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dc.contributor.authorO. Ilyinskii, Petren_US
dc.contributor.authorB. Meriin, Anatolien_US
dc.contributor.authorL. Gabai, Vladimiren_US
dc.contributor.authorV. Usachev, Evgenyen_US
dc.contributor.authorG. Prilipov, Alexeien_US
dc.contributor.authorThoidis, Galinien_US
dc.contributor.authorM. Schnieder, Alexanderen_US
dc.date.accessioned2017-04-24T12:49:52Z
dc.date.available2017-04-24T12:49:52Z
dc.date.issued2008en_US
dc.date.modified2011-10-20T06:39:24Z
dc.identifier.issn09618368en_US
dc.identifier.doi10.1110/ps.083443908en_AU
dc.identifier.urihttp://hdl.handle.net/10072/32042
dc.description.abstractIt is assumed that the proteosome-processing characteristics of fusion constructs can be predicted from the sum of the proteosome sensitivity of their components. In the present study, we observed that a fusion construct consisting of proteosome-degradable proteins does not necessarily result in a proteosomedegradable chimera. Conversely, fusion of proteosome-resistant proteins may result in a proteosomedegradable composite. We previously demonstrated that conserved influenza proteins can be unified into a single fusion antigen that is protective, and that vaccination with combinations of proteosome-resistant and proteosome-degradable antigens resulted in an augmented T-cell response. In the present study we constructed proteosome-degradable mutants of conserved influenza proteins NP, M1, NS1, and M2. These were then fused into multipartite proteins in different positions. The stability and degradation profiles of these fusion constructs were demonstrated to depend on the relative position of the individual proteins within the chimeric molecule. Combining unstable sequences of either NP and M1 or NS1 and M2 resulted in either rapidly proteosome degraded or proteosome-resistant bipartite fusion mutants. However, further unification of the proteosome-degradable forms into a single four-partite fusion molecule resulted in relatively stable chimeric proteins. Conversely, the addition of proteosome-resistant wild-type M2 to proteosomeresistant NP-M1-NS1 fusion protein lead to the decreased stability of the resulting four-partite multigene products, which in one case was clearly proteosome dependent. Additionally, a highly destabilized form of M1 failed to destabilize the wild-type NP. Collectively, we did not observe any additive effect leading to proteosomal degradation/nondegradation of a multigene construct.en_US
dc.description.peerreviewedYesen_US
dc.description.publicationstatusYesen_AU
dc.languageEnglishen_US
dc.language.isoen_AU
dc.publisherWiley-Blackwell Publishing, Inc.en_US
dc.publisher.placeUSAen_US
dc.relation.ispartofstudentpublicationNen_AU
dc.relation.ispartofpagefrom1077en_US
dc.relation.ispartofpageto1085en_US
dc.relation.ispartofissue6en_US
dc.relation.ispartofjournalProtein Scienceen_US
dc.relation.ispartofvolume17en_US
dc.rights.retentionYen_AU
dc.subject.fieldofresearchBiochemistry and Cell Biology not elsewhere classifieden_US
dc.subject.fieldofresearchcode060199en_US
dc.titleThe proteosomal degradation of fusion proteins cannot be predicted from the proteosome susceptibility of their individual componentsen_US
dc.typeJournal articleen_US
dc.type.descriptionC1 - Peer Reviewed (HERDC)en_US
dc.type.codeC - Journal Articlesen_US
gro.rights.copyrightSelf-archiving of the author-manuscript version is not yet supported by this journal. Please refer to the journal link for access to the definitive, published version or contact the author[s] for more information.en_AU
gro.date.issued2008
gro.hasfulltextNo Full Text


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