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1 T6SS activity is silenced in plasmid-containing, antibio
2 T6SS delivers effectors to neighboring cells and corresp
3 T6SS is regulated at transcriptional and posttranslation
4 T6SS is responsible for translocation of a wide range of
5 T6SS sheaths are cytoplasmic tubular structures composed
6 T6SSs are a class of sophisticated cell contact-dependen
9 at one of these, type VI secretion system 5 (T6SS-5), is required for virulence in mammalian infectio
10 ism by bacterial type VI secretion system 5 (T6SS-5), which is an essential virulence factor in both
11 n 11 167 core T6SS components mapping to 906 T6SSs found in 498 bacterial strains representing 240 sp
15 monstrate that this protein is secreted in a T6SS-dependent manner and that it confers a fitness adva
21 ella enterica serovar Typhimurium requires a T6SS encoded within Salmonella pathogenicity island-6 (S
26 Our data suggest that, in P. aeruginosa, T6SS organelle assembly and lethal counterattack are reg
27 We show that, in the case of P. aeruginosa, T6SS-dependent killing of either Vibrio cholerae or Acin
31 chanism that modulates the deployment of all T6SS weapons that may be simultaneously produced within
35 of global control by RsmA to VgrG spike and T6SS toxin transcripts whose genes are scattered on the
36 effector-immunity paradigm for antibacterial T6SS substrates, the toxic activities of these effectors
37 two secreted substrates of the antibacterial T6SS from the opportunistic human pathogen, Serratia mar
38 ation is a general property of antibacterial T6SSs and effector delivery by the system exerts a stron
39 ded into how pathogens utilize antibacterial T6SSs to overcome competitors and succeed in polymicrobi
40 ate that several MIX-containing proteins are T6SS effectors and that they are not required for T6SS a
42 ived from experimentally validated bacterial T6SS effectors we identified a phylogenetically disperse
44 cterial virulence protein expression because T6SS-1 and some effectors of type 3 secretion system 3 (
48 del whereby the CTD of VgrG-5-, propelled by T6SS-5-, plays a key role in inducing membrane fusion, e
50 ly shown and/or predicted to be delivered by T6SSs into target eukaryotic and/or prokaryotic cells as
51 shaped hexamer secreted by all characterized T6SSs, binds specifically to cognate effector molecules.
53 is result also demonstrated that V. cholerae T6SS is capable of delivering effectors that could attac
54 VgrG3 gene, suggesting that the V. cholerae T6SS is functional and mediates antagonistic interbacter
58 It currently contains data on 11 167 core T6SS components mapping to 906 T6SSs found in 498 bacter
60 we conclude that RP4 induces "donor-directed T6SS attacks" at sites corresponding to Mpf-mediated mem
62 seudomonas aeruginosa encodes three distinct T6SS haemolysin coregulated protein (Hcp) secretion isla
63 confirmed that these differences distinguish T6SS classes that resulted from a functional co-evolutio
66 ression of hcp operons and vgrG3 that encode T6SS secreted proteins but has no effect on the expressi
67 approach, we discovered that the FPI-encoded T6SS exports at least three effectors encoded outside of
68 proach to the Hcp secretion island I-encoded T6SS (H1-T6SS) of Pseudomonas aeruginosa led to the iden
70 . pseudomallei strains engineered to express T6SS-5 in vitro show that the VgrG5 C-terminal domain is
72 ncluding many important human pathogens, few T6SS-dependent effector and immunity proteins have been
74 e VgrG5 C-terminal domain is dispensable for T6SS-mediated secretion of Hcp5, demonstrating that the
75 nstrate that PAAR proteins are essential for T6SS-mediated secretion and target cell killing by Vibri
78 kely represents an evolutionary strategy for T6SS effectors to reach their intended substrates regard
79 d to Bacteroides fragilis Unlike GA1 and GA2 T6SS loci, most GA3 loci do not encode identifiable effe
81 ned in two variable regions of GA3 loci, GA3 T6SSs of the species B. fragilis are likely the source o
85 1 and HsiC1 of the Pseudomonas aeruginosa H1-T6SS assemble into tubules resulting from stacking of co
87 r screen failed to identify two predicted H1-T6SS effectors, Tse5 and Tse6, which differ from Hcp-sta
89 the Hcp secretion island I-encoded T6SS (H1-T6SS) of Pseudomonas aeruginosa led to the identificatio
92 the independent contribution of the three H1-T6SS co-regulated vgrG genes, vgrG1abc, to bacterial kil
94 th respect to the requirement for the two H1-T6SS-exported VgrG proteins, whereas Tse5 and Tse6 deliv
95 s (75% decrease in internalization with a H2-T6SS mutant) and into lung epithelial cells through a ph
96 Here we performed a screen to identify H2-T6SS and H3-T6SS regulatory elements and found that the
98 re, we demonstrate that the expression of H2-T6SS genes of strain PAO1 is up-regulated during the tra
99 ggered the characterization of a suite of H2-T6SS toxins and their implication in direct bacterial co
104 oxes in the promoter region and find that H2-T6SS transcription is negatively regulated by iron.
105 have specifically implicated PldA and the H2-T6SS in pathogenesis, we uncovered a specific role for t
107 e the characterization of a P. aeruginosa H3-T6SS-dependent phospholipase D effector, PldB, and its t
109 erformed a screen to identify H2-T6SS and H3-T6SS regulatory elements and found that the posttranscri
110 tein (Hcp) secretion islands (H1, H2, and H3-T6SS), each involved in different aspects of the bacteri
112 e renamed TseF) appears to be secreted by H3-T6SS and is incorporated into outer membrane vesicles (O
113 ximal to the type VI secretion system H3 (H3-T6SS), functions synergistically with known iron acquisi
118 poN regulon has yet to be clearly defined in T6SS-active V. cholerae isolates, which use T6SS to targ
121 tion with bacterial cells carrying an intact T6SS locus and VgrG3 gene, suggesting that the V. choler
122 is a Gram-negative pathogen that can use its T6SS during antagonistic interactions with neighboring p
126 has no effect on the expression of the main T6SS cluster encoding sheath and other structural compon
128 dicted to transit not only the Gram-negative T6SS but also the Gram-positive type VII secretion syste
132 er, the identification and mode of action of T6SS effector proteins that mediate this protective effe
137 likely responsible for the high diversity of T6SS effector-immunity gene profiles observed for V. cho
138 ed in this study underscore the diversity of T6SS-secreted substrates and the distinctly different me
140 cid pH upregulates the expression of Hcp1 of T6SS-1 and TssM, a protein coregulated with T6SS-1.
142 bacterial fitness, systematic prediction of T6SS effectors remains challenging due to high effector
143 ly, these analyses uncover the prevalence of T6SS-dependent competition and reveal its potential role
145 dies suggest that the complete repertoire of T6SS effectors delivered to host cells is encoded by the
147 ion substrates of the T6SS and one subset of T6SS effectors consists of VgrG proteins with C-terminal
148 cations that describe three superfamilies of T6SS proteins, each dedicated to mediate the secretion o
150 Despite the widespread identification of T6SSs among Gram-negative bacteria, the number of experi
152 has documented striking dynamics of opposed T6SS organelles in adjacent sister cells of Pseudomonas
155 eins are found encoded together within other T6SS gene clusters, thus they represent founder members
156 Our findings provide an example of pathogen T6SS-dependent killing of commensal bacteria as a mechan
157 Phylogenetic analysis of phytobacterial T6SS clusters shows that they are distributed in the fiv
159 tructure of a sheath protein complex propels T6SS spike and tube components along with antibacterial
162 g) that likely mark the location of repeated T6SS-mediated protein translocation events between bacte
167 as the Bptm group, appear to encode several T6SSs, we and others have shown that one of these, type
168 components of the type VI secretion system (T6SS) and alginate biosynthetic pathways, whereas DC3000
169 to a bacteriocidal type VI secretion system (T6SS) effector VgrG3, exhibited a colonization defect.
178 The bacterial type VI secretion system (T6SS) is a dynamic organelle that bacteria use to target
185 The bacterial type VI secretion system (T6SS) is a supra-molecular complex akin to bacteriophage
189 The bacterial type VI secretion system (T6SS) is an organelle that is structurally and mechanist
192 ecently discovered type VI secretion system (T6SS) is widespread in bacterial pathogens and used to d
193 The bacterial type VI secretion system (T6SS) mediates antagonistic cell-cell interactions betwe
195 recognition by the type VI secretion system (T6SS) of Gram-negative bacteria, a widespread pathway th
197 ompetitors via the Type VI secretion system (T6SS) precipitates phase separation via the 'Model A' un
198 bour genes for the type VI secretion system (T6SS) that translocates effectors into neighbouring euka
201 ocepacia employs a type VI secretion system (T6SS) to survive in macrophages by disarming Rho-type GT
202 e bacteria use the type VI secretion system (T6SS) to translocate toxic effector proteins into adjace
203 s effectors of the type VI secretion system (T6SS) translocation apparatus; accordingly, we name thes
205 onism, such as the type VI secretion system (T6SS), a multiprotein needle-like apparatus that injects
206 aumannii encodes a type VI secretion system (T6SS), an antibacterial apparatus of Gram-negative bacte
207 res (GA1-3) of the type VI secretion system (T6SS), an effector delivery pathway that mediates interb
208 n system (T2SS), a type VI secretion system (T6SS), autotransporter, and outer membrane vesicles (OMV
209 d component of the type VI secretion system (T6SS), haemolysin co-regulated protein (Hcp), binds dire
210 onism, such as the type VI secretion system (T6SS), have not been defined in this group of organisms.
216 n of the cluster 5 type VI secretion system (T6SS-5) and its associated valine-glycine repeat protein
219 been described: type six secretion systems (T6SS); contact dependent inhibition (CDI); and bacterioc
222 d proteobacteria, type VI secretion systems (T6SSs) are potentially capable of facilitating diverse i
225 Bacteria employ type VI secretion systems (T6SSs) to facilitate interactions with prokaryotic and e
226 how that unlike the bacterial-cell-targeting T6SSs characterized so far, T6SS-5 localizes to the bact
227 umentation of cell-cell interactions (termed T6SS dueling) that likely mark the location of repeated
228 uch cell-cell interactions have been termed "T6SS dueling" and likely reflect a biological process th
240 osmoinduction of alginate synthesis and the T6SS, and resiliency of the T3SS to water limitation, su
246 work illustrates the twin role played by the T6SS, dealing death to local competitors while simultane
247 to directly targeting eukaryotic cells, the T6SS can also target other bacteria coinfecting a mammal
249 w that hsiE1 is a non-essential gene for the T6SS and suggest that HsiE1 may modulate incorporation o
250 indings to our developing picture of how the T6SS assembles and fires, how it is loaded with differen
253 structural and mechanistic insights into the T6SS and show that a phage sheathlike structure is likel
256 e core conserved secretion substrates of the T6SS and one subset of T6SS effectors consists of VgrG p
257 at corresponds to the point of attack of the T6SS apparatus elaborated by a second aggressive T6SS(+)
259 regarding the structure and function of the T6SS as well as the diverse signals and regulatory pathw
260 TssA1 could be a baseplate component of the T6SS Furthermore, we identified similarities between Tss
261 ws the phylogeny and biological roles of the T6SS in plant-associated bacteria, highlighting a remark
262 idespread occurrence and significance of the T6SS is becoming increasingly appreciated, as is its int
265 ian host, highlighting the importance of the T6SS not only for bacterial survival in environmental ec
266 Our results indicate a new model of the T6SS organelle in which the VgrG-PAAR spike complex is d
267 Neither the exact protein composition of the T6SS organelle nor the mechanisms of effector selection
275 that multivalent nanoparticles based on the T6SS sheath represent a versatile scaffold for vaccine a
277 gut in an Hcp1-dependent manner and that the T6SS antibacterial activity is essential for Salmonella
278 d pathogenic phytobacteria suggests that the T6SS provides fitness and colonization advantages in pla
279 nchial epithelial cells, indicating that the T6SS-5 is important in the host-pathogen interaction in
281 a of the order Bacteroidales, and that these T6SS loci segregate into three distinct genetic architec
283 experimentally confirm the identity of this T6SS and, by cryo electron microscopy (cryoEM), show the
286 ve pathogen Pseudomonas aeruginosa has three T6SSs involved in colonization, competition, and full vi
288 h induced soxS in E. coli expressing a toxic T6SS antibacterial effector and in E. coli treated with
291 ore, we provide evidence that one of the two T6SS nanotube subunits, Hcp1, is required for killing Kl
292 otein that establishes contacts with the two T6SS sub-complexes through direct interactions with TssL
293 e identification of numerous uncharacterized T6SS effectors that will undoubtedly lead to the discove
296 T6SS-active V. cholerae isolates, which use T6SS to target both bacterial competitors and eukaryotic
298 Our findings imply a potentially widespread T6SS-mediated mechanism, which deploys a single phosphol
300 significantly reduced in cells infected with T6SS-defective mutants of B. cenocepacia, suggesting tha
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