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| Open AccessA type VII-secreted lipase toxin with reverse domain arrangement
Here Garrett et al. describe a toxin, TslA, secreted by type VII secretion system that has a reverse domain arrangement compared to other previously characterised substrates. The authors show that TslA is a lipase with antibacterial activity.
- Stephen R. Garrett
- , Nicole Mietrach
- & Tracy Palmer
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Article
| Open AccessParabacteroides distasonis ameliorates insulin resistance via activation of intestinal GPR109a
Here, the authors show that the gut commensal Parabacteroides distasonis alleviates insulin resistance via nicotinic acid-intestinal GPR109a axis activation, a process promoted by Dendrobium officinale polysaccharide.
- Yonggan Sun
- , Qixing Nie
- & Shaoping Nie
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Article
| Open AccessSerine peptidase Vpr forms enzymatically active fibrils outside Bacillus bacteria revealed by cryo-EM
Here, cryo-EM is used to identify an unreported fibril species derived from lab-cultured Bacillus amyloiquefaciens composed of the extracellular serine peptidase Vpr. Fibrillar Vpr is shown to be enzymatically active, suggesting the fibril form represents a strategy of enriching Vpr extracellular activity.
- Yijia Cheng
- , Jianting Han
- & Qin Cao
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Article
| Open AccessThe RIX domain defines a class of polymorphic T6SS effectors and secreted adaptors
Bacteria use the type VI secretion system (T6SS) to deliver toxic effectors into bacterial or eukaryotic cells. Here, Kanarek et al. identify a protein domain, RIX, that defines a class of polymorphic T6SS effectors with antibacterial and anti-eukaryotic toxic domains, and that enables T6SS-mediated delivery of other effectors.
- Katarzyna Kanarek
- , Chaya Mushka Fridman
- & Dor Salomon
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| Open AccessMembrane translocation process revealed by in situ structures of type II secretion system secretins
In this work the authors investigate two types of secretins in Escherichia coli, GspDα and GspDβ, and report the Cryo-ET in situ structures of their key intermediate states of during the translocation process. Yielding a resolution ranging from 9 Å to 19 Å, the structures allow the identification of different membrane interaction patterns and ways of transitioning the peptidoglycan layer. These results suggest two distinct models for the membrane translocation of GspDα and GspDβ and provide insights into the inner to outer membrane biogenesis of T2SS secretins.
- Zhili Yu
- , Yaoming Wu
- & Zhao Wang
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| Open AccessA nonstop thrill ride from genes to the assembly of the T3SS injectisome
The type three secretion system (T3SS) is a membrane-anchored nano-machine utilized by many pathogenic bacteria to inject effector proteins and thus take control of host cells. In a recent article, Kaval et al. reveal a striking colocalization of a T3SS-encoding locus, its transcriptional activators, protein products, and the complete structure at the cell membrane, which they claim provides evidence for a mechanism known as ‘transertion’.
- Itzhak Fishov
- & Sharanya Namboodiri
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Article
| Open AccessA trans-kingdom T6SS effector induces the fragmentation of the mitochondrial network and activates innate immune receptor NLRX1 to promote infection
Bacteria can affect cellular processes in other bacteria and in eukaryotic cells by injecting effectors using a type VI secretion system (T6SS). Here, Sá-Pessoa et al. describe how a T6SS effector from the bacterial pathogen Klebsiella pneumoniae triggers the fragmentation of the mitochondrial network in eukaryotic cells.
- Joana Sá-Pessoa
- , Sara López-Montesino
- & José A. Bengoechea
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Article
| Open AccessBrucella effectors NyxA and NyxB target SENP3 to modulate the subcellular localisation of nucleolar proteins
The bacterium Brucella abortus is an intracellular pathogen that modulates autophagy in host cells. Here, the authors identify two B. abortus effectors that interact with host protease SENP3, thus promoting cytoplasmic accumulation of nucleolar proteins associated with ribosomal biogenesis and facilitating intracellular replication of the pathogen
- Arthur Louche
- , Amandine Blanco
- & Suzana P. Salcedo
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Article
| Open AccessA secreted effector with a dual role as a toxin and as a transcriptional factor
Bacteria can deliver toxic effector proteins into the cytosol of neighboring cells. Here, the authors show that Yersinia pseudotuberculosis secretes an effector that modulates gene expression in neighboring cells of the same species and inhibits the growth of other competitors.
- Dandan Wang
- , Lingfang Zhu
- & Xihui Shen
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Article
| Open AccessDirect interaction of a chaperone-bound type III secretion substrate with the export gate
Recruitment of substrates to virulent bacterial type III secretion systems remains enigmatic. Here, a crystal structure reveals two binding sites between a secretion substrate in complex with its chaperone and the cytosolic domain of the export gate.
- Dominic Gilzer
- , Madeleine Schreiner
- & Hartmut H. Niemann
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Article
| Open AccessA periplasmic cinched protein is required for siderophore secretion and virulence of Mycobacterium tuberculosis
The pathogen Mycobacterium tuberculosis uses the siderophores called mycobactins and carboxymycobactins to acquire iron from the host. Here, Zhang et al. identify a protein that is important for siderophore secretion and for the pathogen’s growth in low-iron medium.
- Lei Zhang
- , James E. Kent
- & Michael Niederweis
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Article
| Open AccessCrkII/Abl phosphorylation cascade is critical for NLRC4 inflammasome activity and is blocked by Pseudomonas aeruginosa ExoT
Pseudomonas aeruginosa secretes the toxin ExoT, which is important for pathogenesis. Here, the authors show that ExoT inhibits NLRC4-dependent inflammatory responses during wound infection.
- Mohamed F. Mohamed
- , Kajal Gupta
- & Sasha H. Shafikhani
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Article
| Open AccessInhibition of SRP-dependent protein secretion by the bacterial alarmone (p)ppGpp
Bacterial responses to nutrient limitation and other stress conditions are often modulated by the nucleotide-based second messenger (p)ppGpp. Here, the authors show that (p)ppGpp inhibits the SRP membrane-protein insertion and secretion pathway by binding to GTPases Ffh and FtsY.
- Laura Czech
- , Christopher-Nils Mais
- & Gert Bange
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Article
| Open AccessStructure of a type IV secretion system core complex encoded by multi-drug resistance F plasmids
Bacteria conjugatively transfer DNA through type IV secretion systems (T4SSs). Here, the authors report the structure of a T4SS outer-membrane core complex (OMCC), revealing how a distinct C13:C17 symmetry mismatch exhibited by peripheral ring and central cone substructures is accommodated.
- Xiangan Liu
- , Pratick Khara
- & Bo Hu
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| Open AccessArchitecture of the outer-membrane core complex from a conjugative type IV secretion system
DNA transfer between two bacterial cells is mediated by the conjugative type 4 secretion systems (T4SSs). Here, the authors report the structure of a complete T4SS outer-membrane core complex (OMCC), revealing distinct C17 and C13 symmetries of its central inner and peripheral outer ring regions, respectively.
- Himani Amin
- , Aravindan Ilangovan
- & Tiago R. D. Costa
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Article
| Open AccessToxin secretion and trafficking by Mycobacterium tuberculosis
The tuberculosis necrotizing toxin (TNT) is the major cytotoxicity factor of M. tuberculosis (Mtb). Mtb possesses five type VII secretion systems (ESX). Pajuelo et al. show that the ESX-4 system is required for TNT secretion and that ESX-2 and ESX-4 systems work in concert with ESX-1 to permeabilize the phagosomal membrane and enable trafficking of TNT into the cytoplasm of macrophages infected with Mtb.
- David Pajuelo
- , Uday Tak
- & Michael Niederweis
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Article
| Open AccessThe cell envelope of Staphylococcus aureus selectively controls the sorting of virulence factors
The pathogen Staphylococcus aureus releases several pore-forming toxins, termed leukocidins, that kill immune cells. Here, Zheng et al. show that the retention of a leukocidin on bacterial cells and its release are modulated by lipoteichoic acid and a membrane lipid, which also control the sorting of other surface-associated proteins.
- Xuhui Zheng
- , Gerben Marsman
- & Victor J. Torres
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| Open AccessProcessive dynamics of the usher assembly platform during uropathogenic Escherichia coli P pilus biogenesis
Escherichia coli form pili structures in order to initiate infection of the urinary tract. Here, Thanassi et al., have solved the structures of pili assembly intermediates and provided insights into their biogenesis and assembly.
- Minge Du
- , Zuanning Yuan
- & David G. Thanassi
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| Open AccessDynamic relocalization of cytosolic type III secretion system components prevents premature protein secretion at low external pH
Many bacterial pathogens use a type III secretion system (T3SS) to inject effector proteins into host cells. Here, Wimmi et al. show that the external pH regulates the assembly of T3SS cytosolic components in intestinal pathogens, thus preventing T3SS activity in the stomach and allowing T3SS reactivation in the intestine.
- Stephan Wimmi
- , Alexander Balinovic
- & Andreas Diepold
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| Open AccessSubstrate-engaged type III secretion system structures reveal gating mechanism for unfolded protein translocation
Virulent type III secretion systems (T3SSs) or injectisomes enable pathogenic bacteria to inject effector proteins directly into the host cell cytoplasm. Structures of a needle complex engaged with the effector protein reveal the complete secretion channel and provide insights into the mechanism of substrate translocation through T3SSs.
- Sean Miletic
- , Dirk Fahrenkamp
- & Thomas C. Marlovits
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| Open AccessContact-independent killing mediated by a T6SS effector with intrinsic cell-entry properties
Bacteria can use type VI secretion systems (T6SSs) to inject toxic effector proteins into adjacent cells, in a contact-dependent manner. Here, the authors provide evidence of contact-independent killing by a T6SS effector that is secreted into the extracellular milieu and then taken up by other bacterial cells.
- Li Song
- , Junfeng Pan
- & Xihui Shen
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Article
| Open AccessPore-forming Esx proteins mediate toxin secretion by Mycobacterium tuberculosis
Tuberculosis necrotizing toxin (TNT) is secreted by Mycobacterium tuberculosis to kill host cells. Here, Tak, Dokland and Niederweis show that proteins EsxE and EsxF form membrane-spanning hetero-oligomeric pores that are important for TNT secretion.
- Uday Tak
- , Terje Dokland
- & Michael Niederweis
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Article
| Open AccessPandemic Vibrio cholerae shuts down site-specific recombination to retain an interbacterial defence mechanism
Vibrio cholerae uses a type VI secretion system (T6SS) to kill neighbouring competitors. Here, Santoriello et al. show that a T6SS gene cluster (Aux3) exists as a mobile, prophage-like element in some environmental strains, and as a stable truncated form in pandemic isolates. They propose that Aux3 acquisition increased competitive fitness of pre-pandemic V. cholerae.
- Francis J. Santoriello
- , Lina Michel
- & Stefan Pukatzki
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| Open AccessThe evolution of tit-for-tat in bacteria via the type VI secretion system
Game theory has contributed much to the understanding of social evolution. In an elegant combination of experimental tests and modelling, this study suggests that when bacteria face intense competition, repeated retaliation outcompetes a single tit-for-tat response to attack.
- William P. J. Smith
- , Maj Brodmann
- & Kevin R. Foster
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| Open AccessTssA–TssM–TagA interaction modulates type VI secretion system sheath-tube assembly in Vibrio cholerae
The molecular mechanisms by which the sheath-tube of the bacterial type VI secretion system assembles are not fully understood. Here, the authors present evidence that the priming of the sheath-tube is controlled by TssA–TssM–TagA in Vibrio cholerae.
- Maria Silvina Stietz
- , Xiaoye Liang
- & Tao G. Dong
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Article
| Open AccessMechanism of effector capture and delivery by the type IV secretion system from Legionella pneumophila
A membrane-embedded complex (called T4CC) is essential for injection of Legionella pneumophila effector proteins into human macrophages via a Type IV secretion system. Here, the authors purify and study the T4CC using functional and cryo-EM structural analyses, providing insights into the secretion mechanisms.
- Amit Meir
- , Kevin Macé
- & Gabriel Waksman
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| Open AccessIntramolecular chaperone-mediated secretion of an Rhs effector toxin by a type VI secretion system
Bacterial Rhs proteins with toxic domains are often secreted by type VI secretion systems. Here, the authors show that one of these proteins self-cleaves into three fragments, with the Rhs core and the N-terminal domain facilitating secretion and function of the C-terminal toxic domain.
- Tong-Tong Pei
- , Hao Li
- & Tao G. Dong
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Article
| Open AccessA comparative genomics methodology reveals a widespread family of membrane-disrupting T6SS effectors
Gram-negative bacteria deliver effectors via the type VI secretion system (T6SS) to outcompete their rivals. Here, Fridman et al. present an approach to identify T6SS effectors encoded in bacterial genomes without prior knowledge of their domain content or genetic neighbourhood, and identify a new family of membrane-disrupting effectors.
- Chaya M. Fridman
- , Kinga Keppel
- & Dor Salomon
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Article
| Open AccessAssembly and substrate recognition of curli biogenesis system
A major component of bacterial biofilms is curli amyloid fibrils secreted by the curli biogenesis system. Here authors use cryo-EM to visualize the secretion channel complexes (CsgF-CsgG) with and without the curli substrate and provide insights into curli biogenesis.
- Zhaofeng Yan
- , Meng Yin
- & Xueming Li
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Article
| Open AccessA family of Type VI secretion system effector proteins that form ion-selective pores
Type VI secretion systems (T6SSs) are used by bacteria to inject toxic effector proteins into neighbouring cells. Here, Mariano et al. show that an antibacterial effector from Serratia marcescens forms cation-selective pores that lead to inner-membrane depolarisation and increased outer-membrane permeability.
- Giuseppina Mariano
- , Katharina Trunk
- & Sarah J. Coulthurst
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Article
| Open AccessCore architecture of a bacterial type II secretion system
Bacterial type II secretion systems (T2SSs) translocate virulence factors, toxins and enzymes across the cell outer membrane. Here, Chernyatina and Low use negative stain and cryo-electron microscopy to reveal the core architecture of an assembled T2SS from the pathogen Klebsiella pneumoniae.
- Anastasia A. Chernyatina
- & Harry H. Low
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Article
| Open AccessMultiple conformations facilitate PilT function in the type IV pilus
Bacterial type IV pilus-like systems catalyse the formation of pilin fibres but it is unknown how they are powered. Here, the authors present crystal and cryo-EM structures of the hexameric motor ATPases PilB and PilT from Type IVa Pilus that reveal different conformational states, classify the conformations of all PilT-like ATPase structures and propose a model for PilT function.
- Matthew McCallum
- , Samir Benlekbir
- & P. Lynne Howell
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Article
| Open AccessProtein determinants of dissemination and host specificity of metallo-β-lactamases
Metallo-β-lactamases (MBLs) confer resistance to carbapenem antibiotics. Here, López et al. show that the host range of MBLs depends on the efficiency of MBL signal peptide processing and secretion into outer membrane vesicles, which affects bacterial fitness.
- Carolina López
- , Juan A. Ayala
- & Alejandro J. Vila
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| Open AccessA modular effector with a DNase domain and a marker for T6SS substrates
Bacteria deliver toxic effectors via type VI secretion systems (T6SSs) to dominate competitors. Here, the authors identify a Vibrio antibacterial effector that contains a new DNase toxin domain and a domain of unknown function that can be used as a marker to identify new T6SS effectors.
- Biswanath Jana
- , Chaya M. Fridman
- & Dor Salomon
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Article
| Open AccessAbundance of bacterial Type VI secretion system components measured by targeted proteomics
Type VI secretion systems (T6SS) are important for bacterial interaction, competition and virulence, but the abundance and assembly of their components is still not well understood. Here, the authors apply targeted proteomics to measure the abundance of T6SS components across different species and conditions.
- Lin Lin
- , Emmanuelle Lezan
- & Marek Basler
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Article
| Open AccessBidirectional contraction of a type six secretion system
Bacteria use contractile injection systems, such as type VI secretion systems (T6SS), to secrete proteins that mediate cell-cell interactions. Here, Szwedziak & Pilhofer show that both ends of a T6SS can attach to opposite sides of the cell, enabling the structure to contract in two opposite directions.
- Piotr Szwedziak
- & Martin Pilhofer
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Article
| Open AccessStructure of the type VI secretion system TssK–TssF–TssG baseplate subcomplex revealed by cryo-electron microscopy
Type VI secretion systems (T6SSs) translocate effector proteins into eukaryotic and bacterial recipient cells and are present in many Gram-negative bacteria. Here the authors present the 3.7 Å cryoEM structure of the E.coli T6SS baseplate wedge comprising TssK–TssF–TssG and propose a model for the T6SS baseplate and needle complex.
- Young-Jun Park
- , Kaitlyn D. Lacourse
- & David Veesler
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Article
| Open AccessVariation in bradyrhizobial NopP effector determines symbiotic incompatibility with Rj2-soybeans via effector-triggered immunity
The soybean Rj2 gene encodes a TIR-NBS-LRR protein that confers resistance to nodulation by certain rhizobial strains. Here, the authors show that T3SS effector NopP is an avirulence protein that is necessary for Bradyrhizobium diazoefficiens USDA 122 to trigger Rj2-dependent incompatibility.
- Masayuki Sugawara
- , Satoko Takahashi
- & Kiwamu Minamisawa
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Article
| Open AccessDesigner cells programming quorum-sensing interference with microbes
Bacterial populations communicate with AI-2 signaling molecules, helping to coordinate biofilm development and other group behaviors. Here the authors design a genetic circuit for mammalian cells that allows them to sense bacterial populations and interfere with quorum communication.
- Ferdinand Sedlmayer
- , Dennis Hell
- & Martin Fussenegger
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Article
| Open AccessStructures of chaperone-substrate complexes docked onto the export gate in a type III secretion system
Bacterial flagella are composed of proteins secreted by a type III secretion system (T3SS), which requires the action of dedicated chaperones. Here, Xing et al. report the structures of two ternary complexes among flagellar chaperones, flagellar protein substrates, and the export gate platform protein.
- Qiong Xing
- , Ke Shi
- & Charalampos G. Kalodimos
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Article
| Open AccessType IX secretion system PorM and gliding machinery GldM form arches spanning the periplasmic space
No structural data for the bacterial type IX secretion system (T9SS) are available so far. Here, the authors present the crystal structures of the periplasmic domains from two major T9SS components PorM and GldM, which span most of the periplasmic space, and propose a putative model of the T9SS core membrane complex.
- Philippe Leone
- , Jennifer Roche
- & Alain Roussel
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Article
| Open AccessInsights into the structure and assembly of a bacterial cellulose secretion system
Many Gram-negative bacteria secrete exopolysaccharides via functionally homologous synthase-dependent systems. Here the authors use electron microscopy to reveal that biofilm-promoting cellulose in E. coli is secreted by a conserved multi-component secretion system with a megadalton-sized asymmetric architecture.
- Petya Violinova Krasteva
- , Joaquin Bernal-Bayard
- & Jean-Marc Ghigo
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Article
| Open AccessBacterial outer membrane vesicles suppress tumor by interferon-γ-mediated antitumor response
Bacterial outer membrane vesicles (OMVs) contain immunogens but no study has yet examined their potential in treating cancer. Here, the authors demonstrate that OMVs can suppress established tumours and prevent tumour metastasis by an interferon-γ mediated antitumor response.
- Oh Youn Kim
- , Hyun Taek Park
- & Yong Song Gho
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Article
| Open AccessA systematic exploration of the interactions between bacterial effector proteins and host cell membranes
Microbial pathogens secrete effector proteins into host cells to affect cellular functions. Here, the authors use a yeast-based screen to study around 200 effectors from six bacterial species, showing that over 30% of them interact with the eukaryotic plasma membrane or intracellular organelles.
- Bethany A. Weigele
- , Robert C. Orchard
- & Neal M. Alto
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Article
| Open AccessProphage-triggered membrane vesicle formation through peptidoglycan damage in Bacillus subtilis
It is unclear how Gram-positive bacteria, with a thick cell wall, can release membrane vesicles. Here, Toyofuku et al. show that a prophage-encoded endolysin can generate holes in the cell wall through which cytoplasmic membrane material protrudes and is released as vesicles.
- Masanori Toyofuku
- , Gerardo Cárcamo-Oyarce
- & Leo Eberl
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Article
| Open AccessA prophage tail-like protein is deployed by Burkholderia bacteria to feed on fungi
Some bacteria can feed on live fungi through unclear mechanisms. Here, the authors show that a T3SS-secreted protein, which is homologous to phage tail proteins, allows a Burkholderia gladioli strain to kill and feed on various fungal species.
- Durga Madhab Swain
- , Sunil Kumar Yadav
- & Gopaljee Jha
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Article
| Open AccessNutrient limitation determines the fitness of cheaters in bacterial siderophore cooperation
Cooperative behaviour among individuals provides a collective benefit, but is considered costly. Using Pseudomonas aeruginosa as a model system, the authors show that secretion of the siderophore pyoverdine only incurs a fitness cost and favours cheating when its building blocks carbon or nitrogen are growth-limiting.
- D. Joseph Sexton
- & Martin Schuster
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Article
| Open AccessReactogenicity to major tuberculosis antigens absent in BCG is linked to improved protection against Mycobacterium tuberculosis
MTBVAC, a live attenuatedMycobacterium tuberculosisvaccine under clinical evaluation, contains the major tuberculosis antigens ESAT6 and CFP10, which are absent from the current vaccine, BCG. Here, the authors show that these antigens contribute to enhanced vaccine efficacy in mouse models.
- Nacho Aguilo
- , Jesus Gonzalo-Asensio
- & Carlos Martin
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Article
| Open AccessThe type VI secretion system sheath assembles at the end distal from the membrane anchor
The bacterial Type VI secretion system (T6SS) delivers proteins into target cells using fast contraction of a long sheath anchored to the cell envelope. Here, Vettigeret al. study sheath dynamics in Vibrio choleraespheroplasts, and show that the sheath assembles by addition of subunits at the distal end.
- Andrea Vettiger
- , Julius Winter
- & Marek Basler