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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.
Upfold, Nicole; Ross, Caroline; Bishop, Özlem Tastan; Luke, Garry A; Knox, Caroline.
Afiliación
  • Upfold N; Department of Biochemistry and Microbiology, Rhodes University, Grahamstown 6140, South Africa.
  • Ross C; Research Unit in Bioinformatics (RUBi), Department of Biochemistry and Microbiology, Rhodes University, Grahamstown 6140, South Africa.
  • Bishop ÖT; Research Unit in Bioinformatics (RUBi), Department of Biochemistry and Microbiology, Rhodes University, Grahamstown 6140, South Africa.
  • Luke GA; Centre for Biomolecular Sciences, School of Biology, Biomolecular Sciences Building, University of St Andrews, North Haugh, St Andrews, Scotland KY16 9ST, UK.
  • Knox C; Department of Biochemistry and Microbiology, Rhodes University, Grahamstown 6140, South Africa. Electronic address: caroline.knox@ru.ac.za.
Virus Res ; 244: 153-163, 2018 01 15.
Article en En | MEDLINE | ID: mdl-29155139
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 5h post infection, capsid signal was diffusely cytoplasmic with strong perinuclear staining and moved into large punctate structures from 6 to 8h post infection. A plaque reduction neutralisation assay showed that the anti-TMEV capsid antibodies but not anti-VP1 antibodies could neutralise viral infection in vitro. The VP1 C-terminal residues recognised by the anti-TMEV capsid antibodies were mapped to a loop on the capsid surface near to the putative receptor binding pocket. In silico docking experiments showed that the known TMEV co-receptor, heparan sulfate, interacts with residues of VP1 in the putative receptor binding pocket, residues of VP3 in the adjacent pit and residues of the adjoining VP1 C-terminal loop which is recognised by the anti-TMEV capsid antibodies. These findings suggest that the anti-TMEV capsid antibodies neutralise virus infection by preventing heparan sulfate from binding to the capsid. The antibodies produced in this study are an important tool for further investigating virus-host cell interactions essential to picornavirus assembly.
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Texto completo: 1 Colección: 01-internacional Base de datos: MEDLINE Asunto principal: Virión / Cápside / Theilovirus / Proteínas de la Cápside / Anticuerpos Neutralizantes / Heparitina Sulfato / Anticuerpos Antivirales Tipo de estudio: Prognostic_studies Límite: Animals Idioma: En Revista: Virus Res Asunto de la revista: VIROLOGIA Año: 2018 Tipo del documento: Article País de afiliación: Sudáfrica Pais de publicación: Países Bajos
Texto completo
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Texto completo: 1 Colección: 01-internacional Base de datos: MEDLINE Asunto principal: Virión / Cápside / Theilovirus / Proteínas de la Cápside / Anticuerpos Neutralizantes / Heparitina Sulfato / Anticuerpos Antivirales Tipo de estudio: Prognostic_studies Límite: Animals Idioma: En Revista: Virus Res Asunto de la revista: VIROLOGIA Año: 2018 Tipo del documento: Article País de afiliación: Sudáfrica Pais de publicación: Países Bajos