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Article Dans Une Revue Proceedings of the National Academy of Sciences of the United States of America Année : 2019

Capsid expansion of bacteriophage T5 revealed by high resolution cryoelectron microscopy

Alexis Huet
  • Fonction : Auteur
Robert L. Duda
  • Fonction : Auteur
James F. Conway
  • Fonction : Auteur

Résumé

The large (90-nm) icosahedral capsid of bacteriophage T5 is composed of 775 copies of the major capsid protein (mcp) together with portal, protease, and decoration proteins. Its assembly is a regulated process that involves several intermediates, including a thick-walled round precursor prohead that expands as the viral DNA is packaged to yield a thin-walled and angular mature capsid. We investigated capsid maturation by comparing cryoelectron microscopy (cryo-EM) structures of the prohead, the empty expanded capsid both with and without decoration protein, and the virion capsid at a resolution of 3.8 Å for the latter. We detail the molecular structure of the mcp, its complex pattern of interactions, and their evolution during maturation. The bacteriophage T5 mcp is a variant of the canonical HK97-fold with a high level of plasticity that allows for the precise assembly of a giant macromolecule and the adaptability needed to interact with other proteins and the packaged DNA.

Dates et versions

hal-02307636 , version 1 (07-10-2019)

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Citer

Alexis Huet, Robert L. Duda, Pascale Boulanger, James F. Conway. Capsid expansion of bacteriophage T5 revealed by high resolution cryoelectron microscopy. Proceedings of the National Academy of Sciences of the United States of America, 2019, ⟨10.1073/pnas.1909645116⟩. ⟨hal-02307636⟩
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