Identification of murine B-cell and T-cell epitopes of Escherichia coli outer membrane protein F with synthetic polypeptides.
Identifieur interne : 003664 ( Main/Merge ); précédent : 003663; suivant : 003665Identification of murine B-cell and T-cell epitopes of Escherichia coli outer membrane protein F with synthetic polypeptides.
Auteurs : K M Williams [États-Unis] ; E C Bigley ; R B RaybourneSource :
- Infection and immunity [ 0019-9567 ] ; 2000.
Descripteurs français
- KwdFr :
- Animaux, Anticorps antibactériens (immunologie), Antigènes bactériens (immunologie), Cartographie épitopique (), Division cellulaire, Données de séquences moléculaires, Déterminants antigéniques des lymphocytes B (immunologie), Déterminants antigéniques des lymphocytes T (immunologie), Escherichia coli (immunologie), Interleukine-2 (biosynthèse), Interleukine-4 (biosynthèse), Lignées consanguines de souris, Lymphocytes T (cytologie), Lymphocytes T (immunologie), Peptides (immunologie), Peptides (synthèse chimique), Porines (immunologie), Porines (synthèse chimique), Souris, Séquence d'acides aminés.
- MESH :
- biosynthèse : Interleukine-2, Interleukine-4.
- cytologie : Lymphocytes T.
- immunologie : Anticorps antibactériens, Antigènes bactériens, Déterminants antigéniques des lymphocytes B, Déterminants antigéniques des lymphocytes T, Escherichia coli, Lymphocytes T, Peptides, Porines.
- synthèse chimique : Peptides, Porines.
- Animaux, Cartographie épitopique, Division cellulaire, Données de séquences moléculaires, Lignées consanguines de souris, Souris, Séquence d'acides aminés.
English descriptors
- KwdEn :
- Amino Acid Sequence, Animals, Antibodies, Bacterial (immunology), Antigens, Bacterial (immunology), Cell Division, Epitope Mapping (methods), Epitopes, B-Lymphocyte (immunology), Epitopes, T-Lymphocyte (immunology), Escherichia coli (immunology), Interleukin-2 (biosynthesis), Interleukin-4 (biosynthesis), Mice, Mice, Inbred Strains, Molecular Sequence Data, Peptides (chemical synthesis), Peptides (immunology), Porins (chemical synthesis), Porins (immunology), T-Lymphocytes (cytology), T-Lymphocytes (immunology).
- MESH :
- chemical , biosynthesis : Interleukin-2, Interleukin-4.
- chemical , chemical synthesis : Peptides, Porins.
- chemical , immunology : Antibodies, Bacterial, Antigens, Bacterial, Epitopes, B-Lymphocyte, Epitopes, T-Lymphocyte, Peptides, Porins.
- cytology : T-Lymphocytes.
- immunology : Escherichia coli, T-Lymphocytes.
- methods : Epitope Mapping.
- Amino Acid Sequence, Animals, Cell Division, Mice, Mice, Inbred Strains, Molecular Sequence Data.
Abstract
The major pore-forming outer membrane proteins (Omps) of gram-negative bacteria demonstrate numerous immunomodulating properties and are involved in the virulence of pathogenic strains. Because Escherichia coli OmpF is the best-characterized porin in terms of structural and functional characteristics, in vitro B-cell and T-cell responses to this porin in six different strains of mice were analyzed. Mice were immunized with purified OmpF trimers or overlapping synthetic polypeptides (20-mers) spanning the entire 340-amino-acid sequence of the OmpF monomer. T-cell proliferative responses and immunoglobulin G antibody responses to native OmpF and the peptide analogues were determined. For each strain, patterns of T-cell proliferation were similar regardless of whether native OmpF or synthetic peptides were inoculated, although all strains recognized one or more cryptic determinants. Mice exhibited several haplotype-specific responses, but genetically permissive epitopes were also identified. Four peptides (75-94, 265-284, 295-314, and 305-324) elicited strong T-cell proliferative responses from all strains of mice when mice were presensitized with native OmpF or a homologous peptide. In general, 10 or fewer peptides were recognized by sera from mice immunized with native OmpF or synthetic peptides, and most sera from peptide-immunized mice reacted poorly with the native protein. Four peptides spanning amino acids 45 to 64, 95 to 114, 115 to 134, and 275 to 294 were recognized by sera from all strains immunized with native OmpF but not by sera from peptide-immunized mice. Peptides 245-264 and 305-324 were universally recognized by sera from peptide-immunized mice, but these sera reacted weakly or were negative when tested against the native protein. Based on the pattern of cytokine secretion by proliferating T cells, immunization with native OmpF polarizes T helper cells toward development of a TH1 response. T-cell and B-cell responses have been investigated based on the assumption that differences in epitope specificity could influence protective or pathologic host reactions. Because of the high level of structural homology of OmpF to porins isolated from other enteric pathogens, the identification of T- and B-cell-stimulatory determinants of E. coli OmpF may have broader application.
DOI: 10.1128/iai.68.5.2535-2545.2000
PubMed: 10768941
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pubmed:10768941Le document en format XML
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<term>Animals</term>
<term>Antibodies, Bacterial (immunology)</term>
<term>Antigens, Bacterial (immunology)</term>
<term>Cell Division</term>
<term>Epitope Mapping (methods)</term>
<term>Epitopes, B-Lymphocyte (immunology)</term>
<term>Epitopes, T-Lymphocyte (immunology)</term>
<term>Escherichia coli (immunology)</term>
<term>Interleukin-2 (biosynthesis)</term>
<term>Interleukin-4 (biosynthesis)</term>
<term>Mice</term>
<term>Mice, Inbred Strains</term>
<term>Molecular Sequence Data</term>
<term>Peptides (chemical synthesis)</term>
<term>Peptides (immunology)</term>
<term>Porins (chemical synthesis)</term>
<term>Porins (immunology)</term>
<term>T-Lymphocytes (cytology)</term>
<term>T-Lymphocytes (immunology)</term>
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<term>Anticorps antibactériens (immunologie)</term>
<term>Antigènes bactériens (immunologie)</term>
<term>Cartographie épitopique ()</term>
<term>Division cellulaire</term>
<term>Données de séquences moléculaires</term>
<term>Déterminants antigéniques des lymphocytes B (immunologie)</term>
<term>Déterminants antigéniques des lymphocytes T (immunologie)</term>
<term>Escherichia coli (immunologie)</term>
<term>Interleukine-2 (biosynthèse)</term>
<term>Interleukine-4 (biosynthèse)</term>
<term>Lignées consanguines de souris</term>
<term>Lymphocytes T (cytologie)</term>
<term>Lymphocytes T (immunologie)</term>
<term>Peptides (immunologie)</term>
<term>Peptides (synthèse chimique)</term>
<term>Porines (immunologie)</term>
<term>Porines (synthèse chimique)</term>
<term>Souris</term>
<term>Séquence d'acides aminés</term>
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<term>Interleukin-4</term>
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<term>Porins</term>
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<term>Epitopes, T-Lymphocyte</term>
<term>Peptides</term>
<term>Porins</term>
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<term>Antigènes bactériens</term>
<term>Déterminants antigéniques des lymphocytes B</term>
<term>Déterminants antigéniques des lymphocytes T</term>
<term>Escherichia coli</term>
<term>Lymphocytes T</term>
<term>Peptides</term>
<term>Porines</term>
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<term>T-Lymphocytes</term>
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<keywords scheme="MESH" qualifier="synthèse chimique" xml:lang="fr"><term>Peptides</term>
<term>Porines</term>
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<term>Cell Division</term>
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<term>Mice, Inbred Strains</term>
<term>Molecular Sequence Data</term>
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<term>Cartographie épitopique</term>
<term>Division cellulaire</term>
<term>Données de séquences moléculaires</term>
<term>Lignées consanguines de souris</term>
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<front><div type="abstract" xml:lang="en">The major pore-forming outer membrane proteins (Omps) of gram-negative bacteria demonstrate numerous immunomodulating properties and are involved in the virulence of pathogenic strains. Because Escherichia coli OmpF is the best-characterized porin in terms of structural and functional characteristics, in vitro B-cell and T-cell responses to this porin in six different strains of mice were analyzed. Mice were immunized with purified OmpF trimers or overlapping synthetic polypeptides (20-mers) spanning the entire 340-amino-acid sequence of the OmpF monomer. T-cell proliferative responses and immunoglobulin G antibody responses to native OmpF and the peptide analogues were determined. For each strain, patterns of T-cell proliferation were similar regardless of whether native OmpF or synthetic peptides were inoculated, although all strains recognized one or more cryptic determinants. Mice exhibited several haplotype-specific responses, but genetically permissive epitopes were also identified. Four peptides (75-94, 265-284, 295-314, and 305-324) elicited strong T-cell proliferative responses from all strains of mice when mice were presensitized with native OmpF or a homologous peptide. In general, 10 or fewer peptides were recognized by sera from mice immunized with native OmpF or synthetic peptides, and most sera from peptide-immunized mice reacted poorly with the native protein. Four peptides spanning amino acids 45 to 64, 95 to 114, 115 to 134, and 275 to 294 were recognized by sera from all strains immunized with native OmpF but not by sera from peptide-immunized mice. Peptides 245-264 and 305-324 were universally recognized by sera from peptide-immunized mice, but these sera reacted weakly or were negative when tested against the native protein. Based on the pattern of cytokine secretion by proliferating T cells, immunization with native OmpF polarizes T helper cells toward development of a TH1 response. T-cell and B-cell responses have been investigated based on the assumption that differences in epitope specificity could influence protective or pathologic host reactions. Because of the high level of structural homology of OmpF to porins isolated from other enteric pathogens, the identification of T- and B-cell-stimulatory determinants of E. coli OmpF may have broader application.</div>
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