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Open AccessArticle

Structural Analysis of Jumbo Coliphage phAPEC6

1
Department of Biosystems, KU Leuven, Kasteelpark Arenberg 21—box 2462, 3001 Leuven, Belgium
2
Department of Biology, Vrije Universiteit Brussel, Pleinlaan 2, 1050 Brussel, Belgium
3
Structural Biology Brussels, Vrije Universiteit Brussel, Pleinlaan 2, 1050 Brussels, Belgium
4
VIB Center for Structural Biology, Pleinlaan 2, 1050 Brussels, Belgium
5
Univ. Grenoble Alpes, CEA, CNRS, IBS, F-38000 Grenoble, France
6
Univ. Grenoble Alpes, CNRS, CEA, EMBL, Integrated Structural Biology Grenoble (ISBG), F-38042 Grenoble, France
7
Biomedical Research Institute and Transnational University Limburg, Hasselt University, Agoralaan D, 3590 Hasselt, Belgium
*
Authors to whom correspondence should be addressed.
These authors contributed equally to the work.
Int. J. Mol. Sci. 2020, 21(9), 3119; https://doi.org/10.3390/ijms21093119
Received: 16 April 2020 / Revised: 27 April 2020 / Accepted: 27 April 2020 / Published: 28 April 2020
(This article belongs to the Special Issue Bacteriophage—Molecular Studies)
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. View Full-Text
Keywords: cryo-EM; jumbo phage; HK97-fold cryo-EM; jumbo phage; HK97-fold
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Wagemans, J.; Tsonos, J.; Holtappels, D.; Fortuna, K.; Hernalsteens, J.-P.; De Greve, H.; Estrozi, L.F.; Bacia-Verloop, M.; Moriscot, C.; Noben, J.-P.; Schoehn, G.; Lavigne, R. Structural Analysis of Jumbo Coliphage phAPEC6. Int. J. Mol. Sci. 2020, 21, 3119.

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