-
Je něco špatně v tomto záznamu ?
Complexes of streptavidin-fused antigens with biotinylated antibodies targeting receptors on dendritic cell surface: a novel tool for induction of specific T-cell immune responses
O. Stanek, I. Linhartova, L. Majlessi, C. Leclerc, P. Sebo,
Jazyk angličtina Země Spojené státy americké
Typ dokumentu časopisecké články, práce podpořená grantem
NLK
ProQuest Central
od 1997-02-01 do Před 1 rokem
Medline Complete (EBSCOhost)
od 2011-01-01 do Před 1 rokem
Health & Medicine (ProQuest)
od 1997-02-01 do Před 1 rokem
- MeSH
- antigeny CD11c imunologie metabolismus MeSH
- antigeny chemie genetika imunologie metabolismus MeSH
- biotinylace MeSH
- buněčné linie MeSH
- dendritické buňky imunologie metabolismus MeSH
- kur domácí MeSH
- molekulární sekvence - údaje MeSH
- myši inbrední C57BL MeSH
- myši MeSH
- ovalbumin chemie genetika imunologie metabolismus MeSH
- receptory buněčného povrchu imunologie metabolismus MeSH
- rekombinantní fúzní proteiny chemie genetika imunologie metabolismus MeSH
- rozpustnost MeSH
- sekvence aminokyselin MeSH
- sekvence nukleotidů MeSH
- streptavidin chemie genetika imunologie metabolismus MeSH
- T-lymfocyty imunologie metabolismus MeSH
- zvířata MeSH
- Check Tag
- myši MeSH
- ženské pohlaví MeSH
- zvířata MeSH
- Publikační typ
- časopisecké články MeSH
- práce podpořená grantem MeSH
The choice of tools that enable efficient targeting of exogenous antigens (Ag) for processing and presentation by professional Ag-presenting cells (APC) remains limited. This represents, indeed, a bottleneck in development of vaccines inducing specific T-cell responses. Here, we describe a novel strategy of Ag delivery into APCs. The Ag of choice is fused to the N- or C-terminus of streptavidin (SA) and tetrameric Ag-SA or SA-Ag fusion proteins are produced in E. coli and purified by 2-Iminobiotin-Agarose affinity chromatography. Alternatively, Ag-SA proteins are purified from urea extracts of E. coli inclusion bodies and refolded in vitro into functional tetramers. Complexes with biotinylated antibodies targeting cell surface receptors are formed and used to deliver the Ags of choice for processing and presentation by APCs and induction of Ag-specific CD4+ and CD8+ T-cell responses in vitro and in vivo.
Citace poskytuje Crossref.org
- 000
- 00000naa a2200000 a 4500
- 001
- bmc13001008
- 003
- CZ-PrNML
- 005
- 20130213095428.0
- 007
- ta
- 008
- 130108s2012 xxu f 000 0|eng||
- 009
- AR
- 024 7_
- $a 10.1007/s12033-011-9459-6 $2 doi
- 035 __
- $a (PubMed)22006508
- 040 __
- $a ABA008 $b cze $d ABA008 $e AACR2
- 041 0_
- $a eng
- 044 __
- $a xxu
- 100 1_
- $a Stanek, Ondrej $u Laboratory of Molecular Biology of Bacterial Pathogens, Institute of Microbiology of the ASCR, Videnska 1083, 14220 Prague, Czech Republic.
- 245 10
- $a Complexes of streptavidin-fused antigens with biotinylated antibodies targeting receptors on dendritic cell surface: a novel tool for induction of specific T-cell immune responses / $c O. Stanek, I. Linhartova, L. Majlessi, C. Leclerc, P. Sebo,
- 520 9_
- $a The choice of tools that enable efficient targeting of exogenous antigens (Ag) for processing and presentation by professional Ag-presenting cells (APC) remains limited. This represents, indeed, a bottleneck in development of vaccines inducing specific T-cell responses. Here, we describe a novel strategy of Ag delivery into APCs. The Ag of choice is fused to the N- or C-terminus of streptavidin (SA) and tetrameric Ag-SA or SA-Ag fusion proteins are produced in E. coli and purified by 2-Iminobiotin-Agarose affinity chromatography. Alternatively, Ag-SA proteins are purified from urea extracts of E. coli inclusion bodies and refolded in vitro into functional tetramers. Complexes with biotinylated antibodies targeting cell surface receptors are formed and used to deliver the Ags of choice for processing and presentation by APCs and induction of Ag-specific CD4+ and CD8+ T-cell responses in vitro and in vivo.
- 650 _2
- $a sekvence aminokyselin $7 D000595
- 650 _2
- $a zvířata $7 D000818
- 650 _2
- $a antigeny $x chemie $x genetika $x imunologie $x metabolismus $7 D000941
- 650 _2
- $a antigeny CD11c $x imunologie $x metabolismus $7 D039521
- 650 _2
- $a sekvence nukleotidů $7 D001483
- 650 _2
- $a biotinylace $7 D019921
- 650 _2
- $a buněčné linie $7 D002460
- 650 _2
- $a kur domácí $7 D002645
- 650 _2
- $a dendritické buňky $x imunologie $x metabolismus $7 D003713
- 650 _2
- $a ženské pohlaví $7 D005260
- 650 _2
- $a myši $7 D051379
- 650 _2
- $a myši inbrední C57BL $7 D008810
- 650 _2
- $a molekulární sekvence - údaje $7 D008969
- 650 _2
- $a ovalbumin $x chemie $x genetika $x imunologie $x metabolismus $7 D010047
- 650 _2
- $a receptory buněčného povrchu $x imunologie $x metabolismus $7 D011956
- 650 _2
- $a rekombinantní fúzní proteiny $x chemie $x genetika $x imunologie $x metabolismus $7 D011993
- 650 _2
- $a rozpustnost $7 D012995
- 650 _2
- $a streptavidin $x chemie $x genetika $x imunologie $x metabolismus $7 D019809
- 650 _2
- $a T-lymfocyty $x imunologie $x metabolismus $7 D013601
- 655 _2
- $a časopisecké články $7 D016428
- 655 _2
- $a práce podpořená grantem $7 D013485
- 700 1_
- $a Linhartova, Irena
- 700 1_
- $a Majlessi, Laleh
- 700 1_
- $a Leclerc, Claude
- 700 1_
- $a Sebo, Peter
- 773 0_
- $w MED00180392 $t Molecular biotechnology $x 1559-0305 $g Roč. 51, č. 3 (2012), s. 221-32
- 856 41
- $u https://pubmed.ncbi.nlm.nih.gov/22006508 $y Pubmed
- 910 __
- $a ABA008 $b sig $c sign $y a $z 0
- 990 __
- $a 20130108 $b ABA008
- 991 __
- $a 20130213095612 $b ABA008
- 999 __
- $a ok $b bmc $g 963790 $s 799172
- BAS __
- $a 3
- BAS __
- $a PreBMC
- BMC __
- $a 2012 $b 51 $c 3 $d 221-32 $i 1559-0305 $m Molecular biotechnology $n Mol Biotechnol $x MED00180392
- LZP __
- $a Pubmed-20130108
