- Title
- The generation and characterisation of neutralising antibodies against the Theiler’s murine encephalomyelitis virus (TMEV) GDVII capsid reveals the potential binding site of the host cell co-receptor, heparan sulfate:
- Creator
- Upfold, Nicole, Ross, Caroline J, Tastan Bishop, Özlem, Luke, Garry A, Knox, Caroline M
- Date
- 2018
- Type
- text
- Type
- article
- Identifier
- http://hdl.handle.net/10962/148181
- Identifier
- vital:38717
- Identifier
- DOI: 10.1016/j.virusres.2017.11.017
- Description
- The early stages of picornavirus capsid assembly and the host factors involved are poorly understood. Since the localisation of viral proteins in infected cells can provide information on their function, antibodies against purified Theiler's murine encephalomyelitis virus (TMEV) GDVII capsids were generated by immunisation of rabbits. The resultant anti-TMEV capsid antibodies recognised a C-terminal region of VP1 but not VP2 or VP3 by Western analysis. Examination of the sites of TMEV capsid assembly by indirect immunofluorescence and confocal microscopy showed that at 5 h post infection, capsid signal was diffusely cytoplasmic with strong perinuclear staining and moved into large punctate structures from 6 to 8 h post infection.
- Format
- 11 pages, pdf
- Language
- English
- Relation
- Virus research, Upfold, N., Ross, C., Bishop, Ö.T., Luke, G.A. and Knox, C., 2018. The generation and characterisation of neutralising antibodies against the Theiler’s murine encephalomyelitis virus (TMEV) GDVII capsid reveals the potential binding site of the host cell co-receptor, heparan sulfate. Virus research, 244, pp.153-163., Virus research volume 244 number 4 153 163 January 2018 1872-7492
- Rights
- Publisher
- Rights
- Use of this resource is governed by the terms and conditions of the Elsevier Terms and conditions statement (https://www.elsevier.com/legal/elsevier-website-terms-and-conditions)
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Knox, Caroline M (Prof)
Tastan Bishop, Ozlem (Prof)
RU Research Unit in Bioinformatics (RUBi)
SDG 03. Good Health and Well-Being
RU Department of Biochemistry, Microbiology and Bioinformatics
| Thumbnail | File | Description | Size | Format | |||
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