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

Reddy HK, Carroni M, Hajdu J, Svenda M

Elife 8 (-) - [2019-09-12; online 2019-09-12]

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.

Cryo-EM [Service]

QC bibliography QC xrefs

PubMed 31513011

DOI 10.7554/eLife.48496

Crossref 10.7554/eLife.48496

pii: 48496
pmc: PMC6750898
PDB: 6Q5U