Localization of HLA-A2.1-restricted T cell epitopes in the circumsporozoite protein of Plasmodium falciparum.
Identifieur interne : 002826 ( PubMed/Curation ); précédent : 002825; suivant : 002827Localization of HLA-A2.1-restricted T cell epitopes in the circumsporozoite protein of Plasmodium falciparum.
Auteurs : U. Blum-Tirouvanziam [Suisse] ; C. Servis ; A. Habluetzel ; D. Valmori ; Y. Men ; F. Esposito ; L. Del Nero ; N. Holmes ; N. Fasel ; G. CorradinSource :
- Journal of immunology (Baltimore, Md. : 1950) [ 0022-1767 ] ; 1995.
Descripteurs français
- KwdFr :
- Activation des lymphocytes, Animaux, Antigène HLA-A2 (immunologie), Cartographie épitopique, Cytotoxicité immunologique, Données de séquences moléculaires, Humains, Immunité cellulaire, Interféron gamma (biosynthèse), Liaison aux protéines, Lymphocytes T (immunologie), Paludisme à Plasmodium falciparum (immunologie), Peptides (), Peptides (immunologie), Peptides (métabolisme), Plasmodium falciparum (immunologie), Protéines de protozoaire (immunologie), Souris, Souris transgéniques, Séquence d'acides aminés, Épitopes.
- MESH :
- biosynthèse : Interféron gamma.
- immunologie : Antigène HLA-A2, Lymphocytes T, Paludisme à Plasmodium falciparum, Peptides, Plasmodium falciparum, Protéines de protozoaire.
- métabolisme : Peptides.
- Activation des lymphocytes, Animaux, Cartographie épitopique, Cytotoxicité immunologique, Données de séquences moléculaires, Humains, Immunité cellulaire, Liaison aux protéines, Peptides, Souris, Souris transgéniques, Séquence d'acides aminés, Épitopes.
English descriptors
- KwdEn :
- Amino Acid Sequence, Animals, Cytotoxicity, Immunologic, Epitope Mapping, Epitopes, HLA-A2 Antigen (immunology), Humans, Immunity, Cellular, Interferon-gamma (biosynthesis), Lymphocyte Activation, Malaria, Falciparum (immunology), Mice, Mice, Transgenic, Molecular Sequence Data, Peptides (chemistry), Peptides (immunology), Peptides (metabolism), Plasmodium falciparum (immunology), Protein Binding, Protozoan Proteins (immunology), T-Lymphocytes (immunology).
- MESH :
- chemical , biosynthesis : Interferon-gamma.
- chemical , chemistry : Peptides.
- chemical , immunology : HLA-A2 Antigen, Peptides, Protozoan Proteins.
- chemical , metabolism : Peptides.
- chemical : Epitopes.
- immunology : Malaria, Falciparum, Plasmodium falciparum, T-Lymphocytes.
- Amino Acid Sequence, Animals, Cytotoxicity, Immunologic, Epitope Mapping, Humans, Immunity, Cellular, Lymphocyte Activation, Mice, Mice, Transgenic, Molecular Sequence Data, Protein Binding.
Abstract
Localization of human MHC class I-restricted T cell epitopes in the circumsporozoite (CS) protein of the human parasite Plasmodium falciparum is an important objective in the development of antimalarial vaccines. To this purpose, we synthesized a series of overlapping synthetic 20-mer peptides, spanning the entire sequence of the 7G8 CS molecule except for the central repeat B cell domain. The P.f.CS peptides were first tested for their ability to bind to the human MHC class I HLA-A2.1 molecule on T2, a human cell line. Subsequently, the use of a series of shorter peptide analogues allowed us to determine the optimal A2.1 binding sequence present in several of the 20-mers. Binding P.f.CS peptides were further tested for their capacity to activate PBL from HLA-A2.1+ immune donors living in a malaria-endemic area. Specific IFN-gamma production was detected in the supernatant of cultures of PBL from exposed individuals. Cytotoxic T cell lines and clones were derived from the PBL of one responder, and their activity was shown to be HLA-A2.1-restricted and specific for the peptide 334-342 of the CS protein. In addition, double transgenic HLA-A2.1 x human beta 2-microglobulin mice were immunized with peptide 1-10 of the CS protein. T cells derived from immune lymph nodes displayed a peptide-specific HLA-A2.1-restricted cytolytic activity after one in vitro stimulation.
PubMed: 7535817
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pubmed:7535817Le document en format XML
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<term>Epitopes</term>
<term>HLA-A2 Antigen (immunology)</term>
<term>Humans</term>
<term>Immunity, Cellular</term>
<term>Interferon-gamma (biosynthesis)</term>
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<term>Cytotoxicité immunologique</term>
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<front><div type="abstract" xml:lang="en">Localization of human MHC class I-restricted T cell epitopes in the circumsporozoite (CS) protein of the human parasite Plasmodium falciparum is an important objective in the development of antimalarial vaccines. To this purpose, we synthesized a series of overlapping synthetic 20-mer peptides, spanning the entire sequence of the 7G8 CS molecule except for the central repeat B cell domain. The P.f.CS peptides were first tested for their ability to bind to the human MHC class I HLA-A2.1 molecule on T2, a human cell line. Subsequently, the use of a series of shorter peptide analogues allowed us to determine the optimal A2.1 binding sequence present in several of the 20-mers. Binding P.f.CS peptides were further tested for their capacity to activate PBL from HLA-A2.1+ immune donors living in a malaria-endemic area. Specific IFN-gamma production was detected in the supernatant of cultures of PBL from exposed individuals. Cytotoxic T cell lines and clones were derived from the PBL of one responder, and their activity was shown to be HLA-A2.1-restricted and specific for the peptide 334-342 of the CS protein. In addition, double transgenic HLA-A2.1 x human beta 2-microglobulin mice were immunized with peptide 1-10 of the CS protein. T cells derived from immune lymph nodes displayed a peptide-specific HLA-A2.1-restricted cytolytic activity after one in vitro stimulation.</div>
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<Abstract><AbstractText>Localization of human MHC class I-restricted T cell epitopes in the circumsporozoite (CS) protein of the human parasite Plasmodium falciparum is an important objective in the development of antimalarial vaccines. To this purpose, we synthesized a series of overlapping synthetic 20-mer peptides, spanning the entire sequence of the 7G8 CS molecule except for the central repeat B cell domain. The P.f.CS peptides were first tested for their ability to bind to the human MHC class I HLA-A2.1 molecule on T2, a human cell line. Subsequently, the use of a series of shorter peptide analogues allowed us to determine the optimal A2.1 binding sequence present in several of the 20-mers. Binding P.f.CS peptides were further tested for their capacity to activate PBL from HLA-A2.1+ immune donors living in a malaria-endemic area. Specific IFN-gamma production was detected in the supernatant of cultures of PBL from exposed individuals. Cytotoxic T cell lines and clones were derived from the PBL of one responder, and their activity was shown to be HLA-A2.1-restricted and specific for the peptide 334-342 of the CS protein. In addition, double transgenic HLA-A2.1 x human beta 2-microglobulin mice were immunized with peptide 1-10 of the CS protein. T cells derived from immune lymph nodes displayed a peptide-specific HLA-A2.1-restricted cytolytic activity after one in vitro stimulation.</AbstractText>
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