uu.seUppsala University Publications
Change search
CiteExportLink to record
Permanent link

Direct link
Cite
Citation style
  • apa
  • ieee
  • modern-language-association
  • 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
Structure and stability of icosahedral particles of a covalent coat protein dimer of bacteriophage MS2
Uppsala University, Disciplinary Domain of Science and Technology, Biology, Department of Cell and Molecular Biology, Structural Molecular Biology.
Latvian BMC.
Uppsala University, Disciplinary Domain of Science and Technology, Biology, Department of Cell and Molecular Biology, Structural Molecular Biology.
2009 (English)In: Protein Science, ISSN 0961-8368, Vol. 18, no 8, 1653-1661 p.Article in journal (Refereed) Published
Abstract [en]

Particles formed by the bacteriophage MS2 coat protein mutants with insertions in their surface loops induce a strong immune response against the inserted epitopes. The covalent dimers created by fusion of two copies of the coat protein gene are more tolerant to various insertions into the surface loops than the single subunits. We determined a 4.7Å-resolution crystal structure of an icosahedral particle assembled from covalent dimers and compared its stability to wildtype virions. The structure resembled the wildtype virion except for the intersubunit linker regions. The covalent dimer orientation was random with respect to both icosahedral twofold and quasi-twofold symmetry axes. A fraction of the particles was unstable in phosphate buffer because of assembly defects. Our results provide a structural background for design of modified covalent coat-protein dimer subunits for use in immunization.

Place, publisher, year, edition, pages
2009. Vol. 18, no 8, 1653-1661 p.
Keyword [en]
Virus, Structure, Assembly, Stability
National Category
Biological Sciences
Identifiers
URN: urn:nbn:se:uu:diva-100295DOI: 10.1002/pro.184ISI: 000268882100009OAI: oai:DiVA.org:uu-100295DiVA: diva2:210066
Available from: 2009-03-30 Created: 2009-03-30 Last updated: 2010-07-09Bibliographically approved

Open Access in DiVA

No full text

Other links

Publisher's full text
By organisation
Structural Molecular Biology
In the same journal
Protein Science
Biological Sciences

Search outside of DiVA

GoogleGoogle Scholar

doi
urn-nbn

Altmetric score

doi
urn-nbn
Total: 448 hits
CiteExportLink to record
Permanent link

Direct link
Cite
Citation style
  • apa
  • ieee
  • modern-language-association
  • 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