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Electron cryo-microscopy of bacteriophage PR772 reveals the elusive vertex complex and the capsid architecture
Stockholm University, Faculty of Science, Department of Biochemistry and Biophysics.ORCID iD: 0000-0002-7697-6427
Number of Authors: 42019 (English)In: eLIFE, E-ISSN 2050-084X, Vol. 8, article id e48496Article in journal (Refereed) Published
Abstract [en]

Bacteriophage PR772, a member of the Tectiviridae family, has a 70 nm diameter icosahedral protein capsid that encapsulates a lipid membrane, dsDNA, and various internal proteins. An icosahedrally averaged CryoEM reconstruction of the wild-type virion and a localized reconstruction of the vertex region reveal the composition and the structure of the vertex complex along with new protein conformations that play a vital role in maintaining the capsid architecture of the virion. The overall resolution of the virion is 2.75 angstrom, while the resolution of the protein capsid is 2.3 angstrom. The conventional penta-symmetron formed by the capsomeres is replaced by a large vertex complex in the pseudo T = 25 capsid. All the vertices contain the host-recognition protein, P5; two of these vertices show the presence of the receptor-binding protein, P2. The 3D structure of the vertex complex shows interactions with the viral membrane, indicating a possible mechanism for viral infection.

Place, publisher, year, edition, pages
2019. Vol. 8, article id e48496
National Category
Biological Sciences
Identifiers
URN: urn:nbn:se:su:diva-174842DOI: 10.7554/eLife.48496ISI: 000486655300001PubMedID: 31513011OAI: oai:DiVA.org:su-174842DiVA, id: diva2:1361262
Available from: 2019-10-15 Created: 2019-10-15 Last updated: 2019-10-15Bibliographically approved

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