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Low-pH-induced membrane fusion mediated by human metapneumovirus F protein is a rare, strain-dependent phenomenon

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dc.contributor.authorHerfst, Sander
dc.contributor.authorMas-Lloret, Vicente
dc.contributor.authorVer, Lorena S
dc.contributor.authorWierda, Rutger J
dc.contributor.authorOsterhaus, Albert D M E
dc.contributor.authorFouchier, Ron A M
dc.contributor.authorMelero, Jose Antonio
dc.contributor.funderUnión Europea. Comisión Europea. 5 Programa Marcoes_ES
dc.contributor.funderComunidad de Madrid (España)es_ES
dc.contributor.funderMinisterio de Educación y Ciencia (España)es_ES
dc.date.accessioned2024-02-05T16:43:43Z
dc.date.available2024-02-05T16:43:43Z
dc.date.issued2008-09
dc.description.abstractMembrane fusion promoted by human metapneumovirus (HMPV) fusion (F) protein was suggested to require low pH (R. M. Schowalter, S. E. Smith, and R. E. Dutch, J. Virol. 80:10931-10941, 2006). Using prototype F proteins representing the four HMPV genetic lineages, we detected low-pH-dependent fusion only with some lineage A proteins and not with lineage B proteins. A glycine at position 294 was found responsible for the low-pH requirement in lineage A proteins. Only 6% of all HMPV lineage A F sequences have 294G, and none of the lineage B sequences have 294G. Thus, acidic pH is not a general trigger of HMPV F proteins for activity.es_ES
dc.description.peerreviewedSíes_ES
dc.description.sponsorshipThis work was sponsored in part by the FP5 grant “Hammocs” from the European Union. V.M. was funded by the VIRUSHOST consortium (Comunidad de Madrid), and L.S.V. was the recipient of a predoctoral fellowship from Ministerio Educación y Ciencia (Spain).es_ES
dc.format.number17es_ES
dc.format.page8891-8895es_ES
dc.format.volume82es_ES
dc.identifier.citationJ Virol. 2008 Sep;82(17):8891-5.es_ES
dc.identifier.doi10.1128/JVI.00472-08es_ES
dc.identifier.e-issn1098-5514es_ES
dc.identifier.journalJournal of virologyes_ES
dc.identifier.otherhttps://www.ncbi.nlm.nih.gov/pmc/articles/PMC2519679/pdf/0472-08.pdf
dc.identifier.pubmedID18596097es_ES
dc.identifier.urihttp://hdl.handle.net/20.500.12105/17485
dc.language.isoenges_ES
dc.publisherAmerican Society for Microbiology (ASM)es_ES
dc.relation.publisherversionhttps://doi.org/10.1128/JVI.00472-08es_ES
dc.repisalud.centroISCIII::Centro Nacional de Microbiologíaes_ES
dc.repisalud.institucionISCIIIes_ES
dc.rights.accessRightsopen accesses_ES
dc.rights.licenseAttribution-NonCommercial-NoDerivatives 4.0 Internacional*
dc.rights.urihttp://creativecommons.org/licenses/by-nc-nd/4.0/*
dc.subject.meshAnimalses_ES
dc.subject.meshChlorocebus aethiopses_ES
dc.subject.meshHumanses_ES
dc.subject.meshHydrogen-Ion Concentrationes_ES
dc.subject.meshMembrane Fusiones_ES
dc.subject.meshMetapneumoviruses_ES
dc.subject.meshModels, Moleculares_ES
dc.subject.meshPhylogenyes_ES
dc.subject.meshProtein Conformationes_ES
dc.subject.meshProtein Structure, Secondaryes_ES
dc.subject.meshVero Cellses_ES
dc.subject.meshViral Fusion Proteinses_ES
dc.titleLow-pH-induced membrane fusion mediated by human metapneumovirus F protein is a rare, strain-dependent phenomenones_ES
dc.typeresearch articlees_ES
dc.type.hasVersionVoRes_ES
dspace.entity.typePublication
relation.isAuthorOfPublicationcdaece7c-45bc-4988-bb11-429e0b25402b
relation.isAuthorOfPublication24741838-a235-4f7e-bd9c-117e88631c74
relation.isAuthorOfPublication4559c399-a4a8-4bc3-92ad-e0c684d6ddf3
relation.isAuthorOfPublication.latestForDiscoverycdaece7c-45bc-4988-bb11-429e0b25402b

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