Roles of influenza virus infectivity and glycosylation of viral antigen for recognition of target cells by cytolytic T Lymphocytes
Identifieur interne : 002754 ( Main/Exploration ); précédent : 002753; suivant : 002755Roles of influenza virus infectivity and glycosylation of viral antigen for recognition of target cells by cytolytic T Lymphocytes
Auteurs : H. Ertl [Australie] ; G. L. Ada [Australie]Source :
- 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.
- Teeft :
- Aijap virus, Animals, Ascitic fluid, Assay, Binding Sites, Antibody, Binding experiments, Carbohydrate Metabolism, Cell lysis, Cell membrane, Cell samples, Cell surface, Cells radioactivity, Cold competitors, Cytolytic, Cytotoxic, Cytotoxic assays, Cytotoxicity, Immunologic, Dead cells, Different concentrations, Effector, Effector cells, Ertl, Female, Gene products, Glycosylation, Haemagglutinin, Heterologous effector cells, Immunity, Cellular, Immunol, Infectious virus, Influenza, Influenza virus, Influenza virus antigens, Influenza virus strains, John curtin school, Lowest concentration, Lymphocyte, Lysis, Male, Mastocytoma cells, Matrix protein, Medical research, Mice, Mice, Inbred BALB C, Monoclonal antibody, Monospecific antibody, Normal mouse serum, Ps1s cells, Psis cells, Reagent, Second experiment, Secondary effector, Sendai virus, Sheep, Sicr release, Specific lysis, Spleen cells, Such cells, Susceptibility, Target cell, Target cells, Total amount, Tunicamycin, Tunicamycin treatment, Uninfected cells, Viral, Viral antigen, Viral antigens, Viral infectivity, Virus.
Abstract
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 though 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.
Url:
DOI: 10.1016/S0171-2985(81)80073-3
Affiliations:
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Le document en format XML
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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="Teeft" xml:lang="en"><term>Aijap virus</term><term>Animals</term><term>Ascitic fluid</term><term>Assay</term><term>Binding Sites, Antibody</term><term>Binding experiments</term><term>Carbohydrate Metabolism</term><term>Cell lysis</term><term>Cell membrane</term><term>Cell samples</term><term>Cell surface</term><term>Cells radioactivity</term><term>Cold competitors</term><term>Cytolytic</term><term>Cytotoxic</term><term>Cytotoxic assays</term><term>Cytotoxicity, Immunologic</term><term>Dead cells</term><term>Different concentrations</term><term>Effector</term><term>Effector cells</term><term>Ertl</term><term>Female</term><term>Gene products</term><term>Glycosylation</term><term>Haemagglutinin</term><term>Heterologous effector cells</term><term>Immunity, Cellular</term><term>Immunol</term><term>Infectious virus</term><term>Influenza</term><term>Influenza virus</term><term>Influenza virus antigens</term><term>Influenza virus strains</term><term>John curtin school</term><term>Lowest concentration</term><term>Lymphocyte</term><term>Lysis</term><term>Male</term><term>Mastocytoma cells</term><term>Matrix protein</term><term>Medical research</term><term>Mice</term><term>Mice, Inbred BALB C</term><term>Monoclonal antibody</term><term>Monospecific antibody</term><term>Normal mouse serum</term><term>Ps1s cells</term><term>Psis cells</term><term>Reagent</term><term>Second experiment</term><term>Secondary effector</term><term>Sendai virus</term><term>Sheep</term><term>Sicr release</term><term>Specific lysis</term><term>Spleen cells</term><term>Such cells</term><term>Susceptibility</term><term>Target cell</term><term>Target cells</term><term>Total amount</term><term>Tunicamycin</term><term>Tunicamycin treatment</term><term>Uninfected cells</term><term>Viral</term><term>Viral antigen</term><term>Viral antigens</term><term>Viral infectivity</term><term>Virus</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><langUsage><language ident="en">en</language></langUsage></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">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 though 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><affiliations><list><country><li>Australie</li></country></list><tree><country name="Australie"><noRegion><name sortKey="Ertl, H" sort="Ertl, H" uniqKey="Ertl H" first="H." last="Ertl">H. Ertl</name></noRegion><name sortKey="Ada, G L" sort="Ada, G L" uniqKey="Ada G" first="G. L." last="Ada">G. L. Ada</name><name sortKey="Ada, G L" sort="Ada, G L" uniqKey="Ada G" first="G. L." last="Ada">G. L. Ada</name></country></tree></affiliations></record>Pour manipuler ce document sous Unix (Dilib)
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