ライフサイエンスコーパス: T2SS

1 Here, we report an atomic model for a T2SS pseudopilus from Klebsiella oxytoca, obtained by fi

2 A. hydrophila, namely, a Delta act mutant (a T2SS-associated cytotoxic enterotoxin-encoding gene) and

3 In a tentative model of a T2SS pseudopilus with EpsH at its tip, the conserved cre

4 rom the lungs, whereas those infected with a T2SS-T3SS double deletion were able to clear this mutant

5 CpaB is a membrane-anchored T2SS chaperone that interacts with CpaA and is required

6 The fact that LPS O-polysaccharide and T2SS mutant-induced responses were dependent on TLR2-TLR

7 es responsible for chitinolytic proteins and T2SS components are highly expressed during infection.

8 s potentiated by comparing the wild-type and T2SS mutant legionellae for their capacity to parasitize

9 ration upon the contact with the appropriate T2SS components.

10 reveal the core architecture of an assembled T2SS from the pathogen Klebsiella pneumoniae.

11 measures against the toxins secreted by both T2SS and T3SS.

12 cular mechanisms of substrate recruitment by T2SS remain elusive but a prevailing view is that the se

13 be part of the recruitment mechanism used by T2SS.

14 s on intact cell envelopes show a consistent T2SS structure repetition, highlighting its significance

15 otes unexpectedly possess homologues of core T2SS components.

16 dentity, are not secreted by the counterpart T2SS of each bacterium, indicating a fine-tuned control

17 our findings indicate that the pO157-encoded T2SS contributes to EHEC adherence and intestinal coloni

18 zation but that the colonization of an etpC (T2SS) mutant was reduced approximately 5-fold.

19 s, EpsG, EpsH, EpsI, EpsJ and EpsK, are five T2SS proteins that are thought to assemble into a pseudo

20 tudies where no or little role was found for T2SS in Burkholderia virulence, although virulence facto

21 n, and this process is an essential step for T2SS to assemble.

22 tructed deletion mutations in gspD and gspE, T2SS genes encoding an outer membrane secretin and a cyt

23 our recent analysis of macrophage infection, T2SS is clearly a major component of L. pneumophila intr

24 we reveal the in vivo structure of an intact T2SS imaged within the human pathogen Legionella pneumop

25 a complete architectural model of the intact T2SS that provides insights into the structure and funct

26 phospholipase C, and chitinase activities is T2SS dependent.

27 profiles of B. pseudomallei MSHR668 and its T2SS mutants were noticeably different when analyzed by

28 pili assembled in a heterologous Klebsiella T2SS type 2 secretion system (T2SS) by using cryo-electr

29 sistent with the presence of a mitochondrial T2SS-derived system (miT2SS).

30 rable with those observed upon abrogation of T2SS activity.

31 rable with those observed upon abrogation of T2SS activity.

32 The precise assembly of T2SS, which consists of at least 12 core-components call

33 on the inner to outer membrane biogenesis of T2SS secretins.

34 ent, demonstrating the direct involvement of T2SS in translocation of MtrC and OmcA to the bacterial

35 e bridges, whereas the major pseudopilins of T2SS do not.

36 so abolish N-methylation, the E5A variant of T2SS pseudopilin PulG remains N-methylated but is affect

37 epth characterization of the B. pseudomallei T2SS secretome.

38 e propose that LPS O-polysaccharide and PulA T2SS could be new targets for the design of new antimicr

39 ading enzymes, mainly pectinases, by similar T2SSs, called Out.

40 We hypothesize that such T2SS-induced structuration of some intrinsically disorde

41 key feature of the type 2 secretion system (T2SS) and is made up of multiple pseudopilins that are s

42 ors, including the type II secretion system (T2SS) and type III secretion system (T3SS) and their ass

43 pullulanase (PulA) type 2 secretion system (T2SS) are required for full effectiveness of the immune

44 ous Klebsiella T2SS type 2 secretion system (T2SS) by using cryo-electron microscopy (cryoEM), these

45 Deletions of type II secretion system (T2SS) genes reduced their extracellular release and thei

46 The type II secretion system (T2SS) is a multi-protein complex used by many bacteria t

47 The type II secretion system (T2SS) is a multiprotein envelope-spanning assembly that

48 The type 2 secretion system (T2SS) is present in some Gram-negative eubacteria and us

49 The type II secretion system (T2SS) is used by several Gram-negative bacteria for the

50 The type 2 secretion system (T2SS) occurring in Gram-negative bacteria is composed of

51 ns secreted by the type II secretion system (T2SS) of Pseudomonas aeruginosa during lung infection ha

52 stem (T3SS) and the type 2 secretion system (T2SS) of Salmonella.

53 ses revealed that a type 2 secretion system (T2SS) of the bacterial endosymbiont is required for the

54 etermined that the type II secretion system (T2SS) promotes the ability of Legionella pneumophila to

55 The type II secretion system (T2SS) secretes enzymes and toxins across the outer membr

56 Among these, the Type II Secretion System (T2SS) stands out as a pivotal structural component.

57 esses a functional type II secretion system (T2SS) that is required for full virulence.

58 the multi-protein type II secretion system (T2SS) to selectively translocate virulence factors from

59 The type II secretion system (T2SS) transports fully folded proteins of various functi

60 l of the bacterial type II secretion system (T2SS) which secrets diverse toxins that cause severe dis

61 e exterior using a type II secretion system (T2SS)(3,5).

62 acter, including a type II secretion system (T2SS), a type VI secretion system (T6SS), autotransporte

63 ed by P. aeruginosa type 2 secretion system (T2SS), during chronic infection.

64 stems, including a type II secretion system (T2SS), three type III secretion systems (T3SS), and six

65 hJ and its cognate type II secretion system (T2SS), which also secretes LT, are highly conserved in E

66 onas hydrophila, a type II secretion system (T2SS)-secreted cytotoxic enterotoxin (Act) and the T3SS

67 t substrate of the type II secretion system (T2SS).

68 in component of the type 2 secretion system (T2SS).

69 EHEC pO157-encoded type 2 secretion system (T2SS).

70 Type II secretion systems (T2SS) translocate virulence factors from the periplasmic

71 Bacterial type 2 secretion systems (T2SS), type 4 pili, and archaeal flagella assemble fibre

72 embrane gates in type-two secretion systems (T2SSs) and other bacterial protein secretion systems.

73 ative bacteria use type 2 secretion systems (T2SSs) to secrete proteins involved in virulence and ada

74 Bacterial type II secretion systems (T2SSs) translocate virulence factors, toxins and enzymes

75 of type IV pili, type II secretion systems (T2SSs), archaella, and other less-well-characterized fam

76 horizontally acquired from Archaea and that T2SSs were relatively recently repurposed from type IV p

77 The T2SS component EpsC of Vibrio cholerae plays an importan

78 The T2SS components OutE/L/M affect various interaction site

79 The T2SS is part of an ancient type IV filament superfamily

80 The T2SS of P. aeruginosa may play a role in death from pneu

81 The T2SS of Vibrio cholerae and related species is called th

82 The T2SS spans the bacterial cell envelope and extrudes subs

83 Although the T2SS has only limited sequence and component homology wi

84 +) strains killed mice within a day, and the T2SS(+) strains killed them later.

85 Both the T2SS and YodA proved to be essential for EHEC adherence

86 show that in vivo protease secretion by the T2SS is severely impaired.

87 Death caused by the T2SS(+) strain was accompanied by a >50-fold increase in

88 ce and that its secretion is mediated by the T2SS.

89 alacturonase are known to be secreted by the T2SS.

90 In Vibrio cholerae the T2SS is called the extracellular protein secretion (Eps)

91 y to egress) was considerably slower for the T2SS mutant than it was for the wild-type strain, and th

92 y the major pseudopilin is essential for the T2SS.

93 for interacting with other proteins from the T2SS machinery.

94 wo different pseudopilin components from the T2SS.

95 ants of P. aeruginosa, with mutations in the T2SS and/or T3SS, were used to infect mice.

96 ndicates that this heterodimer occurs in the T2SS of a large number of bacteria.

97 n in the type 4 pili system homologs, in the T2SS, the major protein component of the central pseudop

98 known Vfr-dependent functions, including the T2SS, the T3SS, flagellum- or TFP-dependent motility, vi

99 but disengaged from the inner membrane, the T2SS has a much longer periplasmic vestibule and it has

100 inking the inner-membrane sub-complex of the T2SS in V. cholerae to the outer membrane secretin.

101 2,4(-/-) mice, we reexamined the role of the T2SS system.

102 ssembly proteins, and with components of the T2SS that allow for heterologous fibre assembly.

103 Five proteins of the T2SS, the pseudopilins, are thought to assemble into a p

104 ocuses on the structure and mechanism of the T2SS.

105 ice infected with a strain that had only the T2SS were unable to eradicate the organism from the lung

106 In both animals and plants, the T2SS is increasingly recognized as a key driver of virul

107 Our results show that the T2SS has a highly dynamic modular architecture, with imp

108 of the bacterial vacuoles and found that the T2SS mutant grows at a decreased rate and does not attai

109 Comparative proteome analyses show that the T2SS releases chitinolytic enzymes (chitinase, chitosana

110 ifferences, including, for example, that the T2SS-ATPase complex is usually present but disengaged fr

111 Thus, the T2SS is absolutely required for L. pneumophila to grow t

112 t a cysteine-rich region directs TraA to the T2SS.

113 mmunized with SO7 that was delivered via the T2SS of Salmonella were better protected from challenge

114 al peptide and being mainly secreted via the T2SS.

115 cted for delivery of the SO7 antigen via the T2SS.

116 ated but is affected in interaction with the T2SS component PulM.

117 ization of GspD and GspC subunits within the T2SS could be compatible with a hexamer of dimers arrang

118 This T2SS was found to contribute to envelope integrity, whil

119 verall, mechanistic principles that underlie T2SS function have implication for other closely related

120 Transport of folded proteins via T2SS nanomachines requires the assembly of inner membran