Targeted mutational analysis to unravel the complexity of African horse sickness virus NS3 function in mammalian cells

dc.contributor.authorFerreira-Venter, Linda
dc.contributor.authorVenter, Eudri
dc.contributor.authorTheron, Jacques
dc.contributor.authorVan Staden, Vida
dc.contributor.emailvida.vanstaden@up.ac.zaen_ZA
dc.date.accessioned2019-07-24T09:01:56Z
dc.date.issued2019-05
dc.description.abstractThe African horse sickness virus non-structural protein 3 (NS3) is involved in the final stages of infection. To gain insight into the function of different NS3 domains, we generated reverse genetics-derived mutants, each expressing a modified version of the protein. A functional comparison of these mutants to the wild-type virus in mammalian cells indicated the variable contribution of the different domains to the cytopathic effect and in ensuring effective virus trafficking and release. The transmembrane domains were determined as essential mediators of NS3 localisation, as the abnormal processing of these mutant proteins resulted in their nuclear localisation and interaction with NS1. NS3 cytoplasmic domain disruptions resulted in increased cytosolic virus particle accumulation and abnormal virion tethering to plasma membranes. Other aspects of infection were also affected, such as VIB formation and distribution of the outer capsid proteins. Overall, these results illustrate the intricate role of NS3 in the infection cycle.en_ZA
dc.description.departmentBiochemistryen_ZA
dc.description.departmentGeneticsen_ZA
dc.description.departmentMicrobiology and Plant Pathologyen_ZA
dc.description.embargo2020-05-01
dc.description.librarianhj2019en_ZA
dc.description.sponsorshipThe University of Pretoria Institutional Research Theme, South Africa (Grant A0V004) and the Poliomyelitis Research Foundation, South Africa (Grants 13/21 and 16/26). Graduate bursary support was received from the National Research Foundation of South Africa, South Africa (Grant number 102209 and 116412), the Poliomyelitis Research Foundation, South Africa (Grant 14/91) and the University of Pretoria, South Africa.en_ZA
dc.description.urihttp://www.elsevier.com/locate/yviroen_ZA
dc.identifier.citationFerreira-Venter, L., Venter, E., Theron, J. et al. 2019, 'Targeted mutational analysis to unravel the complexity of African horse sickness virus NS3 function in mammalian cells', Virology, vol. 531, pp. 149-161.en_ZA
dc.identifier.issn0042-6822 (print)
dc.identifier.issn1096-0341 (online)
dc.identifier.other10.1016/j.virol.2019.03.005
dc.identifier.urihttp://hdl.handle.net/2263/70784
dc.language.isoenen_ZA
dc.publisherElsevieren_ZA
dc.rights© 2019 Elsevier Inc. All rights reserved. Notice : this is the author’s version of a work that was accepted for publication in Virology. Changes resulting from the publishing process, such as peer review, editing, corrections, structural formatting, and other quality control mechanisms may not be reflected in this document. A definitive version was subsequently published in Virology, vol. 531, pp. 149-161, 2019. doi : 10.1016/j.virol.2019.03.005.en_ZA
dc.subjectRous sarcoma virus (RSV)en_ZA
dc.subjectPathwayen_ZA
dc.subjectReleaseen_ZA
dc.subjectGagen_ZA
dc.subjectTraffickingen_ZA
dc.subjectLipid raftsen_ZA
dc.subjectInsect cellen_ZA
dc.subjectAfrican horsesickness virus (AHSV)en_ZA
dc.subjectBluetongue virus (BTV)en_ZA
dc.subjectNon-structural protein 3 (NS3)en_ZA
dc.subjectReverse geneticsen_ZA
dc.subjectVirus traffickingen_ZA
dc.subjectVirus releaseen_ZA
dc.subjectNon-structural protein 1 (NS1)en_ZA
dc.subjectProtein functional domainsen_ZA
dc.titleTargeted mutational analysis to unravel the complexity of African horse sickness virus NS3 function in mammalian cellsen_ZA
dc.typePostprint Articleen_ZA

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