Show simple item record

dc.contributor.advisorFielding, Burtram
dc.contributor.authorGordon, Bianca
dc.date.accessioned2021-08-19T08:54:19Z
dc.date.available2021-08-19T08:54:19Z
dc.date.issued2021
dc.identifier.urihttp://hdl.handle.net/11394/8362
dc.descriptionPhilosophiae Doctor - PhDen_US
dc.description.abstractHuman Coronavirus NL63 (HCoV-NL63) is one of seven coronaviruses (CoVs) that cause respiratory disease in the global population. The Membrane (M) and Nucleocapsid (N) proteins are part of the core CoV-structural proteins, crucial in viral replication and virion assembly. Here the expression of HCoV-NL63 M and N was characterized across multiple in vitro systems including bacterial, insect and mammalian. To detect untagged proteins in viral structural studies, anti-peptide antibodies were generated in a mouse model. Polyclonal antisera and hybridoma-secreted antibodies exhibited specific binding to their respective full length protein antigens. Anti-peptide monoclonal antibodies were successfully generated against the HCoV-NL63 M and N proteins. During CoV infection, the interaction of CoV M and N is necessary for the production of infectious virions. For the first time, co-expressed, full length HCoV-NL63 M and N were assayed for protein-protein interaction in a mammalian cell system, allowing for native protein folding and modification. M protein formed higher order homomultimers in the presence and absence of co-expressed N.en_US
dc.language.isoenen_US
dc.publisherUniversity of Western Capeen_US
dc.subjectHuman coronavirusen_US
dc.subjectCoronavirusen_US
dc.subjectStructural proteinsen_US
dc.subjectNucleocapsiden_US
dc.subjectInteractionen_US
dc.titleThe characterisation of human coronavirus nl63 proteinsen_US
dc.rights.holderUniversity of Western Capeen_US


Files in this item

Thumbnail

This item appears in the following Collection(s)

Show simple item record