Murine B-cell and T-cell epitopes of the allergen Hev b 5 from natural rubber latex.
Identifieur interne : 002628 ( PubMed/Curation ); précédent : 002627; suivant : 002629Murine B-cell and T-cell epitopes of the allergen Hev b 5 from natural rubber latex.
Auteurs : J E Slater [États-Unis] ; E J Paupore ; R E O'HehirSource :
- Molecular immunology [ 0161-5890 ] ; 1999.
Descripteurs français
- KwdFr :
- Allergènes (génétique), Allergènes (immunologie), Analyse de séquence, Animaux, Antigènes végétaux, Coopération des lymphocytes, Données de séquences moléculaires, Fragments peptidiques (génétique), Fragments peptidiques (immunologie), Hypersensibilité au latex (immunologie), Lymphocytes B (immunologie), Lymphocytes T (immunologie), Protéines végétales, Présentation d'antigène, Souris, Séquence d'acides aminés, Épitopes (génétique), Épitopes (immunologie).
- MESH :
- génétique : Allergènes, Fragments peptidiques, Épitopes.
- immunologie : Allergènes, Fragments peptidiques, Hypersensibilité au latex, Lymphocytes B, Lymphocytes T, Épitopes.
- Analyse de séquence, Animaux, Antigènes végétaux, Coopération des lymphocytes, Données de séquences moléculaires, Protéines végétales, Présentation d'antigène, Souris, Séquence d'acides aminés.
English descriptors
- KwdEn :
- Allergens (genetics), Allergens (immunology), Amino Acid Sequence, Animals, Antigen Presentation, Antigens, Plant, B-Lymphocytes (immunology), Epitopes (genetics), Epitopes (immunology), Latex Hypersensitivity (immunology), Lymphocyte Cooperation, Mice, Molecular Sequence Data, Peptide Fragments (genetics), Peptide Fragments (immunology), Plant Proteins, Sequence Analysis, T-Lymphocytes (immunology).
- MESH :
- chemical , genetics : Allergens, Epitopes, Peptide Fragments.
- chemical , immunology : Allergens, Epitopes, Peptide Fragments.
- immunology : B-Lymphocytes, Latex Hypersensitivity, T-Lymphocytes.
- Amino Acid Sequence, Animals, Antigen Presentation, Antigens, Plant, Lymphocyte Cooperation, Mice, Molecular Sequence Data, Plant Proteins, Sequence Analysis.
Abstract
Hev b 5, a proline-rich acidic protein with a predominantly random secondary structure, is a major allergen in natural rubber latex and a candidate for specific immunotherapy of latex allergy. As a first step in the identification of candidate peptides for immunotherapy, we have begun to identify the B-cell and T-cell epitopes of Hev b 5 in BALB/c mice. The mice were immunized with a Hev b 5 fusion protein. The B-cell epitopes were determined by the SPOTS method using overlapping octamers or by ELISA inhibition using a series of overlapping 20-mers. The T-cell epitopes were determined by the proliferation and cytokine release of splenocytes cultured in the presence of the 20-mers. Potential antibody binding regions included residues in regions 1-38, 55-74, 109-128 and 132-151. Examination of the binding sequences for common motifs suggested enhanced antibody binding to the KXEE or KEXE sequences, where X is empty, threonine or alanine. Splenocyte stimulation and cytokine release suggest T-cell epitopes with the regions 1-20, 37-56, 73-101 and 109-146. Since they may contain major T-cell epitopes but do not exhibit significant antibody binding, peptide regions 38-48 and 75-101 are candidates for specific immunotherapy to Hev b 5 in the BALB/c mouse model.
DOI: 10.1016/s0161-5890(99)00021-8
PubMed: 10378685
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Hypersensitivity</term><term>T-Lymphocytes</term></keywords><keywords scheme="MESH" xml:lang="en"><term>Amino Acid Sequence</term><term>Animals</term><term>Antigen Presentation</term><term>Antigens, Plant</term><term>Lymphocyte Cooperation</term><term>Mice</term><term>Molecular Sequence Data</term><term>Plant Proteins</term><term>Sequence Analysis</term></keywords><keywords scheme="MESH" xml:lang="fr"><term>Analyse de séquence</term><term>Animaux</term><term>Antigènes végétaux</term><term>Coopération des lymphocytes</term><term>Données de séquences moléculaires</term><term>Protéines végétales</term><term>Présentation d'antigène</term><term>Souris</term><term>Séquence d'acides aminés</term></keywords></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">Hev b 5, a proline-rich acidic protein with a predominantly random secondary structure, is a major allergen in natural rubber latex and a candidate for specific immunotherapy of latex allergy. As a first step in the identification of candidate peptides for immunotherapy, we have begun to identify the B-cell and T-cell epitopes of Hev b 5 in BALB/c mice. The mice were immunized with a Hev b 5 fusion protein. The B-cell epitopes were determined by the SPOTS method using overlapping octamers or by ELISA inhibition using a series of overlapping 20-mers. The T-cell epitopes were determined by the proliferation and cytokine release of splenocytes cultured in the presence of the 20-mers. Potential antibody binding regions included residues in regions 1-38, 55-74, 109-128 and 132-151. Examination of the binding sequences for common motifs suggested enhanced antibody binding to the KXEE or KEXE sequences, where X is empty, threonine or alanine. Splenocyte stimulation and cytokine release suggest T-cell epitopes with the regions 1-20, 37-56, 73-101 and 109-146. Since they may contain major T-cell epitopes but do not exhibit significant antibody binding, peptide regions 38-48 and 75-101 are candidates for specific immunotherapy to Hev b 5 in the BALB/c mouse model.</div></front></TEI><pubmed><MedlineCitation Status="MEDLINE" Owner="NLM"><PMID Version="1">10378685</PMID><DateCompleted><Year>1999</Year><Month>07</Month><Day>06</Day></DateCompleted><DateRevised><Year>2019</Year><Month>08</Month><Day>26</Day></DateRevised><Article PubModel="Print"><Journal><ISSN IssnType="Print">0161-5890</ISSN><JournalIssue CitedMedium="Print"><Volume>36</Volume><Issue>2</Issue><PubDate><Year>1999</Year><Month>Feb</Month></PubDate></JournalIssue><Title>Molecular immunology</Title><ISOAbbreviation>Mol. 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Potential antibody binding regions included residues in regions 1-38, 55-74, 109-128 and 132-151. Examination of the binding sequences for common motifs suggested enhanced antibody binding to the KXEE or KEXE sequences, where X is empty, threonine or alanine. Splenocyte stimulation and cytokine release suggest T-cell epitopes with the regions 1-20, 37-56, 73-101 and 109-146. 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