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dc.contributor.authorMutso, Margiten_US
dc.contributor.authorMorro, Ainhoaen_US
dc.contributor.authorSmedberg, Ceciliaen_US
dc.contributor.authorKasvandik, Sergoen_US
dc.contributor.authorAquilimeba, Murielen_US
dc.contributor.authorTeppor, Monaen_US
dc.contributor.authorTarve, Liisien_US
dc.contributor.authorLulla, Alekseien_US
dc.contributor.authorLulla, Valeriaen_US
dc.contributor.authorSaul, Sirleen_US
dc.contributor.authorThaa, Bastianen_US
dc.contributor.authorMcInerney, Geralden_US
dc.contributor.authorMerits, Andresen_US
dc.contributor.authorVarjak, Margusen_US
dc.date.accessioned2019-05-29T12:41:08Z
dc.date.available2019-05-29T12:41:08Z
dc.date.issued2018en_US
dc.identifier.issn1999-4915en_US
dc.identifier.doi10.3390/v10050226en_US
dc.identifier.urihttp://hdl.handle.net/10072/381885
dc.description.abstractInfection by Chikungunya virus (CHIKV) of the Old World alphaviruses (family Togaviridae) in humans can cause arthritis and arthralgia. The virus encodes four non-structural proteins (nsP) (nsP1, nsp2, nsP3 and nsP4) that act as subunits of the virus replicase. These proteins also interact with numerous host proteins and some crucial interactions are mediated by the unstructured C-terminal hypervariable domain (HVD) of nsP3. In this study, a human cell line expressing EGFP tagged with CHIKV nsP3 HVD was established. Using quantitative proteomics, it was found that CHIKV nsP3 HVD can bind cytoskeletal proteins, including CD2AP, SH3KBP1, CAPZA1, CAPZA2 and CAPZB. The interaction with CD2AP was found to be most evident; its binding site was mapped to the second SH3 ligand-like element in nsP3 HVD. Further assessment indicated that CD2AP can bind to nsP3 HVDs of many different New and Old World alphaviruses. Mutation of the short binding element hampered the ability of the virus to establish infection. The mutation also abolished ability of CD2AP to co-localise with nsP3 and replication complexes of CHIKV; the same was observed for Semliki Forest virus (SFV) harbouring a similar mutation. Similar to CD2AP, its homolog SH3KBP1 also bound the identified motif in CHIKV and SFV nsP3.en_US
dc.description.peerreviewedYesen_US
dc.languageEnglishen_US
dc.publisherMDPIen_US
dc.publisher.placeSwitzerlanden_US
dc.relation.ispartofchapter226en_US
dc.relation.ispartofpagefrom1en_US
dc.relation.ispartofpageto21en_US
dc.relation.ispartofissue5en_US
dc.relation.ispartofjournalVirusesen_US
dc.relation.ispartofvolume10en_US
dc.subject.fieldofresearchMicrobiology not elsewhere classifieden_US
dc.subject.fieldofresearchcode060599en_US
dc.titleMutation of CD2AP and SH3KBP1 binding motif in alphavirus nsP3 hypervariable domain results in attenuated virusen_US
dc.typeJournal articleen_US
dc.type.descriptionC1 - Articlesen_US
dc.type.codeC - Journal Articlesen_US
dc.description.versionPublisheden_US
gro.facultyOffice of the Snr Dep Vice Chancellor, Institute for Glycomicsen_US
gro.rights.copyright© 2018 by the authors. Licensee MDPI, Basel, Switzerland. This article is an open access article distributed under the terms and conditions of the Creative Commons Attribution (CC BY) license (http://creativecommons.org/licenses/by/4.0/).en_US
gro.hasfulltextFull Text
gro.griffith.authorMutso, Margit


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