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TitleStructural Insights into Lactococcal Siphophage p2 Baseplate Activation Mechanism.
Journal, issue, pagesViruses, Vol. 12, Issue 8, Year 2020
Publish dateAug 11, 2020
AuthorsSilvia Spinelli / Denise Tremblay / Sylvain Moineau / Christian Cambillau / Adeline Goulet /
PubMed AbstractVirulent phages infecting , an industry-relevant bacterium, pose a significant risk to the quality of the fermented milk products. Phages of the Skunavirus genus are by far the most isolated ...Virulent phages infecting , an industry-relevant bacterium, pose a significant risk to the quality of the fermented milk products. Phages of the Skunavirus genus are by far the most isolated lactococcal phages in the cheese environments and phage p2 is the model siphophage for this viral genus. The baseplate of phage p2, which is used to recognize its host, was previously shown to display two conformations by X-ray crystallography, a rested state and an activated state ready to bind to the host. The baseplate became only activated and opened in the presence of Ca. However, such an activated state was not previously observed in the virion. Here, using nanobodies binding to the baseplate, we report on the negative staining electron microscopy structure of the activated form of the baseplate directly observed in the p2 virion, that is compatible with the activated baseplate crystal structure. Analyses of this new structure also established the presence of a second distal tail (Dit) hexamer as a component of the baseplate, the topology of which differs largely from the first one. We also observed an uncoupling between the baseplate activation and the tail tip protein (Tal) opening, suggesting an infection mechanism more complex than previously expected.
External linksViruses / PubMed:32796652 / PubMed Central
MethodsEM (single particle)
Resolution22 - 42.2 Å
Structure data

EMDB-11224:
negative staining 3D reconstruction of p2 virion baseplate in activated conformation (3D class with open Tal trimer)
Method: EM (single particle) / Resolution: 35.4 Å

11225

6zig

EMDB-11225: negative staining 3D reconstruction of p2 virion baseplate in activated conformation (3D class with closed Tal trimer)
PDB-6zig: Topological model of the p2 virion baseplate in activated conformation (closed Tal trimer)
Method: EM (single particle) / Resolution: 42.2 Å

11226

6zih

EMDB-11226: Negative staining 3D reconstruction of p2 virion baseplate in activated conformation
PDB-6zih: Topological model of p2 virion baseplate in activated conformation
Method: EM (single particle) / Resolution: 28.7 Å

PDB-6zjj:
Topological model of p2 virion baseplate in resting conformation
Method: ELECTRON MICROSCOPY / Resolution: 22.0 Å

Source
  • lactococcus phage p2 (virus)
KeywordsVIRAL PROTEIN / lactococcal siphophage p2 / baseplate / receptor-binding protein / Distal Tail protein / Tail-associated lysin

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