Influenza virus changes cell-surface glycoproteins including major histocompatibility complex determinants on lymphocytes
Identifieur interne : 002155 ( Main/Exploration ); précédent : 002154; suivant : 002156Influenza virus changes cell-surface glycoproteins including major histocompatibility complex determinants on lymphocytes
Auteurs : Francien T. M. Rotteveel [Pays-Bas] ; Jacques J. Neefjes [Pays-Bas] ; Hidde L. Ploegh [Pays-Bas] ; Cornelius J. Lucas [Pays-Bas]Source :
- Human Immunology [ 0198-8859 ] ; 1989.
English descriptors
- Teeft :
- Antigen, Antigen expression, Biochemical analysis, Cell surface, Central laboratory, Control cells, Determinant, Final concentration, Fluorescence intensity, Fluorescence intensity figure, Glycoprotein, Histocompatibility, Human immunol, Immune, Immunol, Infection, Influenza, Influenza changes glycoproteins, Influenza virus, Influenza virus infection, Interferon, Lymphoblast, Lymphocyte, Major histocompatibility, Moab, Moab binding, Moabs, Monoclonal, Monoclonal antibodies, Neuraminidase, Neuraminidase treatment, Noninfected, Okt3, Other antibodies, Perfringens neuraminidase, Positive cells, Proc natl acad, Region products, Rotteveel, Sialic, Sialic acids, Target cells, Viral, Viral infection, Viral neuraminidase, Virus, Virus infection.
Abstract
Abstract: The effect of influenza virus infection on the expression of major histocompatibility complex (MHC) antigens was investigated. Infection with influenza virus resulted in an increase of the binding of anti-MHC class I and class II antibodies to resting T cells. The binding of anti-MHC class II antibodies to activated T cells was increased approximately threefold. The binding of anti-MHC class I and class II antibodies to Epstein-Barr virus — transformed B cells appeared unaffected after influenza virus infection. Recombinant human interferon-α and/or-γ added to T cells did not enhance the binding of anti-MHC antibodies. Biochemical analysis revealed no increase in the amount of class I and class II antigens as a consequence of viral infection, but a marked decrease in sialic acid content was found, most probably caused by the viral neuraminidase. Pulse-chase experiments suggest that the viral neuraminidase can catalyze the removal of sialic acids both en route to and at the cell surface. The absence of sialic acid residues can explain the increased binding of anti-MHC antibodies, because neuraminidase (clostridium perfringens) treatment of T and Epstein-Barr virus-transformed B cells resulted in a shift in both isoelectric point and antibody binding similar to that observed after influenza virus infection.
Url:
DOI: 10.1016/0198-8859(89)90039-6
Affiliations:
Links toward previous steps (curation, corpus...)
- to stream Istex, to step Corpus: 000F58
- to stream Istex, to step Curation: 000F58
- to stream Istex, to step Checkpoint: 000E76
- to stream Main, to step Merge: 002259
- to stream Main, to step Curation: 002155
Le document en format XML
<record><TEI wicri:istexFullTextTei="biblStruct"><teiHeader><fileDesc><titleStmt><title>Influenza virus changes cell-surface glycoproteins including major histocompatibility complex determinants on lymphocytes</title><author><name sortKey="Rotteveel, Francien T M" sort="Rotteveel, Francien T M" uniqKey="Rotteveel F" first="Francien T. M." last="Rotteveel">Francien T. M. Rotteveel</name></author><author><name sortKey="Neefjes, Jacques J" sort="Neefjes, Jacques J" uniqKey="Neefjes J" first="Jacques J." last="Neefjes">Jacques J. Neefjes</name></author><author><name sortKey="Ploegh, Hidde L" sort="Ploegh, Hidde L" uniqKey="Ploegh H" first="Hidde L." last="Ploegh">Hidde L. Ploegh</name></author><author><name sortKey="Lucas, Cornelius J" sort="Lucas, Cornelius J" uniqKey="Lucas C" first="Cornelius J." last="Lucas">Cornelius J. Lucas</name></author></titleStmt><publicationStmt><idno type="wicri:source">ISTEX</idno><idno type="RBID">ISTEX:D36754121A7E41800B73EDDF7F83E7AC9C87BA9B</idno><date when="1989" year="1989">1989</date><idno type="doi">10.1016/0198-8859(89)90039-6</idno><idno type="url">https://api.istex.fr/ark:/67375/6H6-VKK8QGHR-R/fulltext.pdf</idno><idno type="wicri:Area/Istex/Corpus">000F58</idno><idno type="wicri:explorRef" wicri:stream="Istex" wicri:step="Corpus" wicri:corpus="ISTEX">000F58</idno><idno type="wicri:Area/Istex/Curation">000F58</idno><idno type="wicri:Area/Istex/Checkpoint">000E76</idno><idno type="wicri:explorRef" wicri:stream="Istex" wicri:step="Checkpoint">000E76</idno><idno type="wicri:doubleKey">0198-8859:1989:Rotteveel F:influenza:virus:changes</idno><idno type="wicri:Area/Main/Merge">002259</idno><idno type="wicri:Area/Main/Curation">002155</idno><idno type="wicri:Area/Main/Exploration">002155</idno></publicationStmt><sourceDesc><biblStruct><analytic><title level="a">Influenza virus changes cell-surface glycoproteins including major histocompatibility complex determinants on lymphocytes</title><author><name sortKey="Rotteveel, Francien T M" sort="Rotteveel, Francien T M" uniqKey="Rotteveel F" first="Francien T. M." last="Rotteveel">Francien T. M. Rotteveel</name><affiliation wicri:level="4"><country xml:lang="fr">Pays-Bas</country><wicri:regionArea>From the Central Laboratory of the Netherlands Red Cross Transfusion Service and the Laboratory for Experimental and Clinical Immunology, University of Amsterdam</wicri:regionArea><placeName><settlement type="city">Amsterdam</settlement><region>Hollande-Septentrionale</region></placeName><orgName type="university">Université d'Amsterdam</orgName></affiliation></author><author><name sortKey="Neefjes, Jacques J" sort="Neefjes, Jacques J" uniqKey="Neefjes J" first="Jacques J." last="Neefjes">Jacques J. Neefjes</name><affiliation wicri:level="3"><country xml:lang="fr" wicri:curation="lc">Pays-Bas</country><wicri:regionArea>the Netherlands Cancer Institute, Amsterdam</wicri:regionArea><placeName><settlement type="city">Amsterdam</settlement><region nuts="2" type="province">Hollande-Septentrionale</region></placeName></affiliation></author><author><name sortKey="Ploegh, Hidde L" sort="Ploegh, Hidde L" uniqKey="Ploegh H" first="Hidde L." last="Ploegh">Hidde L. Ploegh</name><affiliation wicri:level="3"><country xml:lang="fr" wicri:curation="lc">Pays-Bas</country><wicri:regionArea>the Netherlands Cancer Institute, Amsterdam</wicri:regionArea><placeName><settlement type="city">Amsterdam</settlement><region nuts="2" type="province">Hollande-Septentrionale</region></placeName></affiliation></author><author><name sortKey="Lucas, Cornelius J" sort="Lucas, Cornelius J" uniqKey="Lucas C" first="Cornelius J." last="Lucas">Cornelius J. Lucas</name><affiliation wicri:level="1"><country xml:lang="fr" wicri:curation="lc">Pays-Bas</country><wicri:regionArea>Address reprint requests to Dr. Cornelius J. Lucas, c/o Publication Secretariat, Central Laboratory of the Netherlands Red Cross Blood Transfusion Service, P.O. Box 9406, 1006 AK Amsterdam</wicri:regionArea><wicri:noRegion>1006 AK Amsterdam</wicri:noRegion></affiliation><affiliation wicri:level="4"><country xml:lang="fr">Pays-Bas</country><wicri:regionArea>From the Central Laboratory of the Netherlands Red Cross Transfusion Service and the Laboratory for Experimental and Clinical Immunology, University of Amsterdam</wicri:regionArea><placeName><settlement type="city">Amsterdam</settlement><region>Hollande-Septentrionale</region></placeName><orgName type="university">Université d'Amsterdam</orgName></affiliation></author></analytic><monogr></monogr><series><title level="j">Human Immunology</title><title level="j" type="abbrev">HIM</title><idno type="ISSN">0198-8859</idno><imprint><publisher>ELSEVIER</publisher><date type="published" when="1989">1989</date><biblScope unit="volume">26</biblScope><biblScope unit="issue">3</biblScope><biblScope unit="page" from="199">199</biblScope><biblScope unit="page" to="213">213</biblScope></imprint><idno type="ISSN">0198-8859</idno></series></biblStruct></sourceDesc><seriesStmt><idno type="ISSN">0198-8859</idno></seriesStmt></fileDesc><profileDesc><textClass><keywords scheme="Teeft" xml:lang="en"><term>Antigen</term><term>Antigen expression</term><term>Biochemical analysis</term><term>Cell surface</term><term>Central laboratory</term><term>Control cells</term><term>Determinant</term><term>Final concentration</term><term>Fluorescence intensity</term><term>Fluorescence intensity figure</term><term>Glycoprotein</term><term>Histocompatibility</term><term>Human immunol</term><term>Immune</term><term>Immunol</term><term>Infection</term><term>Influenza</term><term>Influenza changes glycoproteins</term><term>Influenza virus</term><term>Influenza virus infection</term><term>Interferon</term><term>Lymphoblast</term><term>Lymphocyte</term><term>Major histocompatibility</term><term>Moab</term><term>Moab binding</term><term>Moabs</term><term>Monoclonal</term><term>Monoclonal antibodies</term><term>Neuraminidase</term><term>Neuraminidase treatment</term><term>Noninfected</term><term>Okt3</term><term>Other antibodies</term><term>Perfringens neuraminidase</term><term>Positive cells</term><term>Proc natl acad</term><term>Region products</term><term>Rotteveel</term><term>Sialic</term><term>Sialic acids</term><term>Target cells</term><term>Viral</term><term>Viral infection</term><term>Viral neuraminidase</term><term>Virus</term><term>Virus infection</term></keywords></textClass><langUsage><language ident="en">en</language></langUsage></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">Abstract: The effect of influenza virus infection on the expression of major histocompatibility complex (MHC) antigens was investigated. Infection with influenza virus resulted in an increase of the binding of anti-MHC class I and class II antibodies to resting T cells. The binding of anti-MHC class II antibodies to activated T cells was increased approximately threefold. The binding of anti-MHC class I and class II antibodies to Epstein-Barr virus — transformed B cells appeared unaffected after influenza virus infection. Recombinant human interferon-α and/or-γ added to T cells did not enhance the binding of anti-MHC antibodies. Biochemical analysis revealed no increase in the amount of class I and class II antigens as a consequence of viral infection, but a marked decrease in sialic acid content was found, most probably caused by the viral neuraminidase. Pulse-chase experiments suggest that the viral neuraminidase can catalyze the removal of sialic acids both en route to and at the cell surface. The absence of sialic acid residues can explain the increased binding of anti-MHC antibodies, because neuraminidase (clostridium perfringens) treatment of T and Epstein-Barr virus-transformed B cells resulted in a shift in both isoelectric point and antibody binding similar to that observed after influenza virus infection.</div></front></TEI><affiliations><list><country><li>Pays-Bas</li></country><region><li>Hollande-Septentrionale</li></region><settlement><li>Amsterdam</li></settlement><orgName><li>Université d'Amsterdam</li></orgName></list><tree><country name="Pays-Bas"><region name="Hollande-Septentrionale"><name sortKey="Rotteveel, Francien T M" sort="Rotteveel, Francien T M" uniqKey="Rotteveel F" first="Francien T. M." last="Rotteveel">Francien T. M. Rotteveel</name></region><name sortKey="Lucas, Cornelius J" sort="Lucas, Cornelius J" uniqKey="Lucas C" first="Cornelius J." last="Lucas">Cornelius J. Lucas</name><name sortKey="Lucas, Cornelius J" sort="Lucas, Cornelius J" uniqKey="Lucas C" first="Cornelius J." last="Lucas">Cornelius J. Lucas</name><name sortKey="Neefjes, Jacques J" sort="Neefjes, Jacques J" uniqKey="Neefjes J" first="Jacques J." last="Neefjes">Jacques J. Neefjes</name><name sortKey="Ploegh, Hidde L" sort="Ploegh, Hidde L" uniqKey="Ploegh H" first="Hidde L." last="Ploegh">Hidde L. Ploegh</name></country></tree></affiliations></record>Pour manipuler ce document sous Unix (Dilib)
EXPLOR_STEP=$WICRI_ROOT/Sante/explor/H2N2V1/Data/Main/Exploration
HfdSelect -h $EXPLOR_STEP/biblio.hfd -nk 002155 | SxmlIndent | more
Ou
HfdSelect -h $EXPLOR_AREA/Data/Main/Exploration/biblio.hfd -nk 002155 | SxmlIndent | more
Pour mettre un lien sur cette page dans le réseau Wicri
{{Explor lien
|wiki= Sante
|area= H2N2V1
|flux= Main
|étape= Exploration
|type= RBID
|clé= ISTEX:D36754121A7E41800B73EDDF7F83E7AC9C87BA9B
|texte= Influenza virus changes cell-surface glycoproteins including major histocompatibility complex determinants on lymphocytes
}}
| This area was generated with Dilib version V0.6.33. |  |