Umeå University's logo

umu.sePublications
Change search
CiteExportLink to record
Permanent link

Direct link
Cite
Citation style
  • apa
  • ieee
  • 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
Simultaneous membrane and RNA binding by tick-borne encephalitis virus capsid protein
Faculty of Biological and Environmental Sciences, Molecular and Integrative Bioscience Research Programme, University of Helsinki, Helsinki, Finland; University of Helsinki, Helsinki Institute of Life Sciences-Institute of Biotechnology, Helsinki, Finland.
Faculty of Biological and Environmental Sciences, Molecular and Integrative Bioscience Research Programme, University of Helsinki, Helsinki, Finland; University of Helsinki, Helsinki Institute of Life Sciences-Institute of Biotechnology, Helsinki, Finland.
Umeå University, Faculty of Medicine, Department of Clinical Microbiology. Umeå University, Faculty of Medicine, Molecular Infection Medicine Sweden (MIMS).
Umeå University, Faculty of Medicine, Department of Clinical Microbiology. Umeå University, Faculty of Medicine, Wallenberg Centre for Molecular Medicine at Umeå University (WCMM).ORCID iD: 0000-0001-5116-2577
Show others and affiliations
2023 (English)In: PLoS Pathogens, ISSN 1553-7366, E-ISSN 1553-7374, Vol. 19, no 2, article id e1011125Article in journal (Refereed) Published
Abstract [en]

Tick-borne encephalitis virus is an enveloped, pathogenic, RNA virus in the family Flaviviridae, genus Flavivirus. Viral particles are formed when the nucleocapsid, consisting of an RNA genome and multiple copies of the capsid protein, buds through the endoplasmic reticulum membrane and acquires the viral envelope and the associated proteins. The coordination of the nucleocapsid components to the sites of assembly and budding are poorly understood. Here, we investigate the interactions of the wild-type and truncated capsid proteins with membranes with biophysical methods and model membrane systems. We show that capsid protein initially binds membranes via electrostatic interactions with negatively-charged lipids, which is followed by membrane insertion. Additionally, we show that membrane-bound capsid protein can recruit viral genomic RNA. We confirm the biological relevance of the biophysical findings by using mass spectrometry to show that purified virions contain negatively-charged lipids. Our results suggest that nucleocapsid assembly is coordinated by negatively-charged membrane patches on the endoplasmic reticulum and that the capsid protein mediates direct contacts between the nucleocapsid and the membrane.

Place, publisher, year, edition, pages
Public Library of Science , 2023. Vol. 19, no 2, article id e1011125
National Category
Microbiology in the medical area
Identifiers
URN: urn:nbn:se:umu:diva-205497DOI: 10.1371/journal.ppat.1011125ISI: 000966733300001PubMedID: 36787339Scopus ID: 2-s2.0-85149054055OAI: oai:DiVA.org:umu-205497DiVA, id: diva2:1743206
Available from: 2023-03-14 Created: 2023-03-14 Last updated: 2025-03-03Bibliographically approved

Open Access in DiVA

fulltext(1940 kB)153 downloads
File information
File name FULLTEXT01.pdfFile size 1940 kBChecksum SHA-512
9c7ba469a0caa28ac4431cf536179335de18a0143a0d1bdb5578da1e8811478e6ea1d94c5be810063c21e3ba5dab4c6fd6e1dc8488848703a273d5f01555162d
Type fulltextMimetype application/pdf

Other links

Publisher's full textPubMedScopus

Authority records

Lindgren, MariePace, HudsonÖverby, Anna K.Bally, MartaLundmark, Richard

Search in DiVA

By author/editor
Lindgren, MariePace, HudsonÖverby, Anna K.Bally, MartaLundmark, Richard
By organisation
Department of Clinical MicrobiologyMolecular Infection Medicine Sweden (MIMS)Wallenberg Centre for Molecular Medicine at Umeå University (WCMM)Department of Integrative Medical Biology (IMB)
In the same journal
PLoS Pathogens
Microbiology in the medical area

Search outside of DiVA

GoogleGoogle Scholar
Total: 153 downloads
The number of downloads is the sum of all downloads of full texts. It may include eg previous versions that are now no longer available

doi
pubmed
urn-nbn

Altmetric score

doi
pubmed
urn-nbn
Total: 570 hits
CiteExportLink to record
Permanent link

Direct link
Cite
Citation style
  • apa
  • ieee
  • 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