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TitleStructural basis for loading and inhibition of a bacterial T6SS phospholipase effector by the VgrG spike.
Journal, issue, pagesEMBO J, Vol. 39, Issue 11, Page e104129, Year 2020
Publish dateJun 2, 2020
AuthorsNicolas Flaugnatti / Chiara Rapisarda / Martial Rey / Solène G Beauvois / Viet Anh Nguyen / Stéphane Canaan / Eric Durand / Julia Chamot-Rooke / Eric Cascales / Rémi Fronzes / Laure Journet /
PubMed AbstractThe bacterial type VI secretion system (T6SS) is a macromolecular machine that injects effectors into prokaryotic and eukaryotic cells. The mode of action of the T6SS is similar to contractile phages: ...The bacterial type VI secretion system (T6SS) is a macromolecular machine that injects effectors into prokaryotic and eukaryotic cells. The mode of action of the T6SS is similar to contractile phages: the contraction of a sheath structure pushes a tube topped by a spike into target cells. Effectors are loaded onto the spike or confined into the tube. In enteroaggregative Escherichia coli, the Tle1 phospholipase binds the C-terminal extension of the VgrG trimeric spike. Here, we purify the VgrG-Tle1 complex and show that a VgrG trimer binds three Tle1 monomers and inhibits their activity. Using covalent cross-linking coupled to high-resolution mass spectrometry, we provide information on the sites of contact and further identify the requirement for a Tle1 N-terminal secretion sequence in complex formation. Finally, we report the 2.6-Å-resolution cryo-electron microscopy tri-dimensional structure of the (VgrG) -(Tle1) complex revealing how the effector binds its cargo, and how VgrG inhibits Tle1 phospholipase activity. The inhibition of Tle1 phospholipase activity once bound to VgrG suggests that Tle1 dissociation from VgrG is required upon delivery.
External linksEMBO J / PubMed:32350888 / PubMed Central
MethodsEM (single particle)
Resolution2.3 - 2.6 Å
Structure data

10218

6sjl

EMDB-10218, PDB-6sjl:
Structure of the Tle1 effector bound to the VgrG spike from the Type 6 secretion system
Method: EM (single particle) / Resolution: 2.6 Å

10219

6sk0

EMDB-10219, PDB-6sk0:
The VgrG spike from the Type 6 secretion system
Method: EM (single particle) / Resolution: 2.3 Å

10225

6ski

EMDB-10225, PDB-6ski:
The Tle hydrolase bound to the TTR domain of the VgrG spike of the Type 6 secretion system
Method: EM (single particle) / Resolution: 2.6 Å

Source
  • escherichia coli (E. coli)
KeywordsHYDROLASE / toxin / lipase / effector / bacterial / CHAPERONE / Puncture / spike / tip / carrier / inhibitor

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