umu.sePublications
Change search
CiteExportLink to record
Permanent link

Direct link
Cite
Citation style
  • apa
  • ieee
  • modern-language-association-8th-edition
  • vancouver
  • Other style
More styles
Language
  • de-DE
  • en-GB
  • en-US
  • fi-FI
  • nn-NO
  • nn-NB
  • sv-SE
  • Other locale
More languages
Output format
  • html
  • text
  • asciidoc
  • rtf
VP3 is crucial for the stability of Nora virus virions
Umeå University, Faculty of Medicine, Department of Molecular Biology (Faculty of Medicine).
Umeå University, Faculty of Medicine, Department of Molecular Biology (Faculty of Medicine). Institute of Biomedical Technology, University of Tampere, FI-33520 Tampere, Finland.
Umeå University, Faculty of Medicine, Department of Medical Biochemistry and Biophysics.
Umeå University, Faculty of Medicine, Department of Medical Biochemistry and Biophysics.
Show others and affiliations
2016 (English)In: Virus Research, ISSN 0168-1702, E-ISSN 1872-7492, Vol. 223, 20-27 p.Article in journal (Refereed) Published
Abstract [en]

Nora virus is an enteric virus that causes persistent, non-pathological infection in Drosophila melanogaster. It replicates in the fly gut and is transmitted via the fecal-oral route. Nora virus has a single-stranded positive-sense RNA genome, which is translated in four open reading frames. Reading frame three encodes the VP3 protein, the structure and function of which we have investigated in this work. We have shown that VP3 is a trimer that has an α-helical secondary structure, with a functionally important coiled-coil domain. In order to identify the role of VP3 in the Nora virus life cycle, we constructed VP3-mutants using the cDNA clone of the virus. Our results show that VP3 does not have a role in the actual assembly of the virus particles, but virions that lack VP3 or harbor VP3 with a disrupted coiled coil domain are incapable of transmission via the fecal-oral route. Removing the region downstream of the putative coiled coil appears to have an effect on the fitness of the virus but does not hamper its replication or transmission. We also found that the VP3 protein and particularly the coiled coil domain are crucial for the stability of Nora virus virions when exposed to heat or proteases. Hence, we propose that VP3 is imperative to Nora virus virions as it confers stability to the viral capsid.

Place, publisher, year, edition, pages
Elsevier, 2016. Vol. 223, 20-27 p.
Keyword [en]
RNA viruses, Nora virus, Capsid stability, Virus biology
National Category
Immunology in the medical area
Identifiers
URN: urn:nbn:se:umu:diva-124102DOI: 10.1016/j.virusres.2016.06.011ISI: 000383826600003PubMedID: 27329665OAI: oai:DiVA.org:umu-124102DiVA: diva2:949152
Available from: 2016-07-17 Created: 2016-07-17 Last updated: 2016-11-10Bibliographically approved
In thesis
1. Biology of a small RNA virus that infects Drosophila melanogaster
Open this publication in new window or tab >>Biology of a small RNA virus that infects Drosophila melanogaster
2016 (English)Doctoral thesis, comprehensive summary (Other academic)
Abstract [en]

Drosophila melanogaster has been extensively used as a model organism to study diverse facets of biology, including host-pathogen interactions and the basic biology of its pathogens. I have used the fruit fly as a model to study elementary aspects of Nora virus biology, such as the role of the different proteins encoded by the virus genome. Nora virus, an enteric virus transmitted via the feca-oral route, does not cause any obvious pathology in the fly, although the infection is persistent. Nora virus genome consists of a positive strand RNA that is translated in four open reading frames (ORF).  Since sequence homology studies did not yield much information about the different Nora virus proteins, I have used the cDNA clone of the virus to construct mutants to identify the specific function of each protein. My results have shown that,

1) The protein(s) encoded by ORF 1 are crucial for the replication of the virus genome.

2) The C-terminus of the ORF 1-encoded protein (VP1), is an inhibitor to the RNAi pathway.

3) The transmembrane domain in the N-terminus of the ORF2-encoded protein (VP2) is important for the formation of Nora virus virions.

4) The ORF 3-encoded protein (VP3) forms α-helical trimers and this protein is essential for the stability of Nora virus capsid.                                                    

I have also performed RNA sequencing to investigate the transcriptional response of D. melanogaster in response to Nora virus infection and my results indicate that,                       

5) The upregulation of genes related to cellular stress and protein synthesis and the downregulation of basal digestive machinery, together with the induction of upd3, implies major gut epithelium damage and subsequent regeneration.

Place, publisher, year, edition, pages
Umeå: Umeå University, 2016. 52 p.
Keyword
Nora virus, Drosophila melanogaster, virus biology, host-pathogen interaction
National Category
Cell and Molecular Biology
Research subject
Molecular Biology
Identifiers
urn:nbn:se:umu:diva-127352 (URN)978-91-7601-593-3 (ISBN)
Public defence
2016-12-01, Hörsal 135, Byggnad 9A, Norrlands Universitetssjukhus, Umeå, 14:00 (English)
Opponent
Supervisors
Available from: 2016-11-10 Created: 2016-11-09 Last updated: 2016-11-24Bibliographically approved

Open Access in DiVA

No full text

Other links

Publisher's full textPubMed

Search in DiVA

By author/editor
Sadanandan, Sajna AnandEkström, Jens-OlaJonna, Venkateswara RaoHofer, AndersHultmark, Dan
By organisation
Department of Molecular Biology (Faculty of Medicine)Department of Medical Biochemistry and Biophysics
In the same journal
Virus Research
Immunology in the medical area

Search outside of DiVA

GoogleGoogle Scholar

Altmetric score

Total: 85 hits
CiteExportLink to record
Permanent link

Direct link
Cite
Citation style
  • apa
  • ieee
  • modern-language-association-8th-edition
  • vancouver
  • Other style
More styles
Language
  • de-DE
  • en-GB
  • en-US
  • fi-FI
  • nn-NO
  • nn-NB
  • sv-SE
  • Other locale
More languages
Output format
  • html
  • text
  • asciidoc
  • rtf