Coevolution-Guided Mapping of the Type VI Secretion Membrane Complex-Baseplate Interface

Vanlioğlu, Etienne; Santin, Yoann G.; Filella-Merce, Isaac; Pellarin, Riccardo; Cascales, Éric

doi:10.1016/j.jmb.2022.167918

Cited by 3 publications

(3 citation statements)

References 56 publications

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“…As expected, these encoding genes ( tssK-tssL ) are now genetically linked in nearly all T6SS clusters [ 10 ] reinforcing the concept that they have co-evolved [ 46 ]. At this interface, the N-terminal shoulder domain of TssK binds to the baseplate components TssFG and the C-terminal head domain mediates interactions with the cytosolic domains of the TssL inner membrane protein [ 46–49 ]. The TssKFG complexes polymerize around the VgrG hub even in the absence of TssE.…”

Section: The Membrane Complexmentioning

confidence: 71%

“…Thus, a key step in the genesis of the T6SS gene cluster must have been the recombination and specialization of genes from the two systems mentioned above that resulted in the codification of new proteins that enabled T6SS docking. As expected, these encoding genes ( tssK-tssL ) are now genetically linked in nearly all T6SS clusters [10] reinforcing the concept that they have co-evolved [46]. At this interface, the N-terminal shoulder domain of TssK binds to the baseplate components TssFG and the C-terminal head domain mediates interactions with the cytosolic domains of the TssL inner membrane protein [46–49].…”

Section: The Membrane Complexmentioning

confidence: 84%

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Killing in the name of: T6SS structure and effector diversity

Allsopp

Bernal

2023

Microbiology

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The life of bacteria is challenging, to endure bacteria employ a range of mechanisms to optimize their environment, including deploying the type VI secretion system (T6SS). Acting as a bacterial crossbow, this system delivers effectors responsible for subverting host cells, killing competitors and facilitating general secretion to access common goods. Due to its importance, this lethal machine has been evolutionarily maintained, disseminated and specialized to fulfil these vital functions. In fact, T6SS structural clusters are present in over 25 % of Gram-negative bacteria, varying in number from one to six different genetic clusters per organism. Since its discovery in 2006, research on the T6SS has rapidly progressed, yielding remarkable breakthroughs. The identification and characterization of novel components of the T6SS, combined with biochemical and structural studies, have revealed fascinating mechanisms governing its assembly, loading, firing and disassembly processes. Recent findings have also demonstrated the efficacy of this system against fungal and Gram-positive cells, expanding its scope. Ongoing research continues to uncover an extensive and expanding repertoire of T6SS effectors, the genuine mediators of T6SS function. These studies are shedding light on new aspects of the biology of prokaryotic and eukaryotic organisms. This review provides a comprehensive overview of the T6SS, highlighting recent discoveries of its structure and the diversity of its effectors. Additionally, it injects a personal perspective on avenues for future research, aiming to deepen our understanding of this combative system.

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Section: The Membrane Complexmentioning

confidence: 71%

Section: The Membrane Complexmentioning

confidence: 84%

Killing in the name of: T6SS structure and effector diversity

Allsopp

Bernal

2023

Microbiology

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“…Then, the T6SS correlation matrix revealed two clusters of coevolving genes: one with TC and another with MC genes. BP genes with structural interactions with MC proteins (Vanlioğlu et al, 2023) coevolved with the MC genes but not with TC genes. Conversely, BP genes with common origin with TC genes (Cherrak et al, 2018) coevolved with them but not with MC genes.…”

Section: Discussionmentioning

confidence: 97%

AlignScape, displaying sequence similarity using self-organizing maps

Filella-Merce,

Mallet,

Durand

et al. 2024

Front. Bioinform.

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The current richness of sequence data needs efficient methodologies to display and analyze the complexity of the information in a compact and readable manner. Traditionally, phylogenetic trees and sequence similarity networks have been used to display and analyze sequences of protein families. These methods aim to shed light on key computational biology problems such as sequence classification and functional inference. Here, we present a new methodology, AlignScape, based on self-organizing maps. AlignScape is applied to three large families of proteins: the kinases and GPCRs from human, and bacterial T6SS proteins. AlignScape provides a map of the similarity landscape and a tree representation of multiple sequence alignments These representations are useful to display, cluster, and classify sequences as well as identify functional trends. The efficient GPU implementation of AlignScape allows the analysis of large MSAs in a few minutes. Furthermore, we show how the AlignScape analysis of proteins belonging to the T6SS complex can be used to predict coevolving partners.

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No fitness cost entailed by type VI secretion system synthesis, assembly, contraction, or disassembly in enteroaggregative Escherichia coli

Taillefer,

Giraud,

Cascales

2023

J Bacteriol

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Polymicrobial communities are shaped by beneficial and antagonistic interactions between the different species. One of the key players for competition is the type VI secretion system, a large multiprotein complex that assembles a contractile tail-like structure spanning the entire cytoplasm. This contractile tail is comprised of an inner tube tipped by a puncturing complex and wrapped by a sheath that polymerizes under an extended conformation. Contraction of the sheath propels the needle-like tube complex toward the target cell where it delivers effectors. The ClpV AAA + ATPase is then recruited to the contracted sheath and uses the energy of ATP hydrolysis for its disassembly. Due to the size of the apparatus and its mechanism of disassembly, it is thought that the T6SS mechanism of action is costly for the cell, and hence can significantly impact its fitness. By using enteroaggregative Escherichia coli strains in which the T6SS is arrested at different stages of its mechanism of action, we show here that there is no significant cost associated with T6SS synthesis, assembly, contraction, or disassembly in vitro . IMPORTANCE Bacteria use weapons to deliver effectors into target cells. One of these weapons, the type VI secretion system (T6SS), assembles a contractile tail acting as a spring to propel a toxin-loaded needle. Due to its size and mechanism of action, the T6SS was intuitively thought to be energetically costly. Here, using a combination of mutants and growth measurements in liquid medium, on plates, and in competition experiments, we show that the T6SS does not entail a growth cost to enteroaggregative Escherichia coli .

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Coevolution-Guided Mapping of the Type VI Secretion Membrane Complex-Baseplate Interface

Cited by 3 publications

References 56 publications

Killing in the name of: T6SS structure and effector diversity

Killing in the name of: T6SS structure and effector diversity

AlignScape, displaying sequence similarity using self-organizing maps

No fitness cost entailed by type VI secretion system synthesis, assembly, contraction, or disassembly in enteroaggregative Escherichia coli

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