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Titolo:
DR-ALPHA-EP HETERODIMERS IN DRA TRANSGENIC MICE HINDER EXPRESSION OF E-ALPHA-EP MOLECULES AND ARE MORE EFFICIENT IN ANTIGEN PRESENTATION
Autore:
TREMBLEAU S; GIACOMINI P; GUERY JC; SETINI A; HAMMER J; SETTE A; APPELLA E; ADORINI L;
Indirizzi:
ROCHE MILANO RIC,VIA OLGETTINA 58 I-20132 MILAN ITALY ROCHE MILANO RIC I-20132 MILAN ITALY IST REGINA ELENA,IMMUNOL LAB I-00158 ROME ITALY NCI BETHESDA MD 20892
Titolo Testata:
International immunology
fascicolo: 12, volume: 7, anno: 1995,
pagine: 1927 - 1938
SICI:
0953-8178(1995)7:12<1927:DHIDTM>2.0.ZU;2-U
Fonte:
ISI
Lingua:
ENG
Soggetto:
MAJOR HISTOCOMPATIBILITY COMPLEX; T-CELL RECOGNITION; CLASS-II MOLECULES; MONOCLONAL-ANTIBODIES; HLA-DR; SURFACE EXPRESSION; IA MOLECULE; AMINO-ACIDS; GENE; PEPTIDES;
Keywords:
ANTIGEN PRESENTATION; HEMIXENOGENIC MHC CLASS II; HLA-DRA TRANSGENIC MICE;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Science Citation Index Expanded
Citazioni:
38
Recensione:
Indirizzi per estratti:
Citazione:
S. Trembleau et al., "DR-ALPHA-EP HETERODIMERS IN DRA TRANSGENIC MICE HINDER EXPRESSION OF E-ALPHA-EP MOLECULES AND ARE MORE EFFICIENT IN ANTIGEN PRESENTATION", International immunology, 7(12), 1995, pp. 1927-1938

Abstract

HLA-DRA transgenic (tg) mice on H-2(d) background were constructed tostudy assembly, expression and function of DR alpha:E beta class II heterodimers when an alternate E alpha chain is available. Cytofluorimetric analysis and immunoprecipitation studies demonstrate that the majority (90%) of E beta(d) molecules on class II-positive splenocytes from DRA-tg mice are associated with DR alpha rather than E alpha chains. To characterize the functional role of the interspecies as compared with the wild-type I-E molecules, MHC restriction and T cell epitope immunodominance of synthetic peptides spanning the entire sequence of 65 kDa heat shock protein (hsp) from Mycobacterium tuberculosis were determined in hsp-primed DRA-tg and DBA/2 mice. A similar pattern of responsiveness was observed in both strains, but hsp epitopes recalled a higher response in DRA-tg as compared with DBA/2 mice. A panel of T cell hybridomas specific for two hsp peptides or a hen egg white lysozyme peptide presented by both DR alpha:E beta(d) and E alpha(d):E beta(d) was studied in detail. Surprisingly, DR alpha:E beta(d) dimers present these peptides more efficiently than E alpha:E beta(d), even when the TCR was selected in mice expressing only E alpha(d):E beta d molecules. The higher efficiency of antigen presentation by DR alpha:E beta(d) dimers does not appear to depend on increased binding affinity for peptides, as demonstrated by competition for antigen presentation, noron increased efficiency in the interaction with CD4 molecules. Rather, the higher efficiency of antigen presentation could be explained by a more effective ligand-TCR interaction. This is consistent with molecular modeling based on the class II structure, indicating that 16 out of 17 substitutions between the first domain of E alpha(d) and DR alpha chains lie outside the peptide binding groove and are potentially available for interaction with the TCR.

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Documento generato il 15/07/20 alle ore 03:18:08