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dc.creatorAydillo, Teresa
dc.creatorAyllon, Juan
dc.creatorPavlisin, Amzie
dc.creatorMartínez Romero, Carles
dc.creatorTripathi, Shashank
dc.creatorMena, Ignacio
dc.creatorMoreira Soto, Andrés
dc.creatorVicente Santos, Amanda
dc.creatorCorrales Aguilar, Eugenia
dc.creatorSchwemmle, Martín
dc.creatorGarcía Sastre, Adolfo
dc.date.accessioned2019-02-01T20:33:40Z
dc.date.available2019-02-01T20:33:40Z
dc.date.issued2018-03-14
dc.identifier.citationhttps://jvi.asm.org/content/92/7/e02021-17
dc.identifier.issn1098-5514
dc.identifier.urihttps://hdl.handle.net/10669/76537
dc.description.abstractRecently, two new influenza A-like viruses have been discovered in bats, A/little yellow-shouldered bat/Guatemala/060/2010 (HL17NL10) and A/flat-faced bat/Peru/033/2010 (HL18NL11). The hemagglutinin (HA)-like (HL) and neuraminidase (NA)-like (NL) proteins of these viruses lack hemagglutination and neuraminidase activities, despite their sequence and structural homologies with the HA and NA proteins of conventional influenza A viruses. We have now investigated whether the NS1 proteins of the HL17NL10 and HL18NL11 viruses can functionally replace the NS1 protein of a conventional influenza A virus. For this purpose, we generated recombinant influenza A/Puerto Rico/8/1934 (PR8) H1N1 viruses containing the NS1 protein of the PR8 wild-type, HL17NL10, and HL18NL11 viruses. These viruses (r/NS1PR8, r/NS1HL17, and r/NS1HL18, respectively) were tested for replication in bat and nonbat mammalian cells and in mice. Our results demonstrate that the r/NS1HL17 and r/NS1HL18 viruses are attenuated in vitro and in vivo. However, the bat NS1 recombinant viruses showed a phenotype similar to that of the r/NS1PR8 virus in STAT1/ human A549 cells and mice, both in vitro and in vivo systems being unable to respond to interferon (IFN). Interestingly, multiple mouse passages of the r/NS1HL17 and r/NS1HL18 viruses resulted in selection of mutant viruses containing single amino acid mutations in the viral PB2 protein. In contrast to the parental viruses, virulence and IFN antagonism were restored in the selected PB2 mutants. Our results indicate that the NS1 protein of bat influenza A-like viruses is less efficient than the NS1 protein of its conventional influenza A virus NS1 counterpart in antagonizing the IFN response and that this deficiency can be overcome by the influenza virus PB2 protein.es_ES
dc.description.sponsorshipUniversidad de Costa Rica/[803-B4-656]/UCR/Costa Ricaes_ES
dc.description.sponsorshipCenter for Research on Influenza Pathogenesis (CRIP)es_ES
dc.description.sponsorshipNIAID-funded Center of Excellence for Influenza Research and Surveillance (CEIRS)es_ES
dc.description.sponsorshipDeutsche Forschungsgemeinschaft (SCHW632/15-1)es_ES
dc.language.isoen_USes_ES
dc.relation.ispartof
dc.sourceJournal of Virology, vol. 92(7), pp. 1-18es_ES
dc.subjectInfluenza viruseses_ES
dc.subjectNS1 proteines_ES
dc.subjectBates_ES
dc.subjectInterferonses_ES
dc.subject599.472 867 Chiroptera (Quirópteros, Murciélagos)es_ES
dc.titleSpecific Mutations in the PB2 Protein of Influenza A Virus Compensate for the Lack of Efficient Interferon Antagonism of the NS1 Protein of Bat Influenza A-Like Viruseses_ES
dc.typeartículo científico
dc.date.updated2019-01-11T21:56:04Z
dc.identifier.doi10.1128/JVI.02021-17
dc.description.procedenceUCR::Vicerrectoría de Investigación::Unidades de Investigación::Ciencias de la Salud::Centro de Investigación en Enfermedades Tropicales (CIET)es_ES
dc.description.procedenceUCR::Vicerrectoría de Docencia::Salud::Facultad de Microbiologíaes_ES
dc.identifier.codproyecto803-B4-656


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