description 1
- 101710132601 Capsid protein Proteins 0.000 description 1
- 101710205625 Capsid protein p24 Proteins 0.000 description 1
- 101710094648 Coat protein Proteins 0.000 description 1
- 208000035473 Communicable disease Diseases 0.000 description 1
- 206010059866 Drug resistance Diseases 0.000 description 1
- 108090000790 Enzymes Proteins 0.000 description 1
- 102000004190 Enzymes Human genes 0.000 description 1
- 108010087819 Fc receptors Proteins 0.000 description 1
- 102000009109 Fc receptors Human genes 0.000 description 1
- 208000034826 Genetic Predisposition to Disease Diseases 0.000 description 1
- 108010018962 Glucosephosphate Dehydrogenase Proteins 0.000 description 1
- 102100021181 Golgi phosphoprotein 3 Human genes 0.000 description 1
- 108060003951 Immunoglobulin Proteins 0.000 description 1
- 238000012404 In vitro experiment Methods 0.000 description 1
- 108700005089 MHC Class I Genes Proteins 0.000 description 1
- 108700005092 MHC Class II Genes Proteins 0.000 description 1
- 101710125418 Major capsid protein Proteins 0.000 description 1
- 241000699670 Mus sp. Species 0.000 description 1
- 241000187479 Mycobacterium tuberculosis Species 0.000 description 1
- 206010028470 Mycoplasma infections Diseases 0.000 description 1
- 101710141454 Nucleoprotein Proteins 0.000 description 1
- 101710177166 Phosphoprotein Proteins 0.000 description 1
- 240000009188 Phyllostachys vivax Species 0.000 description 1
- 241000288906 Primates Species 0.000 description 1
- 101710083689 Probable capsid protein Proteins 0.000 description 1
- 206010038997 Retroviral infections Diseases 0.000 description 1
- 101710149279 Small delta antigen Proteins 0.000 description 1
- 102000014169 Steroid 21-Hydroxylase Human genes 0.000 description 1
- 108010011732 Steroid 21-Hydroxylase Proteins 0.000 description 1
- 230000006044 T cell activation Effects 0.000 description 1
- 230000005867 T cell response Effects 0.000 description 1
- 206010054094 Tumour necrosis Diseases 0.000 description 1
- 230000009471 action Effects 0.000 description 1
- 239000002671 adjuvant Substances 0.000 description 1
- 244000000054 animal parasite Species 0.000 description 1
- 238000009175 antibody therapy Methods 0.000 description 1
- 230000009831 antigen interaction Effects 0.000 description 1
- 210000000612 antigen-presenting cell Anatomy 0.000 description 1
- 208000022362 bacterial infectious disease Diseases 0.000 description 1
- 230000008901 benefit Effects 0.000 description 1
- 102000015736 beta 2-Microglobulin Human genes 0.000 description 1
- 108010081355 beta 2-Microglobulin Proteins 0.000 description 1
- 230000015556 catabolic process Effects 0.000 description 1
- 230000020411 cell activation Effects 0.000 description 1
- 230000003915 cell function Effects 0.000 description 1
- 230000001413 cellular effect Effects 0.000 description 1
- 230000007969 cellular immunity Effects 0.000 description 1
- 210000000349 chromosome Anatomy 0.000 description 1
- 230000008576 chronic process Effects 0.000 description 1
- 230000004154 complement system Effects 0.000 description 1
- 238000012258 culturing Methods 0.000 description 1
- 230000009089 cytolysis Effects 0.000 description 1
- 230000001086 cytosolic effect Effects 0.000 description 1
- 210000001151 cytotoxic T lymphocyte Anatomy 0.000 description 1
- 231100000050 cytotoxic potential Toxicity 0.000 description 1
- 230000003013 cytotoxicity Effects 0.000 description 1
- 231100000135 cytotoxicity Toxicity 0.000 description 1
- 230000034994 death Effects 0.000 description 1
- 231100000517 death Toxicity 0.000 description 1
- 230000007423 decrease Effects 0.000 description 1
- 210000004443 dendritic cell Anatomy 0.000 description 1
- 238000011161 development Methods 0.000 description 1
- 238000010790 dilution Methods 0.000 description 1
- 239000012895 dilution Substances 0.000 description 1
- 230000008034 disappearance Effects 0.000 description 1
- 210000003979 eosinophil Anatomy 0.000 description 1
- 230000006870 function Effects 0.000 description 1
- 210000002443 helper t lymphocyte Anatomy 0.000 description 1
- 230000007236 host immunity Effects 0.000 description 1
- 244000000011 human parasite Species 0.000 description 1
- 230000005934 immune activation Effects 0.000 description 1
- 210000002865 immune cell Anatomy 0.000 description 1
- 230000037451 immune surveillance Effects 0.000 description 1
- 102000018358 immunoglobulin Human genes 0.000 description 1
- 230000006872 improvement Effects 0.000 description 1
- 238000000338 in vitro Methods 0.000 description 1
- 230000001939 inductive effect Effects 0.000 description 1
- 230000001524 infective effect Effects 0.000 description 1
- 238000001802 infusion Methods 0.000 description 1
- 230000005764 inhibitory process Effects 0.000 description 1
- 230000002452 interceptive effect Effects 0.000 description 1
- 238000007918 intramuscular administration Methods 0.000 description 1
- 230000002427 irreversible effect Effects 0.000 description 1
- 210000003734 kidney Anatomy 0.000 description 1
- 210000000265 leukocyte Anatomy 0.000 description 1
- 210000004185 liver Anatomy 0.000 description 1
- 210000004698 lymphocyte Anatomy 0.000 description 1
- 239000003550 marker Substances 0.000 description 1
- 230000008774 maternal effect Effects 0.000 description 1
- 102000006240 membrane receptors Human genes 0.000 description 1
- 108020004084 membrane receptors Proteins 0.000 description 1
- 230000004060 metabolic process Effects 0.000 description 1
- 238000010172 mouse model Methods 0.000 description 1
- 230000000869 mutational effect Effects 0.000 description 1
- 210000000822 natural killer cell Anatomy 0.000 description 1
- 210000000440 neutrophil Anatomy 0.000 description 1
- 230000037361 pathway Effects 0.000 description 1
- 230000035515 penetration Effects 0.000 description 1
- 150000003905 phosphatidylinositols Chemical class 0.000 description 1
- 230000035935 pregnancy Effects 0.000 description 1
- 238000011321 prophylaxis Methods 0.000 description 1
- 230000036647 reaction Effects 0.000 description 1
- 230000001850 reproductive effect Effects 0.000 description 1
- 230000012865 response to insecticide Effects 0.000 description 1
- 238000012216 screening Methods 0.000 description 1
- 230000019491 signal transduction Effects 0.000 description 1
- 210000003046 sporozoite Anatomy 0.000 description 1
- 238000007920 subcutaneous administration Methods 0.000 description 1
- 230000000699 topical effect Effects 0.000 description 1
- 229960001005 tuberculin Drugs 0.000 description 1
- 230000007306 turnover Effects 0.000 description 1
- 239000013598 vector Substances 0.000 description 1
Classifications
-
- 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
-
- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61K—PREPARATIONS FOR MEDICAL, DENTAL OR TOILETRY PURPOSES
- A61K38/00—Medicinal preparations containing peptides
- A61K38/04—Peptides having up to 20 amino acids in a fully defined sequence; Derivatives thereof
- A61K38/06—Tripeptides
-
- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61K—PREPARATIONS FOR MEDICAL, DENTAL OR TOILETRY PURPOSES
- A61K38/00—Medicinal preparations containing peptides
- A61K38/04—Peptides having up to 20 amino acids in a fully defined sequence; Derivatives thereof
- A61K38/08—Peptides having 5 to 11 amino acids
-
- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61K—PREPARATIONS FOR MEDICAL, DENTAL OR TOILETRY PURPOSES
- A61K38/00—Medicinal preparations containing peptides
- A61K38/16—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof
- A61K38/17—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof from animals; from humans
- A61K38/19—Cytokines; Lymphokines; Interferons
- A61K38/20—Interleukins [IL]
- A61K38/2026—IL-4
-
- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61K—PREPARATIONS FOR MEDICAL, DENTAL OR TOILETRY PURPOSES
- A61K38/00—Medicinal preparations containing peptides
- A61K38/16—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof
- A61K38/17—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof from animals; from humans
- A61K38/19—Cytokines; Lymphokines; Interferons
- A61K38/20—Interleukins [IL]
- A61K38/2066—IL-10
-
- 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
- A61K39/385—Haptens or antigens, bound to carriers
-
- 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
- A61K39/395—Antibodies; Immunoglobulins; Immune serum, e.g. antilymphocytic serum
-
- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61P—SPECIFIC THERAPEUTIC ACTIVITY OF CHEMICAL COMPOUNDS OR MEDICINAL PREPARATIONS
- A61P17/00—Drugs for dermatological disorders
-
- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61P—SPECIFIC THERAPEUTIC ACTIVITY OF CHEMICAL COMPOUNDS OR MEDICINAL PREPARATIONS
- A61P25/00—Drugs for disorders of the nervous system
-
- 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
- A61P31/04—Antibacterial agents
-
- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61P—SPECIFIC THERAPEUTIC ACTIVITY OF CHEMICAL COMPOUNDS OR MEDICINAL PREPARATIONS
- A61P33/00—Antiparasitic agents
- A61P33/02—Antiprotozoals, e.g. for leishmaniasis, trichomoniasis, toxoplasmosis
- A61P33/06—Antimalarials
-
- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61P—SPECIFIC THERAPEUTIC ACTIVITY OF CHEMICAL COMPOUNDS OR MEDICINAL PREPARATIONS
- A61P37/00—Drugs for immunological or allergic disorders
- A61P37/02—Immunomodulators
- A61P37/04—Immunostimulants
-
- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61P—SPECIFIC THERAPEUTIC ACTIVITY OF CHEMICAL COMPOUNDS OR MEDICINAL PREPARATIONS
- A61P37/00—Drugs for immunological or allergic disorders
- A61P37/02—Immunomodulators
- A61P37/06—Immunosuppressants, e.g. drugs for graft rejection
-
- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61P—SPECIFIC THERAPEUTIC ACTIVITY OF CHEMICAL COMPOUNDS OR MEDICINAL PREPARATIONS
- A61P43/00—Drugs for specific purposes, not provided for in groups A61P1/00-A61P41/00
-
- C—CHEMISTRY; METALLURGY
- C07—ORGANIC CHEMISTRY
- C07K—PEPTIDES
- C07K14/00—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof
- C07K14/435—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof from animals; from humans
- C07K14/46—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof from animals; from humans from vertebrates
- C07K14/47—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof from animals; from humans from vertebrates from mammals
- C07K14/4701—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof from animals; from humans from vertebrates from mammals not used
- C07K14/4715—Pregnancy proteins, e.g. placenta proteins, alpha-feto-protein, pregnancy specific beta glycoprotein
-
- C—CHEMISTRY; METALLURGY
- C07—ORGANIC CHEMISTRY
- C07K—PEPTIDES
- C07K14/00—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof
- C07K14/435—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof from animals; from humans
- C07K14/52—Cytokines; Lymphokines; Interferons
- C07K14/54—Interleukins [IL]
- C07K14/5428—IL-10
-
- C—CHEMISTRY; METALLURGY
- C07—ORGANIC CHEMISTRY
- C07K—PEPTIDES
- C07K14/00—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof
- C07K14/435—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof from animals; from humans
- C07K14/52—Cytokines; Lymphokines; Interferons
- C07K14/54—Interleukins [IL]
- C07K14/5434—IL-12
-
- C—CHEMISTRY; METALLURGY
- C07—ORGANIC CHEMISTRY
- C07K—PEPTIDES
- C07K16/00—Immunoglobulins [IGs], e.g. monoclonal or polyclonal antibodies
- C07K16/08—Immunoglobulins [IGs], e.g. monoclonal or polyclonal antibodies against material from viruses
- C07K16/10—Immunoglobulins [IGs], e.g. monoclonal or polyclonal antibodies against material from viruses from RNA viruses
- C07K16/1036—Retroviridae, e.g. leukemia viruses
- C07K16/1045—Lentiviridae, e.g. HIV, FIV, SIV
- C07K16/1063—Lentiviridae, e.g. HIV, FIV, SIV env, e.g. gp41, gp110/120, gp160, V3, PND, CD4 binding site
-
- C—CHEMISTRY; METALLURGY
- C07—ORGANIC CHEMISTRY
- C07K—PEPTIDES
- C07K16/00—Immunoglobulins [IGs], e.g. monoclonal or polyclonal antibodies
- C07K16/18—Immunoglobulins [IGs], e.g. monoclonal or polyclonal antibodies against material from animals or humans
-
- C—CHEMISTRY; METALLURGY
- C07—ORGANIC CHEMISTRY
- C07K—PEPTIDES
- C07K16/00—Immunoglobulins [IGs], e.g. monoclonal or polyclonal antibodies
- C07K16/18—Immunoglobulins [IGs], e.g. monoclonal or polyclonal antibodies against material from animals or humans
- C07K16/24—Immunoglobulins [IGs], e.g. monoclonal or polyclonal antibodies against material from animals or humans against cytokines, lymphokines or interferons
- C07K16/244—Interleukins [IL]
-
- C—CHEMISTRY; METALLURGY
- C07—ORGANIC CHEMISTRY
- C07K—PEPTIDES
- C07K16/00—Immunoglobulins [IGs], e.g. monoclonal or polyclonal antibodies
- C07K16/18—Immunoglobulins [IGs], e.g. monoclonal or polyclonal antibodies against material from animals or humans
- C07K16/24—Immunoglobulins [IGs], e.g. monoclonal or polyclonal antibodies against material from animals or humans against cytokines, lymphokines or interferons
- C07K16/244—Interleukins [IL]
- C07K16/247—IL-4
-
- C—CHEMISTRY; METALLURGY
- C07—ORGANIC CHEMISTRY
- C07K—PEPTIDES
- C07K4/00—Peptides having up to 20 amino acids in an undefined or only partially defined sequence; Derivatives thereof
-
- C—CHEMISTRY; METALLURGY
- C07—ORGANIC CHEMISTRY
- C07K—PEPTIDES
- C07K5/00—Peptides containing up to four amino acids in a fully defined sequence; Derivatives thereof
- C07K5/04—Peptides containing up to four amino acids in a fully defined sequence; Derivatives thereof containing only normal peptide links
- C07K5/08—Tripeptides
-
- C—CHEMISTRY; METALLURGY
- C07—ORGANIC CHEMISTRY
- C07K—PEPTIDES
- C07K7/00—Peptides having 5 to 20 amino acids in a fully defined sequence; Derivatives thereof
- C07K7/04—Linear peptides containing only normal peptide links
- C07K7/08—Linear peptides containing only normal peptide links having 12 to 20 amino acids
-
- 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
- G01N33/56988—HIV or HTLV
-
- 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
- C12N2740/00—Reverse transcribing RNA viruses
- C12N2740/00011—Details
- C12N2740/10011—Retroviridae
-
- 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
- C12N2740/00—Reverse transcribing RNA viruses
- C12N2740/00011—Details
- C12N2740/10011—Retroviridae
- C12N2740/15011—Lentivirus, not HIV, e.g. FIV, SIV
- C12N2740/15022—New viral proteins or individual genes, new structural or functional aspects of known viral proteins or genes
-
- 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
- C12N2740/00—Reverse transcribing RNA viruses
- C12N2740/00011—Details
- C12N2740/10011—Retroviridae
- C12N2740/16011—Human Immunodeficiency Virus, HIV
- C12N2740/16111—Human Immunodeficiency Virus, HIV concerning HIV env
-
- 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
- C12N2740/00—Reverse transcribing RNA viruses
- C12N2740/00011—Details
- C12N2740/10011—Retroviridae
- C12N2740/16011—Human Immunodeficiency Virus, HIV
- C12N2740/16111—Human Immunodeficiency Virus, HIV concerning HIV env
- C12N2740/16122—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
- 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
Definitions
- the host is then capable of overcoming an infectious challenge without becoming infected or producing the usual antibody and autoantibody peak and subsequent immunosuppression normally associated with infections caused by organisms who utilise these specific amino acid sequences to direct the hosts immune signalling system towards a more pronounced B cell or Th 2 cytokine profiled response.
- Malaria is one of the most important infectious diseases in the World, each year there are 270 million new infections resulting in over 100 million episodes of illness and approximately 2 million deaths. World-wide the malaria problem is getting worse each year.
- the reason for this worsening situation include (A) increased levels of drug resistance on the part of the parasites, (B) increased levels of insecticide resistance on the part of the vectors .
- No vaccine has yet been produced which can successfully induce a protective antibody response and the reason for this is that although antibodies which cross react with many epitopes of the P.
- vivax circumsporozoite are produced in abundance by the current unprotective vaccine candidates, because of the immune blind spot or immunologically privileged sites offered by these specific sequences identified herein, like Interleukin 10 and AFP are not visible to the host immune system which both allow the parasite to gain access to the host cell and to cause the non-specific polyclonal B cell activation and immunosuppressive (Interleukin 10 and/or AFP) like effects which are so universal for people suffering from parasites such as malaria, and Leishmania, the host cannot gain enough immune reactive monocytes to overcome the infection initially because these Interleukin 10/AFP mimic molecules carried by the infecting organism shuts down the vital Th x T cell response needed to clear intra-cellular infections.
- Interleukin 10 and AFP non-specific polyclonal B cell activation and immunosuppressive
- a vaccine for malaria which will enable a human to raise a protective antibody titre against malaria sufficient to prevent infection may be manufactured using amino acid sequences displaying these specific polar arrays.
- Another method expected to be more successful as a vaccine combination is to use passive immunisation with either polyclonal or monoclonal antibodies to these said specific sequences generated either in animal human and/or tissue culture given either before or simultaneously with any of the current malaria vaccine candidates which previously could not produce a protective immune response.
- the said specific sequence when embedded in the cell membrane of the host activate the phosphatidylinositol pathway, which causes the release of Ca++, the phosphosylation of cell proteins and the activation or enhanced activity of certain enzymes related to metabolism. This does not occur in the presence of antibodies to the disclosed specific sequences and the organism like malaria, Mycobacterium Tuberculosis, Leishmania, HIV and others are not able to cause metabolic and immune Th 2 activation and exhaustion. It is an important coincidence that in certain malaria endemic areas that genetic mutations that have caused the deletion of the metabolic activity control enzyme glucose- 6 -phosphate dehydrogenase has conferred on the host immunity to malaria. By intervening at an early stage of infection and neutralising certain properties of the malaria parasite to alter cellular reactions by interfering with these specific membrane signal transduction sequences as defined herein it is possible to confer protective immunity to this organism.
- the present invention utilises the novel discovery that certain amino acid sequences which exhibit specific Ion (bridge) pair arrays enclosed on at least one side by non-polar hydrophobic transmembrane segments can be utilised to enhance the humoral antibody response and down-regulate the T cell or delayed-type hypersensitivity (DTH) response of humans and animals.
- Ion bridge
- DTH delayed-type hypersensitivity
- CD3/TCR mimic membrane interaction molecules which present as hydrophobic Ion bridge pairs are utilised by both the organism itself as specific peptides and by cytokines and also by infectious agents to modulate immune response (A) during periods of reproductive foetal gestation as with the alpha-fetoprotein molecule to prevent foetal rejection by the maternal immune system and (B) during cytokine control of immune functions as with cytokine synthesis inhibitory factor (Interleukin 10) when a Th 2 cytokine profile is required or to curtail the uncontrolled Th ⁇ T4 cell immune response.
- cytokine This cytokine (IL-10) is particularly evident following vaccination to enhance humoral immunity and secure antibody formation, and often causes the temporary disappearance of the Tuberculin reaction which is associated with Th : (DTH) response in patients following vaccination.
- Infectious agents such as viruses (RNA & DNA) mycoplasma, bacteria, malaria and a wide array of human and animal parasites also carry these specific charged array of amino acid sequences which cause the down regulation of the T4 cell response and enhance the humoral (antibody mediated) immune response of their infected host, see sample listing enclosed.
- Anti-serum generated to these specific sequences as presented in AFP, Interleukin 10, EBV-BCRF1 and other peptides and as specified in amino acid sequence, listing enclosed, with this patent can be used to remove Interleukin 10 mimic molecules from the circulation of immunosuppressed patients suffering from viral and/or bacterial and/or fungal, mycoplasmic or parasitic infections, which infection's principle method of defence against the host is to stimulate a Th2 cytokine response and curtail or abolish the Thl cell mediated immune attack.
- This invention relates to methods of treatment of persons and animals with indications of immunodeficiency, wherein the said indication is resultant from viral and/or retroviral infection and/or infectious parasites, bacteria and/or mycoplasma.
- the invention further relates to treatment with the above antiserum either poly or monoclonal in nature for establishing improved immuno response for persons and prophylactic treatment for persons where immuno-malfunction due to genetic pre-disposition or infection is considered a future risk.
- the invention further relates to a screening method for vaccines, manufactured by the use of coat or other peptides from viral, bacterial, parasitic or mycoplasma, to determine and remove and/or neutralise inherent immune suppressive properties - such suppressive potential properties is determined by the manufactured vaccine's reactivity with the said specific amino acid sequences as outlined herein, be they synthetic or natural in origin, e.g. AFP, Interleukin 10, viral or bacterial coat peptides.
- the host organism man or animal
- Treatments used according to this invention employing the poly or monoclonal antiserum to these specific cytokine inhibitory sequences are administered as treatments against viral, bacterial and mycoplasma and parasitic infections which cause immunosuppression by any suitable route including enteric, parenteral, topical, oral, rectal, nasal or vaginal routes.
- Parenteral routes include subcutaneous, intramuscular, intravenous and sublingual administration. The preferred route of administration would be an intravenous one.
- the present invention further provides pharmaceutical formulations, for use in treatments against HIV/HTLV- 1 , II, III and other viral diseases and diseases caused by mycoplasma, bacteria or parasites.
- the present invention also relates to a method comprising inoculating into a patient a human, animal, synthetic or recombinant amino acid sequence with or without adjuvant, to produce an antibody response, the antibodies, mono or polyclonal will cause the binding of the immunosuppressive CD3/TCR mimic interaction molecules already present in the plasma of the infected host will be removed from the circulation of the infected host and normal immune function demonstrating a Th x cytokine profile, i.e. Interleukin 2 and gamma interferon, capable of resisting the infection will be re-established.
- a Th x cytokine profile i.e. Interleukin 2 and gamma interferon
- Vaccines manufactured by the use of coat or other peptides from viral, bacterial, parasitic or mycoplasma may be screened to determine whether they posses these specific amino acid sequences which exhibit these specific Ion bridge pair arrays capable of mimicking the actions of AFP or Interleukin 10 and there inherent immune suppressive properties - such suppressive potential properties is determined by the manufactured vaccine's reactivity with any of the said specific amino acid sequences listed herein which may be removed or neutralised by the antiserum specified in this patent .
- Suitable dosages in accordance with the present invention depend on many factors, e.g. the patient's weight, the mode of administration, the frequency of administration, the type of affliction being treated or prevented, whether the infection presently exists, and if so, to what degree. Suitable dosages for given situations can readily be determined by those skilled in the art without undue experimentation.
- the total treatment time according to the present invention will vary from patient to patient based on sound medical judgement and factors particular to the patient being treated, such as, for example, the age and physical condition of the patient. Those skilled in the art can easily determine suitable total treatment time on a patient by patient basis.
- HIV-1 Human Immunodeficiency Virus Type 1
- AIDS Acquired Immune Deficiency Syndrome
- AIDS is characterised as a profound breakdown in host's cellular and humoral immunity and increased susceptibility to a wide range of opportunistic infections.
- One of the consequences of this immune dysfunction is a marked depletion in absolute CD4+ cells in HIV- infected individuals. Studies over the past years have demonstrated that the destruction of the immune system by HIV-1 is a chronic process, starting at the moment of infection.
- the major histocompatibility complex is a collection of 40-50 genes arrayed within a long continuous stretch of DNA on chromosome 6 in humans .
- the MHC is referred to as the HLA complex in humans.
- the MHC genes are organised into regions encoding three classes of molecules: Class I, Class II and Class III.
- the Class I genes encode glycoproteins expressed on the surface of nearly all nucleated cells, where they present peptide antigens of altered self-cells necessary for the activation of T c cells.
- the Class II genes encode glycoproteins expressed primarily on antigen-presenting cells (macrophages, dendritic cells, and B cells), where they present processed antigenic peptides to Th cells.
- the Class III genes encode somewhat different products that are also associated with the immune process. These include a number of soluble serum proteins (including components of the complement system) , steroid 21-hydroxylase enzymes, and tumour necrosis factors.
- ADCC antibody-dependent cell-mediated cytotoxicity
- a number of white blood cells have cytotoxic potential and express membrane receptors for the Fc region of the antibody IgG molecule.
- this antibody is specifically bound to a target cell which occurs when these specific poly or monoclonal antibodies to these sequences present on AFP, Interleukin 10 bind to HIV infected cells or free viral peptides causing immune Th2 shift.
- Interleukin 10 bind to HIV infected cells or free viral peptides causing immune Th2 shift.
- These cytotoxic Fc receptor-bearing cells can bind to the antibodies' Fc region, and thus to the infected HIV cells, and subsequently cause lysis of these cells.
- ADCC antibody-dependent cell-mediated cytotoxicity
- the variety of cells that have been shown to exhibit ADCC include NK cells. Macrophages, monocytes, neutrophils, and eosinophils. 2.0 OBJECTIVES 2.1 To provide for an administration of monoclonal antibodies to these specified sequences present on AFP and Interleukin 10 and other cytokines and infectious organisms to HIV+ patients. 2.2 To monitor immune system functioning before and after the administration of these mono or polyclonal antibodies.
- Beta-2-microglobulin level 3.6. Appearance of new or improvement of active opportunistic infections.
Landscapes
- Health & Medical Sciences (AREA)
- Chemical & Material Sciences (AREA)
- Life Sciences & Earth Sciences (AREA)
- Organic Chemistry (AREA)
- Medicinal Chemistry (AREA)
- General Health & Medical Sciences (AREA)
- Immunology (AREA)
- Proteomics, Peptides & Aminoacids (AREA)
- Molecular Biology (AREA)
- Biochemistry (AREA)
- Genetics & Genomics (AREA)
- Biophysics (AREA)
- Engineering & Computer Science (AREA)
- Veterinary Medicine (AREA)
- Public Health (AREA)
- Animal Behavior & Ethology (AREA)
- Pharmacology & Pharmacy (AREA)
- Bioinformatics & Cheminformatics (AREA)
- Gastroenterology & Hepatology (AREA)
- Epidemiology (AREA)
- Virology (AREA)
- Zoology (AREA)
- Nuclear Medicine, Radiotherapy & Molecular Imaging (AREA)
- General Chemical & Material Sciences (AREA)
- Chemical Kinetics & Catalysis (AREA)
- Toxicology (AREA)
- Hematology (AREA)
- Microbiology (AREA)
- Biomedical Technology (AREA)
- AIDS & HIV (AREA)
- Tropical Medicine & Parasitology (AREA)
- Oncology (AREA)
- Urology & Nephrology (AREA)
- Mycology (AREA)
- Biotechnology (AREA)
- Food Science & Technology (AREA)
- Pathology (AREA)
- Gynecology & Obstetrics (AREA)
- Pregnancy & Childbirth (AREA)
- Reproductive Health (AREA)
Priority Applications (1)
Application Number | Priority Date | Filing Date | Title |
---|---|---|---|
AU68870/96A AU6887096A (en) | 1996-09-11 | 1996-09-13 | Immune direction therapy |
Applications Claiming Priority (2)
Application Number | Priority Date | Filing Date | Title |
---|---|---|---|
US2518096P | 1996-09-11 | 1996-09-11 | |
US60/025,180 | 1996-09-11 |
Publications (1)
Publication Number | Publication Date |
---|---|
WO1998010792A1 true WO1998010792A1 (en) | 1998-03-19 |
Family
ID=21824510
Family Applications (2)
Application Number | Title | Priority Date | Filing Date |
---|---|---|---|
PCT/IB1996/000945 WO1998010792A1 (en) | 1996-09-11 | 1996-09-13 | Immune direction therapy |
PCT/IB1997/001086 WO1998010787A2 (en) | 1996-09-11 | 1997-09-10 | Pharmaceutical compositions for the treatment of immune disorders |
Family Applications After (1)
Application Number | Title | Priority Date | Filing Date |
---|---|---|---|
PCT/IB1997/001086 WO1998010787A2 (en) | 1996-09-11 | 1997-09-10 | Pharmaceutical compositions for the treatment of immune disorders |
Country Status (9)
Country | Link |
---|---|
EP (1) | EP0929568A2 (de) |
JP (1) | JP2001503613A (de) |
CN (1) | CN1230195A (de) |
AU (2) | AU6887096A (de) |
CA (1) | CA2265885A1 (de) |
IL (1) | IL128806A0 (de) |
NZ (1) | NZ335039A (de) |
SE (1) | SE9900812D0 (de) |
WO (2) | WO1998010792A1 (de) |
Cited By (5)
Publication number | Priority date | Publication date | Assignee | Title |
---|---|---|---|---|
US7553932B1 (en) | 2005-04-25 | 2009-06-30 | La Jolla Institute For Allergy And Immunology | Methods of treating viral infection with IL-10 receptor antagonists |
US7589184B2 (en) | 2004-05-24 | 2009-09-15 | Genvault Corporation | Stable protein storage and stable nucleic acid storage in recoverable form |
US7989590B2 (en) * | 2005-03-22 | 2011-08-02 | Rohto Pharmaceutical Co., Ltd | Peptides that increase collagen or hyaluronic acid production |
US8283165B2 (en) | 2008-09-12 | 2012-10-09 | Genvault Corporation | Matrices and media for storage and stabilization of biomolecules |
EP2989120A4 (de) * | 2013-04-25 | 2017-04-19 | Carmel-Haifa University Economic Corp. | Synthetische entzündungshemmende peptide und verwendungen davon |
Families Citing this family (8)
Publication number | Priority date | Publication date | Assignee | Title |
---|---|---|---|---|
AU5297299A (en) * | 1998-08-17 | 2000-03-06 | Patrick T. Prendergast | Cytokine and cytokine receptor, agonist, antagonist and/or antibody combination for therapeutic use |
WO2000035472A2 (en) * | 1998-12-15 | 2000-06-22 | Hollis-Eden Pharmaceuticals, Inc. | Cytokine combination therapy |
AU2001245453B2 (en) * | 2000-03-14 | 2005-08-25 | National Jewish Medical And Research Center | Method and composition for treating airway hyperresponsiveness |
FI118263B (fi) * | 2002-10-09 | 2007-09-14 | Timo Kalevi Korpela | Kaspaasiaktiivisuutta säätelevät peptidit |
EA008925B1 (ru) * | 2004-12-14 | 2007-08-31 | Товарищество С Ограниченной Ответственностью "Реал Мед Компани" | Способ коррекции иммунного состояния организма при сахарном диабете |
US8932829B2 (en) | 2005-07-07 | 2015-01-13 | Elena Dudich | Recombinant alpha-fetoprotein and compositions thereof |
CN103275222B (zh) * | 2013-05-15 | 2014-04-16 | 中山康方生物医药有限公司 | 一种阻断白介素12 p40功能的单克隆抗体及其编码基因和应用 |
CN114163493B (zh) * | 2021-11-18 | 2023-09-15 | 浙大宁波理工学院 | 一种可作为5型磷酸二酯酶抑制剂的多肽及其应用 |
Citations (3)
Publication number | Priority date | Publication date | Assignee | Title |
---|---|---|---|---|
WO1993017698A1 (en) * | 1992-03-04 | 1993-09-16 | Schering Corporation | Use of interleukin-10 to suppress graft-vs.-host disease |
WO1993018783A1 (en) * | 1992-03-20 | 1993-09-30 | Schering Corporation | Use of interleukin-10 to induce the production of interleukin-1 receptor antagonist |
WO1994006473A1 (en) * | 1992-09-18 | 1994-03-31 | Schering Corporation | Restoration of immunocompetency to t helper cells in hiv infected patients |
Family Cites Families (10)
Publication number | Priority date | Publication date | Assignee | Title |
---|---|---|---|---|
DE3264341D1 (en) * | 1981-01-09 | 1985-08-01 | New York Blood Center Inc | Synthetic antigenic composition and process for making same |
US4822606A (en) * | 1986-04-07 | 1989-04-18 | Duke University | Immunosuppressive synthetic peptides and analogs thereof based on retroviral envelope sequences |
AU1366088A (en) * | 1987-01-28 | 1988-08-24 | Ortho Pharmaceutical Corporation | Immunosuppressive peptides and methods of use |
NZ223980A (en) * | 1987-03-23 | 1991-02-26 | Hiver Ltd | An aids-type virus vaccine comprising an antibody equivalent which recognises an epitope on a cd4 cell-marker |
SE8705197D0 (sv) * | 1987-12-30 | 1987-12-30 | Jonas Blomberg | New peptides, two diagnostic methods using the peptides and a medicament based on the peptides |
MY106163A (en) * | 1990-03-26 | 1995-03-31 | Schering Corp | Bcrf1 antagonists for treating epstein-barr virus infections. |
WO1993011157A1 (en) * | 1991-11-27 | 1993-06-10 | The Council Of The Queensland Institute Of Medical Research | MALARIAL VACCINE AND PEPTIDES COMPRISING HUMAN T-CELL EPITOPE OF CIRCUMSPOROZOITE PROTEIN OF $i(P.VIVAX) |
JPH09501154A (ja) * | 1993-07-28 | 1997-02-04 | メドベット サイエンス プロプライアタリー リミティド | 造血成長因子アンタゴニスト |
PT744027E (pt) * | 1994-01-14 | 2005-05-31 | Rath Matthias | Utilizacao de metodos para identificar oligopeptidos de sinal hidrofilicos |
AU4385696A (en) * | 1996-01-18 | 1997-08-11 | Christian Gronhoj Larsen | Synthetic il-10 analogues |
-
1996
- 1996-09-13 WO PCT/IB1996/000945 patent/WO1998010792A1/en active Application Filing
- 1996-09-13 AU AU68870/96A patent/AU6887096A/en not_active Abandoned
-
1997
- 1997-09-10 WO PCT/IB1997/001086 patent/WO1998010787A2/en not_active Application Discontinuation
- 1997-09-10 CA CA002265885A patent/CA2265885A1/en not_active Abandoned
- 1997-09-10 AU AU41320/97A patent/AU4132097A/en not_active Abandoned
- 1997-09-10 NZ NZ335039A patent/NZ335039A/en unknown
- 1997-09-10 CN CN97197816A patent/CN1230195A/zh active Pending
- 1997-09-10 EP EP97939105A patent/EP0929568A2/de not_active Withdrawn
- 1997-09-10 IL IL12880697A patent/IL128806A0/xx unknown
- 1997-09-10 JP JP51343598A patent/JP2001503613A/ja active Pending
-
1999
- 1999-03-08 SE SE9900812A patent/SE9900812D0/xx not_active Application Discontinuation
Patent Citations (3)
Publication number | Priority date | Publication date | Assignee | Title |
---|---|---|---|---|
WO1993017698A1 (en) * | 1992-03-04 | 1993-09-16 | Schering Corporation | Use of interleukin-10 to suppress graft-vs.-host disease |
WO1993018783A1 (en) * | 1992-03-20 | 1993-09-30 | Schering Corporation | Use of interleukin-10 to induce the production of interleukin-1 receptor antagonist |
WO1994006473A1 (en) * | 1992-09-18 | 1994-03-31 | Schering Corporation | Restoration of immunocompetency to t helper cells in hiv infected patients |
Non-Patent Citations (5)
Title |
---|
A. LANDAY ET AL.: "In vitro restoration of T cell immune function in human immunodeficiency virus-positive persons: Effects of interleukin (IL)-12 and anti-IL-10.", THE JOURNAL OF INFECTIOUS DISEASES, vol. 173, no. 5, May 1996 (1996-05-01), CHICAGO, IL, USA, pages 1085 - 1091, XP000674644 * |
L. BROWN ET AL.: "Synthetic peptides representing sequences within gp41 of HIV as immunogens for murine T- and B-cell responses.", ARCHIVES OF VIROLOGY, vol. 140, no. 4, 1995, VIENNA, AUSTRIA, pages 635 - 654, XP000674654 * |
M. CLERICI ET AL.: "Role of interleukin-10 in T helper cell dysfunction in asymptomatic individuals infected with the human immunodeficiency virus.", THE JOURNAL OF CLINICAL INVESTIGATION, vol. 93, no. 2, February 1994 (1994-02-01), NEW YORK, NY, USA, pages 768 - 775, XP000674643 * |
S. VANINI ET AL.: "Discrete regions of HIV-1 gp41 defined by syncytia-inhibiting affinity-purified human antibodies.", AIDS, vol. 7, no. 2, February 1993 (1993-02-01), LONDON, GB, pages 167 - 174, XP000674642 * |
T. MCCUTCHAN ET AL.: "Sequence of the immunodominant epitope for the surface protein on sporozoites of Plasmodium vivax.", SCIENCE, vol. 230, no. 4732, 20 December 1985 (1985-12-20), WASHINGTON, DC, USA, pages 1381 - 1383, XP000674496 * |
Cited By (9)
Publication number | Priority date | Publication date | Assignee | Title |
---|---|---|---|---|
US7589184B2 (en) | 2004-05-24 | 2009-09-15 | Genvault Corporation | Stable protein storage and stable nucleic acid storage in recoverable form |
US7989590B2 (en) * | 2005-03-22 | 2011-08-02 | Rohto Pharmaceutical Co., Ltd | Peptides that increase collagen or hyaluronic acid production |
US7553932B1 (en) | 2005-04-25 | 2009-06-30 | La Jolla Institute For Allergy And Immunology | Methods of treating viral infection with IL-10 receptor antagonists |
US8283165B2 (en) | 2008-09-12 | 2012-10-09 | Genvault Corporation | Matrices and media for storage and stabilization of biomolecules |
US8951719B2 (en) | 2008-09-12 | 2015-02-10 | Gentegra, LLC. | Matrices and media for storage and stabilization of biomolecules |
US9637513B2 (en) | 2008-09-12 | 2017-05-02 | Gentegra Llc | Matrices and media for storage and stabilization of biomolecules |
US10160997B2 (en) | 2008-09-12 | 2018-12-25 | Gentegra Llc | Matrices and media for storage and stabilization of biomolecules |
EP2989120A4 (de) * | 2013-04-25 | 2017-04-19 | Carmel-Haifa University Economic Corp. | Synthetische entzündungshemmende peptide und verwendungen davon |
US9850278B2 (en) | 2013-04-25 | 2017-12-26 | Carmel-Haifa University Economic Corp. | Synthetic anti-inflammatory peptides and use thereof |
Also Published As
Publication number | Publication date |
---|---|
SE9900812L (sv) | 1999-03-08 |
CN1230195A (zh) | 1999-09-29 |
WO1998010787A2 (en) | 1998-03-19 |
JP2001503613A (ja) | 2001-03-21 |
NZ335039A (en) | 2001-04-27 |
WO1998010787A3 (en) | 1998-07-30 |
SE9900812D0 (sv) | 1999-03-08 |
AU4132097A (en) | 1998-04-02 |
CA2265885A1 (en) | 1998-03-19 |
AU6887096A (en) | 1998-04-02 |
EP0929568A2 (de) | 1999-07-21 |
IL128806A0 (en) | 2000-01-31 |
Similar Documents
Publication | Publication Date | Title |
---|---|---|
KR100235849B1 (ko) | HIV에 대한 면역응답을 유도할 수 있는 펩티드 및 그 펩티드를 함유하는 항 AIDS 예방, 치료제(Peptides Capable of Inducing Immune Response to HIV and Anti-AIDS Agent for Preventing and Curing AIDS) | |
US7744896B1 (en) | HIV-1 Tat compositions | |
Iborra et al. | Vaccination with the Leishmania infantum acidic ribosomal P0 protein plus CpG oligodeoxynucleotides induces protection against cutaneous leishmaniasis in C57BL/6 mice but does not prevent progressive disease in BALB/c mice | |
WO1998010792A1 (en) | Immune direction therapy | |
JP2020513782A (ja) | Hiv感染を治療するキメラ抗原受容体の組換え遺伝子構築およびその応用 | |
Schooley et al. | Two double-blinded, randomized, comparative trials of 4 human immunodeficiency virus type 1 (HIV-1) envelope vaccines in HIV-1—infected individuals across a spectrum of disease severity: AIDS Clinical Trials Groups 209 and 214 | |
US20110142911A1 (en) | HIV epitopes and pharmaceutical composition containing same | |
EP0792354A1 (de) | Gezielte t-lymfozyten | |
JPH10503473A (ja) | 細胞傷害性tリンパ球刺激およびhcv曝露診断用c型肝炎ウイルスコアペプチド | |
Tartz et al. | Immunization with a circumsporozoite epitope fused to Bordetella pertussis adenylate cyclase in conjunction with cytotoxic T-lymphocyte-associated antigen 4 blockade confers protection against Plasmodium berghei liver-stage malaria | |
Perdiguero et al. | Heterologous combination of VSV-GP and NYVAC vectors expressing HIV-1 trimeric gp145 Env as vaccination strategy to induce balanced B and T cell immune responses | |
MX2010012587A (es) | Vector de expresion que codifica el virus alfa replicasa y uso del mismo como adyuvante inmunologico. | |
AU660422B2 (en) | Pathogen-specific CTL therapy | |
EP1545602B1 (de) | Pharmazeutische zusammensetzungen mit einem hiv-hüllprotein und cd4 | |
US7521426B2 (en) | HIV-specific CTL inducing peptides and medicaments for preventing or treating AIDS comprising the peptides | |
Lee et al. | A single point mutation in HIV-1 V3 loop alters the immunogenic properties of rgp120 | |
Bretscher | An hypothesis to explain why cell‐mediated immunity alone can contain infections by certain intracellular parasites and how immune class regulation of the response against such parasites can be subverted | |
Barnes | Strategies for an AIDS Vaccine: In their attempts to develop a vaccine against AIDS, many scientists focus on raising antibodies to a protein from the AIDS virus, a strategy that some researchers think may require modification | |
WO2016080392A1 (ja) | ワクチン及びプライムブーストワクチン | |
WO2012040266A2 (en) | Gene-based adjuvants and compositions thereof to increase antibody production in response to gene-based vaccines | |
Chougnet et al. | Potential clinical applications of interleukin-12 | |
Purner et al. | Cross-reactivity of human Toxoplasma-specific T cells: implications for development of a potential immunotherapeutic or vaccine | |
KR102297440B1 (ko) | 표적 세포 특이적으로 결합하여 다중 면역기능이 강화된 키메라항원 및 이의용도 | |
JP2006188513A (ja) | Cd8+細胞傷害性tリンパ球エピトープペプチド及びその用途 | |
WO2020071869A1 (ko) | 표적 세포 특이적으로 결합하여 다중 면역기능이 강화된 키메라항원 및 이의용도 |
Legal Events
Date | Code | Title | Description |
---|---|---|---|
AK | Designated states |
Kind code of ref document: A1 Designated state(s): AT AU BR CA CH CN DE DK ES GB IL JP KE LU MX NO NZ PT RU SE SG US |
|
AL | Designated countries for regional patents |
Kind code of ref document: A1 Designated state(s): AT BE CH DE DK ES FI FR GB GR IE IT LU MC NL PT SE BF BJ CF CG CI CM GA GN ML MR NE SN TD TG |
|
121 | Ep: the epo has been informed by wipo that ep was designated in this application | ||
REG | Reference to national code |
Ref country code: DE Ref legal event code: 8642 |
|
122 | Ep: pct application non-entry in european phase | ||
NENP | Non-entry into the national phase |
Ref country code: CA |
|
NENP | Non-entry into the national phase |
Ref country code: JP Ref document number: 1998513416 Format of ref document f/p: F |