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dc.contributor.authorYamada, Akio
dc.contributor.authorYoung, James F.
dc.contributor.authorEnnis, Francis A.
dc.date2022-08-11T08:09:10.000
dc.date.accessioned2022-08-23T16:19:48Z
dc.date.available2022-08-23T16:19:48Z
dc.date.issued1985-11-01
dc.date.submitted2017-11-20
dc.identifier.citationJ Exp Med. 1985 Nov 1;162(5):1720-5. doi:10.1084/jem.162.5.1720
dc.identifier.issn0022-1007 (Linking)
dc.identifier.doi10.1084/jem.162.5.1720
dc.identifier.pmid3903026
dc.identifier.urihttp://hdl.handle.net/20.500.14038/35138
dc.description.abstractWe have tested the ability of the c13 protein, which is a hybrid protein of the first 81 amino acids of the viral nonstructural protein (NS1) and the HA2 subunit of viral hemagglutination produced in E. coli, to render target cells susceptible to the lytic activity of influenza virus-specific cytotoxic T lymphocytes (CTL). The results showed that P815 cells coated with c13 protein were lysed by PR8 virus-induced secondary CTL derived from BALB/c mice. Cold-target inhibition tests clearly demonstrated that c13 protein-coated P815 cells were recognized by an H1 subtype-specific CTL population. Furthermore, PR8 virus-induced CTL derived from C3H mice did not lyse c13 protein-coated P815 cells, suggesting that c13 protein was recognized by CTL in conjunction with H-2d products. These findings suggest that this protein interacts with the cellular plasma membrane and makes target cells recognizable by H-2-restricted, influenza virus subtype-specific CTL.
dc.language.isoen_US
dc.relation<a href="http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?db=pubmed&cmd=Retrieve&list_uids=3903026&dopt=Abstract">Link to Article in PubMed</a>
dc.rights© 1985 Rockefeller University Press. Publisher PDF posted as allowed by the publisher's author rights policy at http://www.rupress.org/content/permissions-and-licensing.
dc.subjectImmunity
dc.subjectImmunology and Infectious Disease
dc.subjectImmunology of Infectious Disease
dc.subjectInfectious Disease
dc.subjectVirology
dc.titleInfluenza virus subtype-specific cytotoxic T lymphocytes lyse target cells coated with a protein produced in E. coli
dc.typeJournal Article
dc.source.journaltitleThe Journal of experimental medicine
dc.source.volume162
dc.source.issue5
dc.identifier.legacyfulltexthttps://escholarship.umassmed.edu/cgi/viewcontent.cgi?article=1345&amp;context=infdis_pp&amp;unstamped=1
dc.identifier.legacycoverpagehttps://escholarship.umassmed.edu/infdis_pp/345
dc.identifier.contextkey11095277
refterms.dateFOA2022-08-23T16:19:48Z
html.description.abstract<p>We have tested the ability of the c13 protein, which is a hybrid protein of the first 81 amino acids of the viral nonstructural protein (NS1) and the HA2 subunit of viral hemagglutination produced in E. coli, to render target cells susceptible to the lytic activity of influenza virus-specific cytotoxic T lymphocytes (CTL). The results showed that P815 cells coated with c13 protein were lysed by PR8 virus-induced secondary CTL derived from BALB/c mice. Cold-target inhibition tests clearly demonstrated that c13 protein-coated P815 cells were recognized by an H1 subtype-specific CTL population. Furthermore, PR8 virus-induced CTL derived from C3H mice did not lyse c13 protein-coated P815 cells, suggesting that c13 protein was recognized by CTL in conjunction with H-2d products. These findings suggest that this protein interacts with the cellular plasma membrane and makes target cells recognizable by H-2-restricted, influenza virus subtype-specific CTL.</p>
dc.identifier.submissionpathinfdis_pp/345
dc.contributor.departmentDepartment of Medicine, Division of Infectious Diseases and Immunology
dc.contributor.departmentCenter for Infectious Disease and Vaccine Research
dc.source.pages1720-5


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