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

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

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

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

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

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

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

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

13 phospholipase C, and chitinase activities is T2SS dependent.

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

15 rable with those observed upon abrogation of T2SS activity.

16 rable with those observed upon abrogation of T2SS activity.

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

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

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

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

21 epth characterization of the B. pseudomallei T2SS secretome.

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

44 The T2SS component EpsC of Vibrio cholerae plays an importan

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

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

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

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

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

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

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

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

53 alacturonase are known to be secreted by the T2SS.

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

55 y the major pseudopilin is essential for the T2SS.

56 for interacting with other proteins from the T2SS machinery.

57 wo different pseudopilin components from the T2SS.

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

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

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

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

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

63 2,4(-/-) mice, we reexamined the role of the T2SS system.

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

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

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

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

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

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

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

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