JP5931120B2 - 哺乳動物において免疫を賦活する応答を提供または増強するための複合化された(m)RNAと裸のmRNAとを含んでいる組成物、およびその使用 - Google Patents
哺乳動物において免疫を賦活する応答を提供または増強するための複合化された(m)RNAと裸のmRNAとを含んでいる組成物、およびその使用 Download PDFInfo
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Description
816−25)。
Immunol.15:95−119)などである。最近、インビボにおいて、dsRNA分子もまた使用されている(McCaffrey et al.(2002),Nature 418:38−39;Xia et al.(2002),Nature Biotech.20:1006−1010;Brummelkamp et al.(2002),Cancer Cell 2:243−247)。このように、本発明に係る免疫賦活組成物のアジュバント成分における少なくとも1個の(m)RNAに使用されるsiRNAは、免疫賦活性のRNAであってもよい。そしてsiRNAは、典型的に、約8〜30個のヌクレオチド、好ましくは17〜25個のヌクレオチド、より好ましくは20〜25個、最も好ましくは21〜23個のヌクレオチドの(一本鎖または)二本鎖、好ましくは二本鎖のRNA配列を含む。原則として、上述したようなRNA配列のコード領域に生じる17〜29個の塩基、好ましくは19〜25個の塩基、最も好ましくは21〜23個の塩基の長さを有する全ての断片は、上述したsiRNAのための標的配列として働くことができる。同様に、siRNAはまた、タンパク質の、好ましくは(先天性または適応性)免疫応答の誘導を負に制御する制御タンパク質の、標的塩基配列に対して方向づけられてもよい。この塩基配列は、コード領域内になく、例えば、特にRNAにおける5’側の非コード領域内にある、制御機能を有するRNAの標的非コード領域である。したがって、本発明に係る免疫賦活組成物のアジュバント成分における少なくとも1個の(m)RNAとして使用される、siRNAの標的配列は、上述したタンパク質の塩基配列における翻訳領域および/もしくは非翻訳領域内、ならびに/またはその制御エレメントの領域内に存在することができる。上述したsiRNAの標的配列はまた、非翻訳配列と翻訳配列とをまたぐ領域に存在することもできる。特に、標的配列は、RNAにおけるコード領域の最初にあるトリプレットの上流の少なくとも1個のヌクレオチドを含むことができる。
本明細書では、免疫賦活組成物のアジュバント成分の(m)RNAの少なくとも1個によってコードされた治療的に活性なタンパク質は、自然に生じた組み換えたんぱく質または当業者に公知の単離されたタンパク質の何れから選択されてもよい。治療的に活性なタンパク質は、それらに限定されずに、細胞内のシグナル伝達を刺激する、または阻害するたんぱく質、例えば、サイトカイン、抗体などを含んでもよい。それゆえ、治療的に活性なタンパク質は、位置が保存された4個のシステイン残基(CCCC)を有し、保存されたモティーフシークエンスであるTrp−Ser−X−Trp−Ser(WSXWS)を含む、サイトカインファミリーのクラスIのサイトカインを含んでもよい。上記Xは、保存されていないアミノ酸である。サイトカインファミリーのクラスIのサイトカインは、例えば、IL−3、IL−5といったGM−CSFサブファミリー、例えば、IL−6、IL−11、IL−12といったIL−6サブファミリー、または、例えば、IL−2、IL−4、IL−7、IL−9、IL−15といったIL−2サブファミリー、または、IL−1α、IL−1β、IL−10といったサイトカイン類を含んでもよい。治療的に活性なタンパク質は、また、位置が保存された4個のシステイン残基(CCCC)を有するが、保存されたモティーフシークエンスであるTrp−Ser−X−Trp−Ser(WSXWS)を含まない、サイトカインファミリーのクラスIIのサイトカインを含んでもよい。サイトカインファミリーのクラスIIのサイトカインは、例えば、IFN−α、IFN−β、IFN−γなどを含んでもよい。治療的に活性なタンパク質は、さらに、例えば、TNF−α、TNF−βなどの腫瘍壊死因子のファミリーのサイトカイン、または、IL−8、MIP−1、RANTES、CCR5、CXR4などのG−タンパク質と反応し、膜透過型の7個のへリックスを含むケモカインファミリーのサイトカイン、または、TNF−RI、TNF−RII、CD40、OX40(CD134)、Fasといったサイトカインに特異的な受容体を含んでもよい。
IF、GINGF、GIP、GJA3、GJA8、GJB2、GJB3、GJB6、GJB1、GK、GLA、GLB、GLB1、GLC3B、GLC1B、GLC1C、GLDC、GLI3、GLP1、GLRA1、GLUD1、GM1 (fuc−GM1)、GM2A、GM−CSF、GMPR、GNAI2、GNAS、GNAT1、GNB3、GNE、GNPTA、GNRH、GNRH1、GNRHR、GNS、GnT−V、gp100、GP1BA、GP1BB、GP9、GPC3、GPD2、GPDS1、GPI、GP1BA、GPN1LW、GPNMB/m、GPSC、GPX1、GRHPR、GRK1、GROα、GROβ、GROγ、GRPR、GSE、GSM1、GSN、GSR、GSS、GTD、GTS、GUCA1A、GUCY2D、GULOP、GUSB、GUSM、GUST、GYPA、GYPC、GYS1、GYS2、H0KPP2、H0MG2、HADHA、HADHB、HAGE、HAGH、HAL、HAST−2、HB 1、HBA2、HBA1、HBB、HBBP1、HBD、HBE1、HBG2、HBG1、HBHR、HBP1、HBQ1、HBZ、HBZP、HCA、HCC−1、HCC−4、HCF2、HCG、HCL2、HCL1、HCR、HCVS、HD、HPN、HER2、HER2/NEU、HER3、HERV−K−MEL、HESX1、HEXA、HEXB、HF1、HFE、HF1、HGD、HHC2、HHC3、HHG、HK1 HLA−A、HLA−A*0201−R170I、HLA−A11/m、HLA−A2/m、HLA−DPB1 HLA−DRA、HLCS、HLXB9、HMBS、HMGA2、HMGCL、HMI、HMN2、HMOX1、HMS1 HMW−MAA、HND、HNE、HNF4A、HOAC、HOMEOBOX NKX 3.1、HOM−TES−14/SCP−1、HOM−TES−85、HOXA1 HOXD13、HP、HPC1、HPD、HPE2、HPE1、HPFH、HPFH2、HPRT1、HPS1、HPT、HPV−E6、HPV−E7、HR、HRAS、HRD、HRG、HRPT2、HRPT1、HRX、HSD11B2、HSD17B3、HSD17B4、HSD3B2、HSD3B3、HSN1、HSP70−2M、HSPG2、HST−2、HTC2、HTC1、hTERT、HTN3、HTR2C、HVBS6、HVBS1、HVEC、HV1S、HYAL1、HYR、I−309、IAB、IBGC1、IBM2、ICAM1、ICAM3、iCE、ICHQ、ICR5、ICR1、ICS1、IDDM2、IDDM1、IDS、IDUA、IF、IFNa/b、IFNGR1、IGAD1、IGER、IGF−1R、IGF2R、IGF1、IGH、IGHC、IGHG2、IGHG1、IGHM、IGHR、IGKC、IHG1、IHH、IKBKG、IL1、IL−1 RA、IL10、IL−11、IL12、IL12RB1、IL13、IL−13Rα2、IL−15、IL−16、IL−17、IL18、IL−1a、IL−1α、IL−1b、IL−1β、IL1RAPL1、IL2、IL24、IL−2R、IL2RA、IL2RG、IL3、IL3RA、IL4、IL4R、IL4R、IL−5、IL6、IL−7、IL7R、IL−8、IL−9、未成熟なラミニン受容体、IMMP2L、INDX、INFGR1、INFGR2、INFα、IFN、INFγ、INS、INSR、INVS、IP−10、IP2、IPF1、IP1、IRF6、IRS1、ISCW、ITGA2、ITGA2B、ITGA6、ITGA7、ITGB2、ITGB3、ITGB4、ITIH1、ITM2B、IV、IVD、JAG1、JAK3、JBS、JBTS1、JMS、JPD、KAL1、KAL2、KALI、KLK2、KLK4、KCNA1、KCNE2、KCNE1、KCNH2、KCNJ1、KCNJ2、KCNJ1、KCNQ2、KCNQ3、KCNQ4、KCNQ1、KCS、KERA、KFM、KFS、KFSD、KHK、ki−67、KIAA0020、KIAA0205、KIAA0205/m、KIF1B、KIT、KK−LC−1、KLK3、KLKB1、KM−HN−1、KMS、KNG、KNO、K−RAS/m、KRAS2、KREV1、KRT1、KRT10、KRT12、KRT13、KRT14、KRT14L1、KRT14L2、KRT14L3、KRT16、KRT16L1、KRT16L2、KRT17、KRT18、KRT2A、KRT3、KRT4、KRT5、KRT6 A、KRT6B、KRT9、KRTHB1、KRTHB6、KRT1、KSA、KSS、KWE、KYNU、L0H19CR1、L1CAM、LAGE、LAGE−1、LALL、LAMA2、LAMA3、LAMB3、LAMB1、LAMC2、LAMP2、LAP、LCA5、LCAT、LCCS、LCCS 1、LCFS2、LCS1、LCT、LDHA、LDHB、LDHC、LDLR、LDLR/FUT、LEP、LEWISY、LGCR、LGGF−PBP、LGI1、LGMD2H、LGMD1A、LGMD1B、LHB、LHCGR、LHON、LHRH、LHX3、LIF、LIG1、LIMM、LIMP2、LIPA、LIPA、LIPB、LIPC、LIVIN、L1CAM、LMAN1、LMNA、LMX1B、LOLR、LOR、LOX、LPA、LPL、LPP、LQT4、LRP5、LRS 1、LSFC、LT− β 、LTBP2、LTC4S、LYL1、XCL1、LYZ、M344、MA50、MAA、MADH4、MAFD2、MAFD1、MAGE、MAGE−A1、MAGE−A10、MAGE−A12、MAGE−A2、MAGE−A3、MAGE−A4、MAGE−A6、MAGE−A9、MAGEB1、MAGE−B10、MAGE−B16、MAGE−B17、MAGE−B2、MAGE−B3、MAGE−B4、MAGE−B5、MAGE−B6、MAGE−C1、MAGE−C2、MAGE−C3、MAGE−D1、MAGE−D2、MAGE−D4、MAGE−E1、MAGE−E2、MAGE−F1、MAGE−H1、MAGEL2、MGB1、MGB2、MAN2A1、MAN2B1、MANBA、MANBB、MAOA、MAOB、MAPK8IP1、MAPT、MART−1、MART−2、MART2/m、MAT1A、MBL2、MBP、MBS1、MC1R、MC2R、MC4R、MCC、MCCC2、MCCC1、MCDR1、MCF2、MCKD、MCL1、MC1R、MCOLN1、MCOP、MCOR、MCP−1、MCP−2、MCP−3、MCP−4、MCPH2、MCPH1、MCS、M−CSF、MDB、MDCR、MDM2、MDRV、MDS 1、ME1、ME1/m、ME2、ME20、ME3、MEAX、MEB、MEC CCL−28、MECP2、MEFV、MELANA、MELAS、MEN1 MSLN、MET、MF4、MG50、MG50/PXDN、MGAT2、MGAT5、MGC1
MGCR、MGCT、MGI、MGP、MHC2TA、MHS2、MHS4、MIC2、MIC5、MIDI、MIF、MIP、MIP−5/HCC−2、MITF、MJD、MKI67、MKKS、MKS1、MLH1、MLL、MLLT2、MLLT3、MLLT7、MLLT1、MLS、MLYCD、MMA1a、MMP 11、MMVP1、MN/CA IX−Antigen、MNG1、MN1、MOC31、MOCS2、MOCS1、MOG、MORC、MOS、MOV18、MPD1、MPE、MPFD、MPI、MPIF−1、MPL、MPO、MPS3C、MPZ、MRE11A、MROS、MRP1、MRP2、MRP3、MRSD、MRX14、MRX2、MRX20、MRX3、MRX40、MRXA、MRX1、MS、MS4A2、MSD、MSH2、MSH3、MSH6、MSS、MSSE、MSX2、MSX1、MTATP6、MTC03、MTCO1、MTCYB、MTHFR、MTM1、MTMR2、MTND2、MTND4、MTND5、MTND6、MTND1、MTP、MTR、MTRNR2、MTRNR1、MTRR、MTTE、MTTG、MTTI、MTTK、MTTL2、MTTL1、MTTN、MTTP、MTTS1、MUC1、MUC2、MUC4、MUC5AC、MUM−1、MUM−1/m、MUM−2、MUM−2/m、MUM−3、MUM−3/m、MUT、mutant p21 ras、MUTYH、MVK、MX2、MXI1、MY05A、MYB、MYBPC3、MYC、MYCL2、MYH6、MYH7、MYL2、MYL3、MYMY、MYO15A、MYO1G、MYO5A、MYO7A、MYOC、Myosin/m、MYP2、MYP1、NA88−A、N−アセチルグルコサミニルトランスフェラーゼ−V、NAGA、NAGLU、NAMSD、NAPB、NAT2、NAT、NBIA1、NBS1、NCAM、NCF2、NCF1、NDN 、NDP、NDUFS4、NDUFS7、NDUFS8、NDUFV1、NDUFV2、NEB、NEFH、NEM1、Neo−PAP、neo−PAP/m、NEU1、NEUROD1、NF2、NF1、NFYC/m、NGEP、NHS、NKS1、NKX2E、NM、NME1、NMP22、NMTC、NODAL、NOG、NOS3、NOTCH3、NOTCH1、NP、NPC2、NPC1、NPHL2、NPHP1、NPHS2、NPHS1、NPM/ALK、NPPA、NQO1、NR2E3、NR3C1、NR3C2、NRAS、NRAS/m、NRL、NROB1、NRTN、NSE、NSX、NTRK1、NUMA1、NXF2、NY−CO1、NY−ESO1、NY−ESO−B、NY−LU−12、ALDOA、NYS2、NYS4、NY−SAR−35、NYS1、NYX、OA3、OA1、OAP、OASD、OAT、OCA1、OCA2、OCD1、OCRL、OCRL1、OCT、ODDD、ODT1、OFC1、OFD1、OGDH、OGT、OGT/m、OPA2、OPA1、OPD1、OPEM、OPG、OPN、OPN1LW、OPN1MW、OPN1SW、OPPG、OPTB1、TTD、ORM1、ORP1、OS−9、OS−9/m、OSM
LIF、OTC、OTOF、OTSC1、OXCT1、OYTES1、P15、P190 MINOR BCR−ABL、P2RY12、P3、P16、P40、P4HB、P−501、P53、P53/m、P97、PABPN1、PAFAH1B1、PAFAH1P1、PAGE−4、PAGE−5、PAH、PAI−1、PAI−2、PAK3、PAP、PAPPA、PARK2、PART−1、PATE、PAX2、PAX3、PAX6、PAX7、PAX8、PAX9、PBCA、PBCRA1、PBT、PBX1、PBXP1、PC、PCBD、PCCA、PCCB、PCK2、PCK1、PCLD、PCOS1、PCSK1、PDB1、PDCN、PDE6A、PDE6B、PDEF、PDGFB、PDGFR、PDGFRL、PDHA1、PDR、PDX1、PECAM1、PEE1、PEO1、PEPD、PEX10、PEX12、PEX13、PEX3、PEX5、PEX6、PEX7、PEX1、PF4、PFBI、PFC、PFKFB1、PFKM、PGAM2、PGD、PGK1、PGK1P1、PGL2、PGR、PGS、PHA2A、PHB、PHEX、PHGDH、PHKA2、PHKA1、PHKB、PHKG2、PHP、PHYH、PI、PI3、PIGA、PIM1−KINASE、PIN1、PIP5K1B、PITX2、PITX3、PKD2、PKD3、PKD1、PKDTS、PKHD1、PKLR、PKP1、PKU1、PLA2G2A、PLA2G7、PLAT、PLEC1、PLG、PLI、PLOD、PLP1、PMEL17、PML、PML/RARα、PMM2、PMP22、PMS2、PMS1、PNKD、PNLIP、POF1、POLA、POLH、POMC、PON2、PON1、PORC、POTE、POU1F1、POU3F4、POU4F3、POU1F1、PPAC、PPARG、
PPCD、PPGB、PPH1、PPKB、PPMX、PPOX、PPP1R3A、PPP2R2B、PPT1、PRAME、PRB、PRB3、PRCA1、PRCC、PRD、PRDX5/m、PRF1、PRG4、PRKAR1A、PRKCA、PRKDC、PRKWNK4、PRNP、PROC、PRODH、PROM1、PROP1、PROS1、PRST、PRP8、PRPF31、PRPF8、PRPH2、PRPS2、PRPS1、PRS、PRSS7、PRSS1、PRTN3、PRX、PSA、PSAP、PSCA、PSEN2、PSEN1、PSG1、PSGR、PSM、PSMA、PSORS1、PTC、PTCH、PTCH1、PTCH2、PTEN、PTGS1、PTH、PTHR1、PTLAH、PTOS1、PTPN12、PTPNI l、PTPRK、PTPRK/m、PTS、PUJO、PVR、PVRL1、PWCR、PXE、PXMP3、PXR1、PYGL、PYGM、QDPR、RAB27A、RAD54B、RAD54L、RAG2、RAGE、RAGE−1、RAG1、RAP1、RARA、RASA1、RBAF600/m、RB1、RBP4、RBP4、RBS、RCA1、RCAS1、RCCP2、RCD1、RCV1、RDH5、RDPA、RDS、RECQL2、RECQL3、RECQL4、REG1A、REHOBE、REN、RENBP、RENS1、RET、RFX5、RFXANK、RFXAP、RGR、RHAG、RHAMM/CD168、RHD、RHO、Rip−1、RLBP1、RLN2、RLN1、RLS、RMD1、RMRP、ROM1、ROR2、RP、RP1、RP14、RP17、RP2、RP6、RP9、RPD1、RPE65、RPGR、RPGRIP1、RP1、RP10、RPS19、RPS2、RPS4X、RPS4Y、RPS6KA3、RRAS2、RS1、RSN、RSS、RU1、RU2、RUNX2、RUNXl、RWS、RYR1、S−100、SAA1、SACS、SAG、SAGE、SALL1、SARDH、SART1、SART2
、SART3、SAS、SAX1、SCA2、SCA4、SCA5、SCA7、SCA8、SCA1、SCC、SCCD、SCF、SCLC1、SCN1A、SCN1B、SCN4A、SCN5A、SCNN1A、SCNN1B、SCNN1G、SCO2、SCP1、SCZD2、SCZD3、SCZD4、SCZD6、SCZD1、SDF−1a/b、SDHA、SDHD、SDYS、SEDL、SERPENA7、SERPINA3、SERPINA6、SERPINA1、SERPINC1、SERPIND1、SERPINE1、SERPINF2、SERPING1、SERPINI1、SFTPA1、SFTPB、SFTPC、SFTPD、SGCA、SGCB、SGCD、SGCE、SGM1、SGSH、SGY−1、SH2D1A、SHBG、SHFM2、SHFM3、SHFM1、SHH、SHOX、SI、SIAL、SIALYL LEWISX 、SIASD、S11、SIM1、SIRT2/m、SIX3、SJS1、SKP2、SLC10A2、SLC12A1、SLC12A3、SLC17A5、SLC19A2、SLC22A1L、SLC22A5、SLC25A13、SLC25A15、SLC25A20、SLC25A4、SLC25A5、SLC25A6、SLC26A2、SLC26A3、SLC26A4、SLC2A1、SLC2A2、SLC2A4、SLC3A1、SLC4A1、SLC4A4、SLC5A1、SLC5A5、SLC6A2、SLC6A3、SLC6A4、SLC7A7、SLC7A9、SLC11A1、SLOS、SMA、SMAD1、SMAL、SMARCB1、SMAX2、SMCR、SMCY、SM1、SMN2、SMN1、SMPD1、SNCA、SNRPN、SOD2、SOD3、SOD1、SOS1、SOST、SOX9、SOX10、Sp17、SPANXC、SPG23、SPG3A、SPG4、SPG5A、SPG5B、SPG6、SPG7、SPINK1、SPINK5、SPPK、SPPM、SPSMA、SPTA1、SPTB、SPTLC1、SRC、SRD5A2、SRPX、SRS、SRY、SShCG、SSTR2、SSX1、SSX2 (HOM−MEL−40/SSX2)、SSX4、ST8、STAMP−1、STAR、STARP1、STATH、STEAP、STK2、STK11、STn/ KLH、STO、STOM、STS、SUOX、SURF1、サバイビン−2B、SYCP1、SYM1、SYN1、SYNS1、SYP、SYT/SSX、SYT−SSX−1、SYT−SSX−2、TA−90、TAAL6、TACSTD1、TACSTD2、TAG72、TAF7L、TAF1、TAGE、TAG−72、TALI、TAM、TAP2、TAP1、TAPVR1、TARC、TARP、TAT、TAZ、TBP、TBX22、TBX3、TBX5、TBXA2R、TBXAS1、TCAP、TCF2、TCF1、TCIRG1、TCL2、TCL4、TCL1A、TCN2、TCOF1、TCR、TCRA、TDD、TDFA、TDRD1、TECK、TECTA、TEK、TEL/AML1、TELAB1、TEX15、TF、TFAP2B、TFE3、TFR2、TG、TGFA、TGF−β、TGFBI、TGFB1、TGFBR2、TGFBRE、TGFβ、TGFβRII、TGIF、TGM−4、TGM1、TH、THAS、THBD、THC、THC2、THM、THPO、THRA、THRB、TIMM8A、TIMP2、TIMP3、TIMP1、TITF1、TKCR、TKT、TLP、TLR1、TLR10、TLR2、TLR3、TLR4、TLR4、TLR5、TLR6、TLR7、TLR8、TLR9、TLX1、TM4SF1、TM4SF2、TMC1、TMD、TMIP、TNDM、TNF、TNFRSF11A、TNFRSF1A、TNFRSF6、TNFSF5、TNFSF6、TNFα、TNFβ、TNNI3、TNNT2、TOC、TOP2A、TOP1、TP53、TP63、TPA、TPBG、TPI、TPI/m、TPI1、TPM3、TPM1、TPMT、TPO、TPS、TPTA、TRA、TRAG3、TRAPPC2、TRC8、TREH、TRG、TRH、TRIM32、TRIM37、TRP1、TRP2、TRP−2/6b、TRP−2/INT2、Trp−p8、TRPS1、TS、TSC2、TSC3、TSC1、TSG101、TSHB、TSHR、TSP−180、TST、TTGA2B、TTN、TTPA、TTR、TU M2−PK、TULP1、TWIST、TYH、TYR、TYROBP、TYROBP、TYRP1、TYS、UBE2A、UBE3A、UBE1、UCHL1、UFS、UGT1A、ULR、UMPK、UMPS、UOX、UPA、UQCRC1、URO5、UROD、UPK1B、UROS、USH2A、USH3A、USH1A、USH1C、USP9Y、UV24、VBCH、VCF、VDI、VDR、VEGF、VEGFR−2、VEGFR−1、VEGFR−2/FLK−1、VHL、VIM、VMD2、VMD1、VMGLOM、VNEZ、VNF、VP、VRNI、VWF、VWS、WAS、WBS2、WFS2、WFS1、WHCR、WHN、WISP3、WMS、WRN、WS2A、WS2B、WSN、WSS、WT2、WT3、WT1、WTS、WWS、XAGE、XDH、XIC、XIST、XK、XM、XPA、XPC、XRCC9、XS、ZAP70、ZFHX1B、ZFX、ZFY、ZIC2、ZIC3、ZNF145、ZNF261、ZNF35、ZNF41、ZNF6、ZNF198、ZWS1。
mirabilis、Pseudomonas aeroguinosa、Pseudomonas syringae、Rhizobium meliloti、Rhodobacter sphaeroides、Roseburia cecicola、Roseburis hominis、Salmonella typhimurium、Salmonella bongori、Salmonella typhi、Salmonella enteritidis、Serpulina hyodysenteriae、Serratia marcescens、Shigella boydii、Treponema phagedenis、Vibrio alginolyticus、Vibrio cholerae、Vibrio parahaemolyticus、Wolinella succinogenes および Yersinia enterocoliticaが挙げられる。
代替的に、免疫賦活性のアジュバント成分の(m)RNAの少なくとも1個が、抗原をコードしてもよい。本発明によれば、用語「抗原」は、免疫系によって認識され、適応性の免疫応答の一部としての抗体(または抗原に特異的なT細胞)の形成などによって、抗原特異的な免疫応答を引き起こすことができる物質をいう。これに関連して、適応性の免疫応答の第1のステップは、抗原提示細胞による、ナイーブな抗原に特異的なT細胞の活性化である。この活性化は、ナイーブT細胞が常に通過する、リンパ組織や器官において生じる。抗原提示細胞として機能することができる3つの細胞タイプは、樹状細胞、マクロファージ、B細胞である。上記細胞のそれぞれは、免疫の各応答を引き出すことにおいて、互いに異なる機能を有している。食作用およびマクロピノサイトーシスによって抗原が取り込まれた樹状細胞の組織は、リンパ組織の局部へ進入するための感染によって刺激され、成熟した樹状細胞に分化する。マクロファージは、細菌のような、粒子状の抗原を摂取し、感染因子によって誘導されて、MHCのクラスIIの分子を発現する。B細胞の受容体を介して、可溶性のタンパク質抗原を取り込み、結合するB細胞の新規な能力は、T細胞を誘導するために重要であってもよい。MHCの分子上への抗原の発現によって、T細胞の活性化を導き、T細胞の増殖およびアームドエフェクターT細胞への分化を誘導する。エフェクターT細胞の最も重要な機能は、CD8の細胞毒性のT細胞による感染された細胞の死と、細胞媒介性免疫を共に作動させるTHIによるマクロファージの活性化と、抗体の異なる各クラスを生成するために、TH2およびTH1の各細胞の双方によるB細胞の活性化であり、それゆえ、ヒトの免疫の応答を作動させる。T細胞は、直接的には、抗原を認識して結合しないが、代わりに、例えば、病原性のタンパク質抗原の短いペプチド断片を認識する、T細胞受容体によって抗原を認識する。病原性のタンパク質抗原は、他の細胞の表面上のMHC分子に結合されている。
ラセマーゼ,ART−4,ARTC1/m,B7H4,BAGE−1,BCL−2,bcr/abl,ベータ−カテニン/m,BING−4,BRCA1/m,BRCA2/m,CA 15−3/CA 27−29,CA 19−9,CA72−4,CA125,カルレティキュリン,CAMEL,CASP−8/m,カテプシンB,カテプシンL,CD19,CD20,CD22,CD25,CDE30,CD33,CD4,CD52,CD55,CD56,CD80,CDC27/m,CDK4/m,CDKN2A/m,CEA,CLCA2,CML28,CML66,COA−1/m,コアクトシン様タンパク質,コラージュ XXIII,COX−2,CT−9/BRD6,Cten,サイクリンB1,サイクリンD1,cyp−B,CYPB1,DAM−10,DAM−6,DEK−CAN,EFTUD2/m,EGFR,ELF2/m,EMMPRIN,EpCam,EphA2,EphA3,ErbB3,ETV6−AML1,EZH2,FGF−5,FN,Frau−1,G250,GAGE−1,GAGE−2,GAGE−3,GAGE−4,GAGE−5,GAGE−6,GAGE7b,GAGE−8,GDEP,GnT−V,gp100,GPC3,GPNMB/m,HAGE,HAST−2,ヘプシン,Her2/neu,HERV−K−MEL,HLA−A*0201−R17I,HLA−A11/m,HLA−A2/m,HNE,ホメオボックスNKX3.1,HOM−TES−14/SCP−1,HOM−TES−85,HPV−E6,HPV−E7,HSP70−2M,HST−2,hTERT,iCE,IGF−1R,IL−13Ra2,IL−2R,IL−5,未成熟なラミニン受容体,カリクレイン−2,カリクレイン−4,Ki67,KIAA0205,KIAA0205/m,KK−LC−1,K−Ras/m,LAGE−A1,LDLR−FUT,MAGE−A1,MAGE−A2,MAGE−A3,MAGE−A4,MAGE−A6,MAGE−A9,MAGE−A10,MAGE−A12,MAGE−B1,MAGE−B2,MAGE−B3,MAGE−B4,MAGE−B5,MAGE−B6,MAGE−B10,MAGE−B16,MAGE−B17,MAGE−C1,MAGE−C2,MAGE−C3,MAGE−D1,MAGE−D2,MAGE−D4,MAGE−E1,MAGE−E2,MAGE−F1,MAGE−H1,MAGEL2,マンマグロビンA(mammaglobin A),MART−1/メラン−A,MART−2,MART−2/m,マトリックスタンパク質22,MC1R,M−CSF,ME1/m,メソテリン(mesothelin),MG50/PXDN,MMP11,MN/CA
IX−抗原,MRP−3,MUC−1,MUC−2,MUM−1/m,MUM−2/m,MUM−3/m,ミオシン クラスI/m,NA88−A,N−アセチルグルコサミニルトランスフェラーゼ−V,Neo−PAP,Neo−PAP/m,NFYC/m,NGEP,NMP22,NPM/ALK,N−Ras/m,NSE,NY−ESO−1,NY−ESO−B,OA1,OFA−iLRP,OGT,OGT/m,OS−9,OS−9/m,オステオカルシン,オステオポンチン,p15,p190 マイナー bcr−abl,p53,p53/m,PAGE−4,PAI−1,PAI−2,PART−1,PATE,PDEF,Pim−1−キナーゼ,Pin−1,Pml/PARalpha,POTE,PRAME,PRDX5/m,プロステイン(prostein),プロテイナーゼ−3,PSA,PSCA,PSGR,PSM,PSMA,PTPRK/m,RAGE−1,RBAF600/m,RHAMM/CD168,RU1,RU2,S−100,SAGE,SART−1,SART−2,SART−3,SCC,SIRT2/m,Sp17,SSX−1,SSX−2/HOM−MEL−40,SSX−4,STAMP−1,STEAP,サバイビン,サバイビン−2B,SYT−SSX−1,SYT−SSX−2,TA−90,TAG−72,TARP,TEL−AML1,TGFbeta,TGFbetaRII,TGM−4,TPI/m,TRAG−3,TRG,TRP−1,TRP−2/6b,TRP/INT2,TRP−p8,チロシナーゼ,UPA,VEGF,VEGFR−2/FLK−1,およびWT1。
・PSA(前立腺特異的抗原)=KLK3(カリクレイン−3)、
・PSMA(前立腺特異的膜抗原)、
・PSCA(前立腺幹細胞抗原)、
・STEAP(前立腺の6回膜貫通型の上皮抗原)。
・hTERT、
・WT1、
・MAGE−A2、
・5T4、
・MAGE−A3、
・MUC1、
・Her−2/neu、
・NY−ESO−1、
・CEA、
・サバイビン、
・MAGE−C1、および/または
・MAGE−C2、
これらの抗原の任意の組合せであっても可能である。
a)これらの少なくとも2個の抗原における、少なくとも1個、好ましくは2個、3個、4個、5個、またはさらに6個は、以下から選択される:
・5T4
・NY−ESO−1、
・MAGE−A2、
・MAGE−A3、
・MAGE−C1、および/または
・MAGE−C2、ならびに、
b)さらなる抗原は、本明細書中に明示される少なくとも1個の抗原、好ましくは本明細書中に記載されている抗原の組合せ、群、または部分群から選択される。例えば、このさらなる抗原は、例えば以下から選択される:
・hTERT、
・WT1、
・MAGE−A2、
・5T4、
・MAGE−A3、
・MUC1、
・Her−2/neu、
・NY−ESO−1、
・CEA、
・サバイビン、
・MAGE−C1、および/または
・MAGE−C2。
さらなる実施形態によれば、本発明に係る免疫賦活組成物のアジュバント成分における、少なくとも1個の(m)RNAは、抗体をコードしていてもよい。本発明によれば、この抗体は、あらゆる抗体から選択されてもよい。あらゆる抗体とは、例えば、組み換えられて産生されたあらゆる抗体、もしくは自然発生的なあらゆる抗体、公知であって、特に治療的な目的、診断上の目的もしくは科学的な目的に適している抗体、または特異的な癌疾患に関連して同定された抗体である。本明細書中、用語「抗体」は、その広い意味において用いられ、特にモノクローナル抗体およびポリクローナル抗体(アゴニスト、アンタゴニスト、および遮断抗体または中和抗体を含む)、ならびにポリエピトピック特異性を有する抗体種を包含する。本発明によれば、「抗体」は、一般的にあらゆる公知の抗体(例えばIgM、IgD、IgG、IgAおよびIgE)を含む。公知の抗体とは、例えば自然発生的な抗体、宿主生物内において免疫化により産生された抗体、自然発生的な抗体または宿主生物内において免疫化により産生された抗体から、単離されかつ同定された抗体、および公知の生体分子法によって組換えにより生産された抗体であり、また同様に、キメラ抗体、ヒト抗体、ヒト化抗体、二重特異性抗体、細胞内抗体、すなわち細胞内で発現される抗体および特異的なセルコンパートメントに任意に局在する抗体、ならびに上述した抗体の断片および変異体である。一般的に、抗体は、軽鎖と重鎖とからなり、軽鎖と重鎖とはどちらも可変ドメインおよび定常ドメインを有する。軽鎖は、N末可変ドメイン、VL、およびC末定常ドメイン、CLからなる。その一方、IgG抗体の重鎖は、例えば、N末可変ドメイン、VH、ならびに3つの定常ドメイン、CH1、CH2およびCH3により構成されている。単鎖の抗体は、同様に、本発明の改変された(m)RNAにおけるRNA、好ましくは一本鎖RNA、より好ましくはmRNAによりコードされていてもよい。
プロリンに関するコドンは、CCUまたはCCAからCCCまたはCCGへG/C修飾され得る;
アルギニンに関するコドンは、CGU、CGA、AGAまたはAGGから、CGCまたはCGGへG/C修飾され得る;
アラニンに関するコドンは、GCUまたはGCAからGCCまたはGCGへG/C修飾され得る;
グリシンに関するコドンは、GGUまたはGGAからGGCまたはGGGへG/C修飾され得る、が挙げられる。
フェニルアラニンに関するコドンは、UUUからUUCへG/C修飾され得る;
ロイシンに関するコドンは、UUA、UUG、CUUまたはCUAから、CUCまたはCUGへG/C修飾され得る;
セリンに関するコドンは、UCU、UCAまたはAGUから、UCC、UCGまたはAGCへG/C修飾され得る;
チロシンに関するコドンは、UAUからUACへG/C修飾され得る;
システインに関するコドンは、UGUからUGCへG/C修飾され得る;
ヒスチジンに関するコドンは、CAUからCACへG/C修飾され得る;
グルタミンに関するコドンは、CAAからCAGへG/C修飾され得る;
イソロイシンに関するコドンは、AUUまたはAUAからAUCへG/C修飾され得る;
スレオニンに関するコドンは、ACUまたはACAからACCまたはACGへG/C修飾され得る;
アスパラギンに関するコドンは、AAUからAACへG/C修飾され得る;
リシンに関するコドンは、AAAからAAGへG/C修飾され得る;
バリンに関するコドンは、GUUまたはGUAからGUCまたはGUGへG/C修飾され得る;
アスパラギン酸に関するコドンは、GAUからGACへG/C修飾され得る;
グルタミン酸に関するコドンは、GAAからGAGへG/C修飾され得る;
停止コドンUAAは、UAGまたはUGAへG/C修飾され得る、が挙げられる。
修飾されていない配列(ネイティブなRNA)においてスレオニンをコードするすべてのコドンからACC(またはACG)への置換、および
本来セリンをコードするすべてのコドンからUCC(または、UCGもしくはAGC)への置換;
元の配列においてイソロイシンをコードするすべてのコドンからAUCへの置換、
本来リシンをコードするすべてのコドンからAAGへの置換、および
本来チロシンをコードするすべてのコドンからUACへの置換;
元の配列においてバリンをコードするすべてのコドンからGUC(またはGUG)への置換、
本来グルタミン酸をコードするすべてのコドンからGAGへの置換、
本来アラニンをコードするすべてのコドンからGCC(またはGCG)への置換、および
本来アルギニンをコードするすべてのコドンからCGC(またはCGG)への置換;
元の配列においてバリンをコードするすべてのコドンからGUC(またはGUG)への置換、
本来グルタミン酸をコードするすべてのコドンからGAGへの置換、
本来アラニンをコードするすべてのコドンからGCC(またはGCG)への置換、
本来グリシンをコードするすべてのコドンからGGC(またはGGG)への置換、および
本来アスパラギンをコードするすべてのコドンからAACへの置換;
元の配列においてバリンをコードするすべてのコドンからGUC(またはGUG)への置換、
本来フェニルアラニンをコードするすべてのコドンからUUGへの置換、
本来システインをコードするすべてのコドンからUGCへの置換、
本来ロイシンをコードするすべてのコドンからCUG(またはCUC)への置換、
本来グルタミンをコードするすべてのコドンからCAGへの置換、および
本来プロリンをコードするすべてのコドンからCCC(またはCCG)への置換;などを用いることが好ましい。
ス誘導細胞がん(例えば、頸癌(cervical carcinoma)=子宮頸癌(cervical cancer))、腺がん、ヘルペスウイルス誘導腫瘍(例えば、バーキットリンパ腫、EBV誘導B細胞リンパ腫)、肝炎B誘発腫瘍(幹細胞腫瘍)、HTLV−1およびHTLV−2誘導リンパ腫)、聴神経腫瘍、肺がん(lung carcinomas= lung cancer = bronchial carcinom)、小細胞肺がん、咽頭がん、肛門がん、グリア芽細胞腫、直腸がん、星状細胞腫、脳腫瘍、網膜芽細胞腫、基底細胞腫、脳腫瘍転移、髄芽細胞腫、膣がん、膵臓がん、精巣がん、ホジキン症候群、髄膜腫、シュネーベルガー病、脳下垂体腫瘍、菌状息肉腫、カルチノイド、神経鞘腫、棘細胞がん、バーキットリンパ腫、喉頭がん、腎臓がん、胸腺腫、体細胞腫、骨がん、非ホジキンリンパ腫、尿道がん、CUP症候群、頭頸部腫瘍、乏突起神経膠腫、外陰部癌、腸がん、結腸がん、食道腫瘍(oesophageal carcinoma)(=食道がん(oesophageal cancer))、いぼの発達、小腸の腫瘍、頭蓋咽頭腫、卵巣腫瘍、生殖器腫瘍、卵巣がん(ovarian cancer)(=卵巣腫瘍(ovarian carcinoma))、膵腫瘍(pancreatic carcinoma)(=膵がん(pancreatic cancer))、子宮内膜がん、肝臓腫瘍転移、陰茎がん、舌がん、胆嚢がん、白血病、形質細胞腫、瞼腫瘍、前立腺がん(prostate cancer)(前立腺腫瘍(prostate tumors))などから選択されることが好ましい。
a)いずれのRNAも上記に規定される通りであるカチオン性またはポリカチオン性の化合物と複合体化されている少なくとも1個の本発明の(m)RNA、または治療的に活性なタンパク質、抗原および/または抗体の少なくとも1個をそれぞれコードしている少なくとも1個の遊離のmRNAにとっての鋳型としての(デオキシ)リボ核酸の調製/準備と;
b)RNAポリメラーゼ、適切なバッファー、ヌクレオチド混合物、化学修飾されているヌクレオシドおよび天然に存在するヌクレオシドを有している1個以上のヌクレオチドを必要に応じて含んでいるヌクレオチド混合物、ならびに必要に応じてRNase阻害剤を含んでいるインビトロ転写培地への、上記(デオキシ)リボ核酸の添加と;
c)上記インビトロ転写培地における上記(デオキシ)リボ核酸のインキュベーションおよび(デオキシ)リボ核酸のインビトロ転写と;
d)必要に応じて、組み込まれなかったヌクレオチドの、上記インビトロ転写培地からの精製および除去とを包含している。上記(m)RNAおよび遊離のmRNAは、上述の通りである。1個以上の上記ヌクレオチドは、1個以上の天然に存在するヌクレオシドA、G、Uおよび/またはCにとっての(部分的または完全な)代替物としての、上述ように規定される化学修飾されているヌクレオシドから選択される化学修飾されているヌクレオシド、ならびに天然に存在するヌクレオシドA、G、Uおよび/またはCのすべてが置き換えられているのではない場合に必要に応じて天然に存在するヌクレオシドA、G、Uおよび/またはCを有している。
(a)血液細胞、プロフェッショナル(professional)抗原提示細胞(APC)、特に樹状細胞(DC)の回収;ならびに
(b)上記血液細胞、プロフェッショナル抗原提示細胞(APC)、特に樹状細胞(DC)の、本発明の免疫賦活組成物もしくはその成分、本発明の薬学的組成物または本発明のワクチンを用いたトランスフェクション
を包含している。
a)好ましくは上述のような少なくとも1個の(m)RNAを特定の比率において、上述のようなカチオン性またはポリカチオン性の化合物と混合することによって、上述のようなカチオン性またはポリカチオン性の化合物と複合体化されている少なくとも1個の(m)RNAを含んでいるか、または当該(m)RNAからなる「免疫賦活成分」を調製するステップ;ならびに
b)ステップa)にしたがって調製された免疫賦活成分に、上述のような治療的に活性なタンパク質、抗原および/または抗体の少なくとも1個をコードしている少なくとも1個の遊離のmRNAを特定の比率において添加することによって、本発明の免疫賦活組成物を調製するステップ
を包含している。
以下の図面は、本発明をさらに例証するものと意図されている。それらは、本発明の対象をそれらに限定するとは意図されない。
る本発明の組成物の50μlが加えられて、37℃において一晩中にわたってサイトカインの放出を刺激した。複合体化されているRNAおよび遊離のRNAを含んでいる組成物を用いたhPBMCにおけるサイトカイン(TNFαおよびIL−16)の分泌は、ELISA検出における有意な上昇を示し、良好な免疫賦活特性を示している。
より良好なコドンの利用および安定性のためのCG最適化配列、
muag(変異体化αグロブリンの3’UTR)、
3’末端における70×アデノシン(ポリAテイル)、
3’末端における30×シトシン(ポリCテイル)
を含んでいた。
ORFは斜字体として示されており、muag(変異体化αグロブリンの3’UTR)は破線を用いて示されており、ポリAテイルは1本線を用いて下線が付されており、ポリCテイルは二重線を用いて下線が付されている。
以下の実施例は本発明をさらに例証するものと意図される。それらは本発明の対象をそれらに限定するものと意図されない。
以下の試験のために、本明細書に使用されるようなPpルシフェラーゼ配列をコードしているそれぞれのmRNAに対応しており、Ppルシフェラーゼ(Photinus pyralis)をコードしているDNA配列が調製され、続くトランスフェクションおよびワクチン接種の試験のために使用された。したがって、ネイティブなPpルシフェラーゼをコードしているmRNAに対応するDNA配列は、ポリAタグ(A70)を用いて修飾されて、配列番号121になる(図8を参照のこと)。最終的な構築物は、1816ヌクレオチドの長さを有しており、「T7TS−Ppluc(wt)−A70」と名づけられた。
以下の試験のために、Gallus gallusのオボアルブミンをコードしており、それぞれのmRNA配列に対応するさらなるDNA配列が、調製され、続くトランスフェクションおよびワクチン接種の試験のために使用された。したがって、ネイティブなGallus gallusのオボアルブミンをコードしているmRNAに対応するDNA配列は、より良好なコドンの利用および安定化のためにGC最適化された。それから、Gallus gallusのオボアルブミンをコードしているmRNAに対応するDNA配列は、ポリAタグおよびポリCタグ(A70−C30)を用いて修飾されているRNActive構築物に移された。最終的な構築物は、1365ヌクレオチドの長さを有しており、「CAP−GcOva(GC)−muag−A70−C30」と名づけられた。当該構築物は、以下の配列要素:
より良好なコドンの利用および安定性のためのCG最適化配列、
muag(変異体化αグロブリンの3’UTR)、
3’末端における70×アデノシン(ポリAテイル)、
3’末端における30×シトシン(ポリCテイル)
を含んでいた。対応するmRNA配列は図7に示されている(配列番号120を参照のこと)。
組換えプラスミドDNAは直線化され、T7 RNAポリメラーゼを用いてインビトロ転写された。DNAの鋳型はそれから、DNAseI消化によって分解された。RNAはLiCl沈殿によって回収され、HPLC抽出(PUREMessger(登録商標)、CureVac Gmbh、Tubingen、Germany)によってさらに精製された。
以下の試験に使用されるmRNAは、指示されている比率(1:1−1:4)(w/w)においてmRNAに対するプロタミンの添加によってプロタミンと複合体化されている。10分間にわたるインキュベーションの後に遊離のRNAが加えられた。
本試験において、容易に調製されたmRNA:プロタミン複合体および/または遊離のRNAを含んでいる組成物の、翻訳に対する影響が試験された。したがって、プロタミンと複合体化されているLacZ−mRNAとの組合せ(2:1および1:1)のあり、またはなしの、ルシフェラーゼ(Pp Luc)をコードしている10μgの遊離のmRNAを含んでいる組成物が調製され、耳介の皮内に注射された。
mRNAの間における複合体形成は考えられず、すでに形成されているLacZ:プロタミン複合体の安定性を示している。
一般的な方法:
300000のE.G7−OVA腫瘍細胞がC57 BL/6マウスに移植される。3週間後に、マウスは、Gallus gallusのオボアルブミンをコードしているGCリッチの20μgのmRNAを含んでいる本発明の組成物を用いて、3週間のうちに8回にわたってワクチン接種された。腫瘍の大きさは、腫瘍細胞の移植から18日後に測定された。
300000のE.G7−OVA腫瘍細胞がC57 BL/6マウスに移植された。マウスは、Gallus gallusのオボアルブミンをコードしているGCリッチの20μgのmRNAをそれぞれ含んでいる本発明の組成物を用いて、2週間のうちに8回にわたってワクチン接種された。この試験のために、3:1の比率においてプロタミンと全体的に複合体化されているRNA、または複合体化されているRNAが1:1、1:4および1:8の比率(w/w)において遊離のRNAと混合されたRNAのいずれかが使用された。
300000のE.G7−OVA腫瘍細胞がC57 BL/6マウスに移植された。マウスは、Gallus gallusのオボアルブミンをコードしているGCリッチの20μgのmRNAをそれぞれ含んでいる本発明の組成物を用いて、3週間のうちに8回にわたってワクチン接種された。この第2の試験のために、改善されたプロトコルにしたがった、3:1の比率においてその全体が複合体化されているRNA、または複合体化されているRNAが3:1のRNA:プロタミン+遊離のRNA(1:1)の比率において遊離のRNAと混合されたRNAのいずれかが使用された。
この試験のためにhPBMCは、Ficoll上における遠心分離(2000rpmにおいて20分間にわたって)によって単離され、続いてPBSにおいて2回にわたって洗浄された。それからhPBMCは、FCS、10%DMSOにおいて5×107/mlの密度に再懸濁された。1mlの分取物が凍結され、−80℃に保存された。
C57 BL/6マウスは、Gallus gallusのオボアルブミンをコードしているCGリッチのmRNA、および「無関係」な対照RNA(pB−Luc RNA)のそれぞれ16μgを用いて、8回にわたってワクチン接種された。したがって、RNAは、2:1の比率においてプロタミンを用いて全体的に調合されたか、またはその比率が改善されたプロトコルにしたがって(2:1のRNA:プロタミン+遊離のRNA(1:1))調合された。最後にワクチン接種してから2週間後に、血液サンプルは回収され、オボアルブミン特異的な抗体の発現が測定された。
この試験のために、プロタミンを用いた異なる製剤計画の、ルシフェラーゼの翻訳に対する影響が調べられた。グループごとに2匹のマウスが、
(1)50%の遊離のRNAと組み合わせてプロタミンが複合体化されている(2:1)50%のLuc−RNAを含んでいる組成物、
(2)4:1の比率においてプロタミンと複合体化されているLuc−RNAを含んでいる組成物、
(3)100%の遊離のRNA、または
(4)対照としてのラクトリンガーバッファー
を用いて4つの異なる部位の皮内に注射を受けた。
すべてのサンプルは、ルシフェラーゼをコードしている10μgのmRNA(Luc−RNA(すなわち配列番号121に係る上述の構築物「T7TS−Ppluc(wt)−A70」))を50μlのラクトリンガーバッファーにおいて含んでいた。また、第1および第2のグループは同量のプロタミンを含んでいたが、それらは異なる製剤として調合された。グループ(1)の組成物は本発明にしたがって調製された。
この試験のために、以下の組成:
(1)プロタミンと複合体化されている20μgのLuc−RNA(2:1)(w/w)および20μgの遊離Luc−RNAを含んでいる2:1(50%)+遊離(50%)(すなわち本発明の免疫賦活組成物)、
(2)プロタミンと複合体化されている40μgのLuc−RNA(4:1)(w/w)を含んでいる4:1(100%)、
(3)40μgの遊離Luc−RNA、
(4)10μgのプロタミン、ならびに
(5)800μlのRiLa(すべてのサンプルは800μlの最終容積までラクトリンガーバッファーに溶解された)
においてルシフェラーゼ(Luc−RNA(すなわち配列番号121に係る上述の構築物「T7TS−Ppluc(wt)−A70」))をコードしている40μgのmRNAがBalb/cマウス(1グループごとに4匹のマウス)の尾静脈に静脈注射された。4時間後に、眼窩後静脈の穿刺によって血液が採取され、血清がサイトカイン(IL−12)ELISAに使用された。ELISAは実施例7に記載の通りに実施された。
ワクチン接種:
Balb/cマウスは、インフルエンザA/Puerto Rico(PR8)のヘマグルチニン(HA)をコードしているGCリッチの20μgのmRNA、または注入バッファー(80%ラクトリンガー液)を用いて2回にわたってワクチン接種された。したがって、RNAは、2:1の比率においてプロタミンと全体的に調合されたか、またはその比率が本発明にしたがって2:1のRNA:プロタミン;遊離のRNA(1:1)(w/w)であった。製剤に関して異なる2つのプロタミン(プロタミン塩酸塩(プロタミンバレアント)およびプロタミン硫酸塩(プロタミンLEO))が試験された。
最後のワクチン接種後の異なる時点において血液サンプルは回収され、ヘマグルチニン特異的抗体の発現がELISA(図11および12)またはヘマグルチニン阻害アッセイ(HAI)(図13)によって決定された。
ELISAによる抗原特異的抗体の検出のために、MaxiSrobプレート(Nalgene Nunc international)は抗原(不活化PRB)を用いて被覆された。1×PBS、0.05%Tweenおよび1%のBSAを用いたブロッキングの後に、プレートはマウスの血清を用いて4時間にわたって室温においてインキュベートされた。続いてビオチンが結合した二次抗体が加えられた。洗浄の後に、プレートはホースラディッシュペルオキシダーゼを用いてインキュベートされ、酵素活性は基質(2,2’−アジノ−ビス(3−エチル−ベンズチアゾリン−6−スルホン酸))の転換を測定(OD405nm)することによって決定された。吸光度はTecanのELISAプレートリーダーを用いて405nmにおいて測定された。免疫後の2週間において得られた血清の解析の結果は図11に示されている。図11に示されているように、遊離のRNAと複合体化されているRNAは、全体的に複合体化されているRNAを用いたワクチン接種と比べて、高い液性免疫応答を導く。裸のRNAと比べて、複合体化されているRNAはより高いIgG2a抗体の力価を導き、これはTh1誘導応答の指標である。
また、免疫されたマウスの血清はHAIアッセイによって分析された。HAIアッセイにおいてウイルス性のヘマグルチニンの相互作用を阻害することによってウイルスを中和する抗体および宿主細胞上におけるシアル酸が検出された。
Claims (10)
- (a)カチオン性またはポリカチオン性の化合物と複合体化された少なくとも1個のRNAを含んでいるか、カチオン性またはポリカチオン性の化合物と複合体化された少なくとも1個のRNAからなる、アジュバント成分と
(b)少なくとも1個の治療的に活性な、タンパク質、抗原および/または抗体をコードする、少なくとも1個の遊離のmRNAと
を含んでおり、
哺乳動物において、先天性の免疫応答を誘発するか、増強することができ、必要に応じて適応性の免疫応答を誘発するか、増強することができる、免疫賦活組成物。 - 前記アジュバント成分の少なくとも1個のRNAが、短いRNAオリゴヌクレオチド、mRNAを含むコーディングRNA、免疫賦活性のRNA、siRNA、アンチセンスRNA、またはリボスイッチ、リボザイムもしくはアプタマーから選択される、請求項1に記載の免疫賦活組成物。
- 前記アジュバント成分の少なくとも1個のRNAがmRNAである、請求項1または2に記載の免疫賦活組成物。
- 前記少なくとも1個の遊離のmRNAと前記アジュバント成分の少なくとも1個のRNAとが、互いに同一である、請求項1〜3のいずれか1項に記載の免疫賦活組成物。
- 前記少なくとも1個のmRNAと前記アジュバント成分の少なくとも1個のRNAとが、互いに異なる、請求項1〜3のいずれか1項に記載の免疫賦活組成物。
- 前記アジュバント成分中の前記RNAと前記カチオン性またはポリカチオン性の化合物とのN/Pの比は、0.1〜10であり、
該0.1〜10は、0.3〜4、0.5〜2、0.7〜2、および0.7〜15を含む、請求項1〜5のいずれか1項に記載の免疫賦活組成物。 - 前記アジュバント成分のRNAと、前記成分(b)の前記少なくとも1個の遊離のmRNAとのモル比が、1:1のモル比を含む0.001:1〜1:0.001のモル比から選択され得る、請求項1〜6のいずれか1項に記載の免疫賦活組成物。
- 前記少なくとも1個の遊離のmRNAおよび/または前記アジュバント成分の少なくとも1個のRNAが、GCによって安定化されている、請求項1〜7のいずれか1項に記載の免疫賦活組成物。
- 前記GCによって安定化されたRNAのコード領域のG/C含有量が、ネイティブなRNAのコード領域のG/C含有量と比較して増加しており、
該GCによって安定化された修飾されたRNAのコードされたアミノ酸配列が、該ネイティブな修飾されたRNAのコードされたアミノ酸配列と比較して変化していない、請求項8に記載の免疫賦活組成物。 - 請求項1〜9のいずれか1項にて規定した免疫賦活組成物を調製するための方法であって、
請求項1〜9にて規定した、少なくとも1個のRNAとカチオン性またはポリカチオン性の化合物とを特定の比にて混合することによって、カチオン性またはポリカチオン性の化合物と複合体化された少なくとも1個のRNAを含んでいるか、カチオン性またはポリカチオン性の化合物と複合体化された少なくとも1個のRNAからなる、アジュバント成分を調製する工程(a)と、
請求項1〜9のいずれか1項にて規定した少なくとも1個の遊離のmRNAを、工程(a)にて調製されたアジュバント成分に特定の比にて添加することによって、本発明の免疫賦活組成物を調製する工程(b)と
を包含しており、
該少なくとも1個の遊離のmRNAは、請求項1〜9のいずれか1項にて規定した少なくとも1個の治療的に活性なタンパク質、抗原および/または抗体をコードするをコードしている、方法。
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PCT/EP2008/008304 WO2010037408A1 (en) | 2008-09-30 | 2008-09-30 | Composition comprising a complexed (m)rna and a naked mrna for providing or enhancing an immunostimulatory response in a mammal and uses thereof |
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