Murine B-cell and T-cell epitopes of the allergen Hev b 5 from natural rubber latex.
Identifieur interne : 002628 ( PubMed/Corpus ); précédent : 002627; suivant : 002629Murine B-cell and T-cell epitopes of the allergen Hev b 5 from natural rubber latex.
Auteurs : J E Slater ; E J Paupore ; R E O'HehirSource :
- Molecular immunology [ 0161-5890 ] ; 1999.
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
Links to Exploration step
pubmed:10378685Le document en format XML
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<author><name sortKey="Paupore, E J" sort="Paupore, E J" uniqKey="Paupore E" first="E J" last="Paupore">E J Paupore</name>
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<author><name sortKey="O Hehir, R E" sort="O Hehir, R E" uniqKey="O Hehir R" first="R E" last="O'Hehir">R E O'Hehir</name>
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<term>Amino Acid Sequence</term>
<term>Animals</term>
<term>Antigen Presentation</term>
<term>Antigens, Plant</term>
<term>B-Lymphocytes (immunology)</term>
<term>Epitopes (genetics)</term>
<term>Epitopes (immunology)</term>
<term>Latex Hypersensitivity (immunology)</term>
<term>Lymphocyte Cooperation</term>
<term>Mice</term>
<term>Molecular Sequence Data</term>
<term>Peptide Fragments (genetics)</term>
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<term>Plant Proteins</term>
<term>Sequence Analysis</term>
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<term>Animals</term>
<term>Antigen Presentation</term>
<term>Antigens, Plant</term>
<term>Lymphocyte Cooperation</term>
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<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>
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<Abstract><AbstractText>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.</AbstractText>
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