Recognition of the PB1, neuraminidase, and matrix proteins of influenza virus A/NT/60/68 by cytotoxic T lymphocytes
Identifieur interne : 002147 ( Main/Exploration ); précédent : 002146; suivant : 002148Recognition of the PB1, neuraminidase, and matrix proteins of influenza virus A/NT/60/68 by cytotoxic T lymphocytes
Auteurs : Philip A. Reay [Royaume-Uni, États-Unis] ; Ian M. Jones [Royaume-Uni] ; Frances M. Gotch [Royaume-Uni] ; Andrew J. Mcmichael [Royaume-Uni] ; George G. BrownleeSource :
- Virology [ 0042-6822 ] ; 1989.
English descriptors
- Teeft :
- Amino, Amino acids, Assay, Bennink, Ctls, Cytotoxic, Epitope, Gotch, Haemagglutinin, Human ctls, Influenza, Influenza ctls, Influenza virus, Lymphocyte, Lysed target cells, Lysis, Matrix, Matrix protein, Mcmichael, Minor target antigen, Mouse, Murine, Neuraminidase, Nucleoprotein, Polyclonal, Polyclonal ctls, Reay, Recombinant, Recombinant vaccinia virus, Recombinant vaccinia viruses, Specific lysis, Splenocytes, Subtypes, Syngeneic, Syngeneic target cells, Target antigen, Target antigens, Target cells, Townsend, Uninfected, Vaccinia, Viral, Virus, Yewdell.
Abstract
Abstract: We have investigated the recognition of the PB1, neuraminidase, and matrix (Ml) proteins of influenza virus A/NT/ 60/68 (H3N2 subtype) by secondary in vitro stimulated polyclonal cytotoxic T lymphocyte (CTL) populations. While these three proteins have different functions and cellular locations, they can all be recognized as target antigens. However, the immunogenicity of these proteins for CTLs is under strict genetic control. Thus, PB1 protein is recognized as a cross-reactive target antigen by CTLs raised in CBA (H-2k) but not BALB/c (H-2d) mice. CBA, but not BALB/c mice, also generate a low-level CTL response to the neuraminidase. This latter response was only detectable following in vivo priming of CBA mice with a recombinant vaccinia virus expressing neuraminidase (N2-VACC). The matrix protein, expressed from recombinant vaccinia virus M-VACC, was not recognized as an antigen by CTL generated from either CBA or BALB/c strains of mice. By contrast, human HLA-A2-restricted influenza virus-specific CTLs were shown to recognize this matrix protein as a target antigen. Endogenous expression of as little as 90 amino acids of the matrix protein was sufficient to render target cells susceptible to lysis by such CTLs.
Url:
DOI: 10.1016/0042-6822(89)90439-X
Affiliations:
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Mcmichael</name><affiliation wicri:level="1"><country xml:lang="fr">Royaume-Uni</country><wicri:regionArea>Institute for Molecular Medicine, John Radcliffe Hospital, Oxford OX3 9DU</wicri:regionArea><wicri:noRegion>Oxford OX3 9DU</wicri:noRegion></affiliation></author><author><name sortKey="Brownlee, George G" sort="Brownlee, George G" uniqKey="Brownlee G" first="George G." last="Brownlee">George G. Brownlee</name><affiliation><wicri:noCountry code="no comma">To whom requests for reprints should be addressed.</wicri:noCountry></affiliation></author></analytic><monogr></monogr><series><title level="j">Virology</title><title level="j" type="abbrev">YVIRO</title><idno type="ISSN">0042-6822</idno><imprint><publisher>ELSEVIER</publisher><date type="published" when="1989">1989</date><biblScope unit="volume">170</biblScope><biblScope unit="issue">2</biblScope><biblScope unit="page" from="477">477</biblScope><biblScope unit="page" to="485">485</biblScope></imprint><idno type="ISSN">0042-6822</idno></series></biblStruct></sourceDesc><seriesStmt><idno type="ISSN">0042-6822</idno></seriesStmt></fileDesc><profileDesc><textClass><keywords scheme="Teeft" xml:lang="en"><term>Amino</term><term>Amino acids</term><term>Assay</term><term>Bennink</term><term>Ctls</term><term>Cytotoxic</term><term>Epitope</term><term>Gotch</term><term>Haemagglutinin</term><term>Human ctls</term><term>Influenza</term><term>Influenza ctls</term><term>Influenza virus</term><term>Lymphocyte</term><term>Lysed target cells</term><term>Lysis</term><term>Matrix</term><term>Matrix protein</term><term>Mcmichael</term><term>Minor target antigen</term><term>Mouse</term><term>Murine</term><term>Neuraminidase</term><term>Nucleoprotein</term><term>Polyclonal</term><term>Polyclonal ctls</term><term>Reay</term><term>Recombinant</term><term>Recombinant vaccinia virus</term><term>Recombinant vaccinia viruses</term><term>Specific lysis</term><term>Splenocytes</term><term>Subtypes</term><term>Syngeneic</term><term>Syngeneic target cells</term><term>Target antigen</term><term>Target antigens</term><term>Target cells</term><term>Townsend</term><term>Uninfected</term><term>Vaccinia</term><term>Viral</term><term>Virus</term><term>Yewdell</term></keywords></textClass><langUsage><language ident="en">en</language></langUsage></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">Abstract: We have investigated the recognition of the PB1, neuraminidase, and matrix (Ml) proteins of influenza virus A/NT/ 60/68 (H3N2 subtype) by secondary in vitro stimulated polyclonal cytotoxic T lymphocyte (CTL) populations. While these three proteins have different functions and cellular locations, they can all be recognized as target antigens. However, the immunogenicity of these proteins for CTLs is under strict genetic control. Thus, PB1 protein is recognized as a cross-reactive target antigen by CTLs raised in CBA (H-2k) but not BALB/c (H-2d) mice. CBA, but not BALB/c mice, also generate a low-level CTL response to the neuraminidase. This latter response was only detectable following in vivo priming of CBA mice with a recombinant vaccinia virus expressing neuraminidase (N2-VACC). The matrix protein, expressed from recombinant vaccinia virus M-VACC, was not recognized as an antigen by CTL generated from either CBA or BALB/c strains of mice. By contrast, human HLA-A2-restricted influenza virus-specific CTLs were shown to recognize this matrix protein as a target antigen. Endogenous expression of as little as 90 amino acids of the matrix protein was sufficient to render target cells susceptible to lysis by such CTLs.</div></front></TEI><affiliations><list><country><li>Royaume-Uni</li><li>États-Unis</li></country><region><li>Angleterre</li><li>Californie</li><li>Oxfordshire</li></region><settlement><li>Oxford</li></settlement><orgName><li>Université d'Oxford</li></orgName></list><tree><noCountry><name sortKey="Brownlee, George G" sort="Brownlee, George G" uniqKey="Brownlee G" first="George G." last="Brownlee">George G. Brownlee</name></noCountry><country name="Royaume-Uni"><region name="Angleterre"><name sortKey="Reay, Philip A" sort="Reay, Philip A" uniqKey="Reay P" first="Philip A." last="Reay">Philip A. Reay</name></region><name sortKey="Gotch, Frances M" sort="Gotch, Frances M" uniqKey="Gotch F" first="Frances M." last="Gotch">Frances M. Gotch</name><name sortKey="Jones, Ian M" sort="Jones, Ian M" uniqKey="Jones I" first="Ian M." last="Jones">Ian M. Jones</name><name sortKey="Mcmichael, Andrew J" sort="Mcmichael, Andrew J" uniqKey="Mcmichael A" first="Andrew J." last="Mcmichael">Andrew J. Mcmichael</name></country><country name="États-Unis"><region name="Californie"><name sortKey="Reay, Philip A" sort="Reay, Philip A" uniqKey="Reay P" first="Philip A." last="Reay">Philip A. Reay</name></region></country></tree></affiliations></record>Pour manipuler ce document sous Unix (Dilib)
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