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Induction and Suppression of an Autoimmune Disease by Oligomerized T Cell Epitopes

Identifieur interne : 000046 ( Ncbi/Merge ); précédent : 000045; suivant : 000047

Induction and Suppression of an Autoimmune Disease by Oligomerized T Cell Epitopes

Auteurs : Kirsten Falk [États-Unis] ; Olaf Rötzschke [États-Unis] ; Laura Santambrogio [États-Unis] ; Martin E. Dorf [États-Unis] ; Celia Brosnan [États-Unis] ; Jack L. Strominger [États-Unis]

Source :

RBID : PMC:2195838

Descripteurs français

English descriptors

Abstract

T cell epitope peptides derived from proteolipid protein (PLP139–151) or myelin basic protein (MBP86–100) induce experimental autoimmune encephalomyelitis (EAE) in “susceptible” strains of mice (e.g., SJL/J). In this study, we show that the encephalitogenic effect of these epitopes when injected subcutaneously in complete Freund's adjuvant was significantly enhanced if administered to the animal in a multimerized form as a T cell epitope oligomer (i.e., as multiple repeats of the peptide epitope, such as 16-mers). Oligomer-treated SJL/J mice developed EAE faster and showed a more severe progression of the disease than animals treated with peptide alone. In addition, haplotype-matched B10.S mice, “resistant” to EAE induction by peptide, on injection of 16-mers developed a severe form of EAE. Even more striking, however, was the dramatic suppression of incidence and severity of the disease, seen after single intravenous injections of only 50 μg of the PLP139–151 16-mer, administered to SJL/J mice 7 d after the induction of the disease. Although relapse occurred at about day 45, an additional injection several days before that maintained the suppression. Importantly, the specific suppressive effect of oligomer treatment was also evident if EAE was induced with spinal cord homogenate instead of the single peptide antigen. By contrast, the PLP139–151 peptide accelerated rather than retarded the progression of disease.


Url:
PubMed: 10684863
PubMed Central: 2195838

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PMC:2195838

Le document en format XML

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<div type="abstract" xml:lang="en">
<p>T cell epitope peptides derived from proteolipid protein (PLP139–151) or myelin basic protein (MBP86–100) induce experimental autoimmune encephalomyelitis (EAE) in “susceptible” strains of mice (e.g., SJL/J). In this study, we show that the encephalitogenic effect of these epitopes when injected subcutaneously in complete Freund's adjuvant was significantly enhanced if administered to the animal in a multimerized form as a T cell epitope oligomer (i.e., as multiple repeats of the peptide epitope, such as 16-mers). Oligomer-treated SJL/J mice developed EAE faster and showed a more severe progression of the disease than animals treated with peptide alone. In addition, haplotype-matched B10.S mice, “resistant” to EAE induction by peptide, on injection of 16-mers developed a severe form of EAE. Even more striking, however, was the dramatic suppression of incidence and severity of the disease, seen after single intravenous injections of only 50 μg of the PLP139–151 16-mer, administered to SJL/J mice 7 d after the induction of the disease. Although relapse occurred at about day 45, an additional injection several days before that maintained the suppression. Importantly, the specific suppressive effect of oligomer treatment was also evident if EAE was induced with spinal cord homogenate instead of the single peptide antigen. By contrast, the PLP139–151 peptide accelerated rather than retarded the progression of disease.</p>
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<name sortKey="Santambrogio, Laura" sort="Santambrogio, Laura" uniqKey="Santambrogio L" first="Laura" last="Santambrogio">Laura Santambrogio</name>
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<name sortKey="Dorf, Martin E" sort="Dorf, Martin E" uniqKey="Dorf M" first="Martin E." last="Dorf">Martin E. Dorf</name>
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<name sortKey="Falk, Kirsten" sort="Falk, Kirsten" uniqKey="Falk K" first="Kirsten" last="Falk">Kirsten Falk</name>
<affiliation wicri:level="2">
<nlm:aff id="a">From the Department of Molecular and Cellular Biology, Harvard University, Cambridge, Massachusetts 02138</nlm:aff>
<country xml:lang="fr">États-Unis</country>
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<region type="state">Massachusetts</region>
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<author>
<name sortKey="Rotzschke, Olaf" sort="Rotzschke, Olaf" uniqKey="Rotzschke O" first="Olaf" last="Rötzschke">Olaf Rötzschke</name>
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<nlm:aff id="a">From the Department of Molecular and Cellular Biology, Harvard University, Cambridge, Massachusetts 02138</nlm:aff>
<country xml:lang="fr">États-Unis</country>
<placeName>
<region type="state">Massachusetts</region>
</placeName>
<wicri:cityArea>From the Department of Molecular and Cellular Biology, Harvard University, Cambridge</wicri:cityArea>
</affiliation>
</author>
<author>
<name sortKey="Santambrogio, Laura" sort="Santambrogio, Laura" uniqKey="Santambrogio L" first="Laura" last="Santambrogio">Laura Santambrogio</name>
<affiliation wicri:level="2">
<nlm:aff id="b">Department of Cancer Immunology and AIDS, Dana-Farber Cancer Institute, Boston, Massachusetts 02115</nlm:aff>
<country xml:lang="fr">États-Unis</country>
<placeName>
<region type="state">Massachusetts</region>
</placeName>
<wicri:cityArea>Department of Cancer Immunology and AIDS, Dana-Farber Cancer Institute, Boston</wicri:cityArea>
</affiliation>
</author>
<author>
<name sortKey="Dorf, Martin E" sort="Dorf, Martin E" uniqKey="Dorf M" first="Martin E." last="Dorf">Martin E. Dorf</name>
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<nlm:aff id="c">Department of Pathology, Harvard Medical School, Boston, Massachusetts 02115</nlm:aff>
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<region type="state">Massachusetts</region>
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<wicri:cityArea>Department of Pathology, Harvard Medical School, Boston</wicri:cityArea>
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</author>
<author>
<name sortKey="Brosnan, Celia" sort="Brosnan, Celia" uniqKey="Brosnan C" first="Celia" last="Brosnan">Celia Brosnan</name>
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<nlm:aff id="d">Department of Pathology, Albert Einstein College of Medicine, Bronx, New York 10461</nlm:aff>
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<placeName>
<region type="state">État de New York</region>
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<wicri:cityArea>Department of Pathology, Albert Einstein College of Medicine, Bronx</wicri:cityArea>
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</author>
<author>
<name sortKey="Strominger, Jack L" sort="Strominger, Jack L" uniqKey="Strominger J" first="Jack L." last="Strominger">Jack L. Strominger</name>
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<nlm:aff id="a">From the Department of Molecular and Cellular Biology, Harvard University, Cambridge, Massachusetts 02138</nlm:aff>
<country xml:lang="fr">États-Unis</country>
<placeName>
<region type="state">Massachusetts</region>
</placeName>
<wicri:cityArea>From the Department of Molecular and Cellular Biology, Harvard University, Cambridge</wicri:cityArea>
</affiliation>
<affiliation wicri:level="2">
<nlm:aff id="b">Department of Cancer Immunology and AIDS, Dana-Farber Cancer Institute, Boston, Massachusetts 02115</nlm:aff>
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<region type="state">Massachusetts</region>
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<wicri:cityArea>Department of Cancer Immunology and AIDS, Dana-Farber Cancer Institute, Boston</wicri:cityArea>
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<series>
<title level="j">The Journal of Experimental Medicine</title>
<idno type="ISSN">0022-1007</idno>
<idno type="eISSN">1540-9538</idno>
<imprint>
<date when="2000">2000</date>
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<div type="abstract" xml:lang="en">
<p>T cell epitope peptides derived from proteolipid protein (PLP139–151) or myelin basic protein (MBP86–100) induce experimental autoimmune encephalomyelitis (EAE) in “susceptible” strains of mice (e.g., SJL/J). In this study, we show that the encephalitogenic effect of these epitopes when injected subcutaneously in complete Freund's adjuvant was significantly enhanced if administered to the animal in a multimerized form as a T cell epitope oligomer (i.e., as multiple repeats of the peptide epitope, such as 16-mers). Oligomer-treated SJL/J mice developed EAE faster and showed a more severe progression of the disease than animals treated with peptide alone. In addition, haplotype-matched B10.S mice, “resistant” to EAE induction by peptide, on injection of 16-mers developed a severe form of EAE. Even more striking, however, was the dramatic suppression of incidence and severity of the disease, seen after single intravenous injections of only 50 μg of the PLP139–151 16-mer, administered to SJL/J mice 7 d after the induction of the disease. Although relapse occurred at about day 45, an additional injection several days before that maintained the suppression. Importantly, the specific suppressive effect of oligomer treatment was also evident if EAE was induced with spinal cord homogenate instead of the single peptide antigen. By contrast, the PLP139–151 peptide accelerated rather than retarded the progression of disease.</p>
</div>
</front>
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<profileDesc>
<textClass>
<keywords scheme="KwdEn" xml:lang="en">
<term>Animals</term>
<term>Encephalomyelitis, Autoimmune, Experimental (immunology)</term>
<term>Encephalomyelitis, Autoimmune, Experimental (pathology)</term>
<term>Encephalomyelitis, Autoimmune, Experimental (prevention & control)</term>
<term>Epitopes (immunology)</term>
<term>Epitopes (pharmacology)</term>
<term>Freund's Adjuvant</term>
<term>Immunosuppressive Agents (pharmacology)</term>
<term>Lymphocyte Activation</term>
<term>Mice</term>
<term>Mice, Inbred AKR</term>
<term>Mice, Inbred BALB C</term>
<term>Mice, Inbred Strains</term>
<term>Myelin Basic Protein (genetics)</term>
<term>Myelin Basic Protein (immunology)</term>
<term>Myelin Basic Protein (pharmacology)</term>
<term>Myelin Proteolipid Protein (genetics)</term>
<term>Myelin Proteolipid Protein (immunology)</term>
<term>Myelin Proteolipid Protein (pharmacology)</term>
<term>Species Specificity</term>
<term>T-Lymphocytes (immunology)</term>
<term>T-Lymphocytes (pathology)</term>
<term>Time Factors</term>
</keywords>
<keywords scheme="KwdFr" xml:lang="fr">
<term>Activation des lymphocytes</term>
<term>Adjuvant Freund</term>
<term>Animaux</term>
<term>Encéphalomyélite auto-immune expérimentale ()</term>
<term>Encéphalomyélite auto-immune expérimentale (anatomopathologie)</term>
<term>Encéphalomyélite auto-immune expérimentale (immunologie)</term>
<term>Facteurs temps</term>
<term>Immunosuppresseurs (pharmacologie)</term>
<term>Lignées consanguines de souris</term>
<term>Lymphocytes T (anatomopathologie)</term>
<term>Lymphocytes T (immunologie)</term>
<term>Protéine basique de la myéline (génétique)</term>
<term>Protéine basique de la myéline (immunologie)</term>
<term>Protéine basique de la myéline (pharmacologie)</term>
<term>Protéine protéolipidique myéline (génétique)</term>
<term>Protéine protéolipidique myéline (immunologie)</term>
<term>Protéine protéolipidique myéline (pharmacologie)</term>
<term>Souris</term>
<term>Souris de lignée AKR</term>
<term>Souris de lignée BALB C</term>
<term>Spécificité d'espèce</term>
<term>Épitopes (immunologie)</term>
<term>Épitopes (pharmacologie)</term>
</keywords>
<keywords scheme="MESH" type="chemical" qualifier="genetics" xml:lang="en">
<term>Myelin Basic Protein</term>
<term>Myelin Proteolipid Protein</term>
</keywords>
<keywords scheme="MESH" type="chemical" qualifier="immunology" xml:lang="en">
<term>Epitopes</term>
<term>Myelin Basic Protein</term>
<term>Myelin Proteolipid Protein</term>
</keywords>
<keywords scheme="MESH" qualifier="anatomopathologie" xml:lang="fr">
<term>Encéphalomyélite auto-immune expérimentale</term>
<term>Lymphocytes T</term>
</keywords>
<keywords scheme="MESH" qualifier="génétique" xml:lang="fr">
<term>Protéine basique de la myéline</term>
<term>Protéine protéolipidique myéline</term>
</keywords>
<keywords scheme="MESH" qualifier="immunologie" xml:lang="fr">
<term>Encéphalomyélite auto-immune expérimentale</term>
<term>Lymphocytes T</term>
<term>Protéine basique de la myéline</term>
<term>Protéine protéolipidique myéline</term>
<term>Épitopes</term>
</keywords>
<keywords scheme="MESH" qualifier="immunology" xml:lang="en">
<term>Encephalomyelitis, Autoimmune, Experimental</term>
<term>T-Lymphocytes</term>
</keywords>
<keywords scheme="MESH" qualifier="pathology" xml:lang="en">
<term>Encephalomyelitis, Autoimmune, Experimental</term>
<term>T-Lymphocytes</term>
</keywords>
<keywords scheme="MESH" qualifier="pharmacologie" xml:lang="fr">
<term>Immunosuppresseurs</term>
<term>Protéine basique de la myéline</term>
<term>Protéine protéolipidique myéline</term>
<term>Épitopes</term>
</keywords>
<keywords scheme="MESH" type="chemical" qualifier="pharmacology" xml:lang="en">
<term>Epitopes</term>
<term>Immunosuppressive Agents</term>
<term>Myelin Basic Protein</term>
<term>Myelin Proteolipid Protein</term>
</keywords>
<keywords scheme="MESH" qualifier="prevention & control" xml:lang="en">
<term>Encephalomyelitis, Autoimmune, Experimental</term>
</keywords>
<keywords scheme="MESH" xml:lang="en">
<term>Animals</term>
<term>Freund's Adjuvant</term>
<term>Lymphocyte Activation</term>
<term>Mice</term>
<term>Mice, Inbred AKR</term>
<term>Mice, Inbred BALB C</term>
<term>Mice, Inbred Strains</term>
<term>Species Specificity</term>
<term>Time Factors</term>
</keywords>
<keywords scheme="MESH" xml:lang="fr">
<term>Activation des lymphocytes</term>
<term>Adjuvant Freund</term>
<term>Animaux</term>
<term>Encéphalomyélite auto-immune expérimentale</term>
<term>Facteurs temps</term>
<term>Lignées consanguines de souris</term>
<term>Souris</term>
<term>Souris de lignée AKR</term>
<term>Souris de lignée BALB C</term>
<term>Spécificité d'espèce</term>
</keywords>
</textClass>
</profileDesc>
</teiHeader>
<front>
<div type="abstract" xml:lang="en">T cell epitope peptides derived from proteolipid protein (PLP139-151) or myelin basic protein (MBP86-100) induce experimental autoimmune encephalomyelitis (EAE) in "susceptible" strains of mice (e.g., SJL/J). In this study, we show that the encephalitogenic effect of these epitopes when injected subcutaneously in complete Freund's adjuvant was significantly enhanced if administered to the animal in a multimerized form as a T cell epitope oligomer (i.e., as multiple repeats of the peptide epitope, such as 16-mers). Oligomer-treated SJL/J mice developed EAE faster and showed a more severe progression of the disease than animals treated with peptide alone. In addition, haplotype-matched B10.S mice, "resistant" to EAE induction by peptide, on injection of 16-mers developed a severe form of EAE. Even more striking, however, was the dramatic suppression of incidence and severity of the disease, seen after single intravenous injections of only 50 microg of the PLP139-151 16-mer, administered to SJL/J mice 7 d after the induction of the disease. Although relapse occurred at about day 45, an additional injection several days before that maintained the suppression. Importantly, the specific suppressive effect of oligomer treatment was also evident if EAE was induced with spinal cord homogenate instead of the single peptide antigen. By contrast, the PLP139-151 peptide accelerated rather than retarded the progression of disease.</div>
</front>
</TEI>
</pubmed>
</double>
</record>

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