Roles of influenza virus infectivity and glycosylation of viral antigen for recognition of target cells by cytolytic T lymphocytes.
Identifieur interne : 000583 ( PubMed/Curation ); précédent : 000582; suivant : 000584Roles of influenza virus infectivity and glycosylation of viral antigen for recognition of target cells by cytolytic T lymphocytes.
Auteurs : H. Ertl ; G L AdaSource :
- Immunobiology [ 0171-2985 ] ; 1981.
Descripteurs français
- KwdFr :
- Animaux, Antigènes H-2 (immunologie), Antigènes viraux (immunologie), Capping (immunologie) (), Cytotoxicité immunologique, Femelle, Hémagglutinines (immunologie), Immunité cellulaire, Infections à Orthomyxoviridae (immunologie), Lymphocytes T (immunologie), Mâle, Métabolisme des glucides, Ovis, Sites de fixation des anticorps, Souris, Souris de lignée BALB C, Tunicamycine (pharmacologie), Virus de la grippe A (immunologie).
- MESH :
- immunologie : Antigènes H-2, Antigènes viraux, Hémagglutinines, Infections à Orthomyxoviridae, Lymphocytes T, Virus de la grippe A.
- pharmacologie : Tunicamycine.
- Animaux, Capping (immunologie), Cytotoxicité immunologique, Femelle, Immunité cellulaire, Mâle, Métabolisme des glucides, Ovis, Sites de fixation des anticorps, Souris, Souris de lignée BALB C.
English descriptors
- KwdEn :
- Animals, Antigens, Viral (immunology), Binding Sites, Antibody, Carbohydrate Metabolism, Cytotoxicity, Immunologic, Female, H-2 Antigens (immunology), Hemagglutinins (immunology), Immunity, Cellular, Immunologic Capping (drug effects), Influenza A virus (immunology), Male, Mice, Mice, Inbred BALB C, Orthomyxoviridae Infections (immunology), Sheep, T-Lymphocytes (immunology), Tunicamycin (pharmacology).
- MESH :
- chemical , immunology : Antigens, Viral, H-2 Antigens, Hemagglutinins.
- drug effects : Immunologic Capping.
- immunology : Influenza A virus, Orthomyxoviridae Infections, T-Lymphocytes.
- chemical , pharmacology : Tunicamycin.
- Animals, Binding Sites, Antibody, Carbohydrate Metabolism, Cytotoxicity, Immunologic, Female, Immunity, Cellular, Male, Mice, Mice, Inbred BALB C, Sheep.
Abstract
The influenza virus strains A/JAP (H2N2) and the recombinant strain A/JAP/BEL (H2N1) were tested before and after UV-light inactivation for their ability to sensitize target cells for cytotoxic T-cell lysis (CTL). Infectious preparations were efficient sensitizers for both specific and cross-reactive CTL, exposure of the cells to even low doses of virus resulting in almost maximum susceptibility. When inactivated, however, A/JAP/BEL was about 10 times more efficient than A/JAP at sensitizing the cells for specific CTL; neither sensitized the cells for cross-reactive CTL. Thus factors other than or in addition to a cleaved haemagglutinin (HA) molecule are important in the fusion of the virus with the cell membrane. Target cells which were infected with virus and exposed to different concentrations of tunicamycin, which inhibits glycosylation, became susceptible to CTL by both specific and cross-reactive effector cells through to a lesser extent than controls. Infected cells showed both strong haemadsorption and cocapping of the HA with K, D gene products. Both of these properties were greatly diminished in the presence of even low concentrations of tunicamycin. Analysis of binding studies using labelled monoclonal anti-HA IgG showed that, in the presence of tunicamycin, the total amount of HA expressed at the cell surface was not reduced, but there was an increase in the dissociation constant of the reaction between expressed HA and antibody. This latter finding was thought to reflect a conformational change in the HA antigen, which might be the reason for the reduced susceptibility to CTL.
DOI: 10.1016/S0171-2985(81)80073-3
PubMed: 6971249
Links toward previous steps (curation, corpus...)
- to stream PubMed, to step Corpus: Pour aller vers cette notice dans l'étape Curation :000583
Links to Exploration step
pubmed:6971249Le document en format XML
<record><TEI><teiHeader><fileDesc><titleStmt><title xml:lang="en">Roles of influenza virus infectivity and glycosylation of viral antigen for recognition of target cells by cytolytic T lymphocytes.</title><author><name sortKey="Ertl, H" sort="Ertl, H" uniqKey="Ertl H" first="H" last="Ertl">H. Ertl</name></author><author><name sortKey="Ada, G L" sort="Ada, G L" uniqKey="Ada G" first="G L" last="Ada">G L Ada</name></author></titleStmt><publicationStmt><idno type="wicri:source">PubMed</idno><date when="1981">1981</date><idno type="RBID">pubmed:6971249</idno><idno type="pmid">6971249</idno><idno type="doi">10.1016/S0171-2985(81)80073-3</idno><idno type="wicri:Area/PubMed/Corpus">000583</idno><idno type="wicri:explorRef" wicri:stream="PubMed" wicri:step="Corpus" wicri:corpus="PubMed">000583</idno><idno type="wicri:Area/PubMed/Curation">000583</idno><idno type="wicri:explorRef" wicri:stream="PubMed" wicri:step="Curation">000583</idno></publicationStmt><sourceDesc><biblStruct><analytic><title xml:lang="en">Roles of influenza virus infectivity and glycosylation of viral antigen for recognition of target cells by cytolytic T lymphocytes.</title><author><name sortKey="Ertl, H" sort="Ertl, H" uniqKey="Ertl H" first="H" last="Ertl">H. Ertl</name></author><author><name sortKey="Ada, G L" sort="Ada, G L" uniqKey="Ada G" first="G L" last="Ada">G L Ada</name></author></analytic><series><title level="j">Immunobiology</title><idno type="ISSN">0171-2985</idno><imprint><date when="1981" type="published">1981</date></imprint></series></biblStruct></sourceDesc></fileDesc><profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>Animals</term><term>Antigens, Viral (immunology)</term><term>Binding Sites, Antibody</term><term>Carbohydrate Metabolism</term><term>Cytotoxicity, Immunologic</term><term>Female</term><term>H-2 Antigens (immunology)</term><term>Hemagglutinins (immunology)</term><term>Immunity, Cellular</term><term>Immunologic Capping (drug effects)</term><term>Influenza A virus (immunology)</term><term>Male</term><term>Mice</term><term>Mice, Inbred BALB C</term><term>Orthomyxoviridae Infections (immunology)</term><term>Sheep</term><term>T-Lymphocytes (immunology)</term><term>Tunicamycin (pharmacology)</term></keywords><keywords scheme="KwdFr" xml:lang="fr"><term>Animaux</term><term>Antigènes H-2 (immunologie)</term><term>Antigènes viraux (immunologie)</term><term>Capping (immunologie) ()</term><term>Cytotoxicité immunologique</term><term>Femelle</term><term>Hémagglutinines (immunologie)</term><term>Immunité cellulaire</term><term>Infections à Orthomyxoviridae (immunologie)</term><term>Lymphocytes T (immunologie)</term><term>Mâle</term><term>Métabolisme des glucides</term><term>Ovis</term><term>Sites de fixation des anticorps</term><term>Souris</term><term>Souris de lignée BALB C</term><term>Tunicamycine (pharmacologie)</term><term>Virus de la grippe A (immunologie)</term></keywords><keywords scheme="MESH" type="chemical" qualifier="immunology" xml:lang="en"><term>Antigens, Viral</term><term>H-2 Antigens</term><term>Hemagglutinins</term></keywords><keywords scheme="MESH" qualifier="drug effects" xml:lang="en"><term>Immunologic Capping</term></keywords><keywords scheme="MESH" qualifier="immunologie" xml:lang="fr"><term>Antigènes H-2</term><term>Antigènes viraux</term><term>Hémagglutinines</term><term>Infections à Orthomyxoviridae</term><term>Lymphocytes T</term><term>Virus de la grippe A</term></keywords><keywords scheme="MESH" qualifier="immunology" xml:lang="en"><term>Influenza A virus</term><term>Orthomyxoviridae Infections</term><term>T-Lymphocytes</term></keywords><keywords scheme="MESH" qualifier="pharmacologie" xml:lang="fr"><term>Tunicamycine</term></keywords><keywords scheme="MESH" type="chemical" qualifier="pharmacology" xml:lang="en"><term>Tunicamycin</term></keywords><keywords scheme="MESH" xml:lang="en"><term>Animals</term><term>Binding Sites, Antibody</term><term>Carbohydrate Metabolism</term><term>Cytotoxicity, Immunologic</term><term>Female</term><term>Immunity, Cellular</term><term>Male</term><term>Mice</term><term>Mice, Inbred BALB C</term><term>Sheep</term></keywords><keywords scheme="MESH" xml:lang="fr"><term>Animaux</term><term>Capping (immunologie)</term><term>Cytotoxicité immunologique</term><term>Femelle</term><term>Immunité cellulaire</term><term>Mâle</term><term>Métabolisme des glucides</term><term>Ovis</term><term>Sites de fixation des anticorps</term><term>Souris</term><term>Souris de lignée BALB C</term></keywords></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">The influenza virus strains A/JAP (H2N2) and the recombinant strain A/JAP/BEL (H2N1) were tested before and after UV-light inactivation for their ability to sensitize target cells for cytotoxic T-cell lysis (CTL). Infectious preparations were efficient sensitizers for both specific and cross-reactive CTL, exposure of the cells to even low doses of virus resulting in almost maximum susceptibility. When inactivated, however, A/JAP/BEL was about 10 times more efficient than A/JAP at sensitizing the cells for specific CTL; neither sensitized the cells for cross-reactive CTL. Thus factors other than or in addition to a cleaved haemagglutinin (HA) molecule are important in the fusion of the virus with the cell membrane. Target cells which were infected with virus and exposed to different concentrations of tunicamycin, which inhibits glycosylation, became susceptible to CTL by both specific and cross-reactive effector cells through to a lesser extent than controls. Infected cells showed both strong haemadsorption and cocapping of the HA with K, D gene products. Both of these properties were greatly diminished in the presence of even low concentrations of tunicamycin. Analysis of binding studies using labelled monoclonal anti-HA IgG showed that, in the presence of tunicamycin, the total amount of HA expressed at the cell surface was not reduced, but there was an increase in the dissociation constant of the reaction between expressed HA and antibody. This latter finding was thought to reflect a conformational change in the HA antigen, which might be the reason for the reduced susceptibility to CTL.</div></front></TEI><pubmed><MedlineCitation Status="MEDLINE" Owner="NLM"><PMID Version="1">6971249</PMID><DateCompleted><Year>1981</Year><Month>06</Month><Day>13</Day></DateCompleted><DateRevised><Year>2011</Year><Month>11</Month><Day>17</Day></DateRevised><Article PubModel="Print"><Journal><ISSN IssnType="Print">0171-2985</ISSN><JournalIssue CitedMedium="Print"><Volume>158</Volume><Issue>3</Issue><PubDate><Year>1981</Year></PubDate></JournalIssue><Title>Immunobiology</Title><ISOAbbreviation>Immunobiology</ISOAbbreviation></Journal><ArticleTitle>Roles of influenza virus infectivity and glycosylation of viral antigen for recognition of target cells by cytolytic T lymphocytes.</ArticleTitle><Pagination><MedlinePgn>239-53</MedlinePgn></Pagination><Abstract><AbstractText>The influenza virus strains A/JAP (H2N2) and the recombinant strain A/JAP/BEL (H2N1) were tested before and after UV-light inactivation for their ability to sensitize target cells for cytotoxic T-cell lysis (CTL). Infectious preparations were efficient sensitizers for both specific and cross-reactive CTL, exposure of the cells to even low doses of virus resulting in almost maximum susceptibility. When inactivated, however, A/JAP/BEL was about 10 times more efficient than A/JAP at sensitizing the cells for specific CTL; neither sensitized the cells for cross-reactive CTL. Thus factors other than or in addition to a cleaved haemagglutinin (HA) molecule are important in the fusion of the virus with the cell membrane. Target cells which were infected with virus and exposed to different concentrations of tunicamycin, which inhibits glycosylation, became susceptible to CTL by both specific and cross-reactive effector cells through to a lesser extent than controls. Infected cells showed both strong haemadsorption and cocapping of the HA with K, D gene products. Both of these properties were greatly diminished in the presence of even low concentrations of tunicamycin. Analysis of binding studies using labelled monoclonal anti-HA IgG showed that, in the presence of tunicamycin, the total amount of HA expressed at the cell surface was not reduced, but there was an increase in the dissociation constant of the reaction between expressed HA and antibody. This latter finding was thought to reflect a conformational change in the HA antigen, which might be the reason for the reduced susceptibility to CTL.</AbstractText></Abstract><AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Ertl</LastName><ForeName>H</ForeName><Initials>H</Initials></Author><Author ValidYN="Y"><LastName>Ada</LastName><ForeName>G L</ForeName><Initials>GL</Initials></Author></AuthorList><Language>eng</Language><PublicationTypeList><PublicationType UI="D016428">Journal Article</PublicationType></PublicationTypeList></Article><MedlineJournalInfo><Country>Netherlands</Country><MedlineTA>Immunobiology</MedlineTA><NlmUniqueID>8002742</NlmUniqueID><ISSNLinking>0171-2985</ISSNLinking></MedlineJournalInfo><ChemicalList><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D000956">Antigens, Viral</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D006183">H-2 Antigens</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D006388">Hemagglutinins</NameOfSubstance></Chemical><Chemical><RegistryNumber>11089-65-9</RegistryNumber><NameOfSubstance UI="D014415">Tunicamycin</NameOfSubstance></Chemical></ChemicalList><CitationSubset>IM</CitationSubset><MeshHeadingList><MeshHeading><DescriptorName UI="D000818" MajorTopicYN="N">Animals</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D000956" MajorTopicYN="N">Antigens, Viral</DescriptorName><QualifierName UI="Q000276" MajorTopicYN="Y">immunology</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D001666" MajorTopicYN="N">Binding Sites, Antibody</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D050260" MajorTopicYN="Y">Carbohydrate Metabolism</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D003602" MajorTopicYN="Y">Cytotoxicity, Immunologic</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D005260" MajorTopicYN="N">Female</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D006183" MajorTopicYN="N">H-2 Antigens</DescriptorName><QualifierName UI="Q000276" MajorTopicYN="N">immunology</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D006388" MajorTopicYN="N">Hemagglutinins</DescriptorName><QualifierName UI="Q000276" MajorTopicYN="N">immunology</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D007111" MajorTopicYN="N">Immunity, Cellular</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D007152" MajorTopicYN="N">Immunologic Capping</DescriptorName><QualifierName UI="Q000187" MajorTopicYN="N">drug effects</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D009980" MajorTopicYN="N">Influenza A virus</DescriptorName><QualifierName UI="Q000276" MajorTopicYN="N">immunology</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D008297" MajorTopicYN="N">Male</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D051379" MajorTopicYN="N">Mice</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D008807" MajorTopicYN="N">Mice, Inbred BALB C</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D009976" MajorTopicYN="N">Orthomyxoviridae Infections</DescriptorName><QualifierName UI="Q000276" MajorTopicYN="Y">immunology</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D012756" MajorTopicYN="N">Sheep</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D013601" MajorTopicYN="N">T-Lymphocytes</DescriptorName><QualifierName UI="Q000276" MajorTopicYN="N">immunology</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D014415" MajorTopicYN="N">Tunicamycin</DescriptorName><QualifierName UI="Q000494" MajorTopicYN="N">pharmacology</QualifierName></MeshHeading></MeshHeadingList></MedlineCitation><PubmedData><History><PubMedPubDate PubStatus="pubmed"><Year>1981</Year><Month>1</Month><Day>1</Day></PubMedPubDate><PubMedPubDate PubStatus="medline"><Year>1981</Year><Month>1</Month><Day>1</Day><Hour>0</Hour><Minute>1</Minute></PubMedPubDate><PubMedPubDate PubStatus="entrez"><Year>1981</Year><Month>1</Month><Day>1</Day><Hour>0</Hour><Minute>0</Minute></PubMedPubDate></History><PublicationStatus>ppublish</PublicationStatus><ArticleIdList><ArticleId IdType="pubmed">6971249</ArticleId><ArticleId IdType="pii">S0171-2985(81)80073-3</ArticleId><ArticleId IdType="doi">10.1016/S0171-2985(81)80073-3</ArticleId></ArticleIdList></PubmedData></pubmed></record>Pour manipuler ce document sous Unix (Dilib)
EXPLOR_STEP=$WICRI_ROOT/Sante/explor/H2N2V1/Data/PubMed/Curation
HfdSelect -h $EXPLOR_STEP/biblio.hfd -nk 000583 | SxmlIndent | more
Ou
HfdSelect -h $EXPLOR_AREA/Data/PubMed/Curation/biblio.hfd -nk 000583 | SxmlIndent | more
Pour mettre un lien sur cette page dans le réseau Wicri
{{Explor lien
|wiki= Sante
|area= H2N2V1
|flux= PubMed
|étape= Curation
|type= RBID
|clé= pubmed:6971249
|texte= Roles of influenza virus infectivity and glycosylation of viral antigen for recognition of target cells by cytolytic T lymphocytes.
}}
Pour générer des pages wiki
HfdIndexSelect -h $EXPLOR_AREA/Data/PubMed/Curation/RBID.i -Sk "pubmed:6971249" \
| HfdSelect -Kh $EXPLOR_AREA/Data/PubMed/Curation/biblio.hfd \
| NlmPubMed2Wicri -a H2N2V1
| This area was generated with Dilib version V0.6.33. |  |