Structural Analysis of Jumbo Coliphage phAPEC6

Jeroen Wagemans, Jessica Tsonos, Dominique Holtappels, Kiandro Fortuna, Jean-Pierre Hernalsteens, Henri De Greve, Leandro F Estrozi, Maria Bacia-Verloop, Christine Moriscot, Jean-Paul Noben, Guy Schoehn, R Lavigne

Onderzoeksoutput: Articlepeer review

9 Citaten (Scopus)

Samenvatting

The phAPEC6 genome encodes 551 predicted gene products, with the vast majority (83%) of unknown function. Of these, 62 have been identified as virion-associated proteins by mass spectrometry (ESI-MS/MS), including the major capsid protein (Gp225; present in 1620 copies), which shows a HK97 capsid protein-based fold. Cryo-electron microscopy experiments showed that the 350-kbp DNA molecule of Escherichia coli virus phAPEC6 is packaged in at least 15 concentric layers in the phage capsid. A capsid inner body rod is also present, measuring about 91 nm by 18 nm and oriented along the portal axis. In the phAPEC6 contractile tail, 25 hexameric stacked rings can be distinguished, built of the identified tail sheath protein (Gp277). Cryo-EM reconstruction reveals the base of the unique hairy fibers observed during an initial transmission electron microscopy (TEM) analysis. These very unusual filaments are ordered at three annular positions along the contractile sheath, as well as around the capsid, and may be involved in host interaction.

Originele taal-2English
Artikelnummer3119
Aantal pagina's13
TijdschriftInternational Journal of Molecular Sciences
Volume21
Nummer van het tijdschrift9
DOI's
StatusPublished - mei 2020

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