Electron cryo-microscopy of bacteriophage PR772 reveals the elusive vertex complex and the capsid architecture

. 2019 Sep 12 ; 8 () : . [epub] 20190912

Jazyk angličtina Země Anglie, Velká Británie Médium electronic

Typ dokumentu časopisecké články, práce podpořená grantem

Perzistentní odkaz   https://www.medvik.cz/link/pmid31513011

Grantová podpora
828-2012-108 Vetenskapsrådet - International
628-2008-1109 Vetenskapsrådet - International
822-2010-6157 Vetenskapsrådet - International
822-2012-5260 Vetenskapsrådet - International
KAW-2011.081 Knut och Alice Wallenbergs Stiftelse - International
ERC-291602 European Research Council - International
349-2011-6488 Vetenskapsrådet - International
2015-06107 Vetenskapsrådet - International
CZ.02.1.01/0.0/0.0/15_003/0000447 European Commission - International
CZ.02.1.01/0.0/0.0/15_003/0000447 European Structural and Investment Funds - International

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 Å, while the resolution of the protein capsid is 2.3 Å. 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.

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