ライフサイエンスコーパス: cytolysin

1 O (PFO) is a sterol-dependent, pore-forming cytolysin.

2 y increasing expression of MCP-1, MCP-3, and cytolysin.

3 faecalis produce a two-subunit toxin, termed cytolysin.

4 ross-resistant to nisin and the pAD1-encoded cytolysin.

5 treptolysin O (SLO), a cholesterol-dependent cytolysin.

6 sceptible to the bactericidal effects of the cytolysin.

7 serum passaged to enhance the production of cytolysin.

8 es, demonstrating the possible presence of a cytolysin.

9 le cytotoxic component, possibly a hemolytic cytolysin.

10 onent lantibiotic homologous to enterococcal cytolysin.

11 d, but inactive, lectin from Vibrio cholerae cytolysin.

12 l cell resilience to a cholesterol-dependent cytolysin.

13 (PFO), a pore-forming cholesterol-dependent cytolysin.

14 density by perfringolysin O, a pore-forming cytolysin.

15 erved for perforin and cholesterol-dependent cytolysins.

16 e repeats-in-toxin (RTX) family of bacterial cytolysins.

17 ell death through the action of pore-forming cytolysins.

18 ulatory proteins and increased expression of cytolysins.

19 elong to the family of cholesterol-dependent cytolysins.

20 Cytolysin A (ClyA) is an alpha-pore forming toxin from p

21 The alpha-pore-forming toxin Cytolysin A (ClyA) is responsible for the hemolytic acti

22 ein (tCSP) fused to Salmonella serovar Typhi cytolysin A (ClyA) were constructed as a first step in t

23 g enzyme properties, in this work we evolved Cytolysin A from Salmonella typhi (ClyA) to a high level

24 ibe the cryptic chromosomally encoded 34-kDa cytolysin A hemolysin of Salmonella enterica serovar Typ

25 s the structural gene for the GBS haemolysin/cytolysin, a novel bacterial toxin.

26 the prototype for the cholesterol-dependent cytolysins, a family of bacterial pore-forming toxins th

27 We unveil early steps in NLP cytolysin action that determine plant clade-specific tox

28 rate that cytolysin immunity is unrelated to cytolysin activator (CylA) expression as previously prop

29 ogens, many of which exhibit pore-forming or cytolysin activity

30 infections, exhibit decreased beta-hemolysin/cytolysin activity, and show increased sensitivity to au

31 netic locus encoding the GBS beta-haemolysin/cytolysin activity.

32 etic locus (cyl) required for GBS haemolysin/cytolysin activity.

33 ate that another group of virulence factors, cytolysins, aid in the penetration of superantigens acro

34 toxins are the membrane-active pore-forming cytolysin alpha-toxin (Hla) and the amphipathic alpha-he

35 The staphylococcal cytolysin alpha-toxin and the streptococcal cytolysin st

36 ere proinflammatory, only the staphylococcal cytolysin alpha-toxin induced a strong immune response f

37 otoxins B and C, and enterotoxin-like X) and cytolysins (alpha-, beta-, and gamma-toxins) and challen

38 virulence were produced by both strains, and cytolysins (alpha-toxin and gamma-toxin), superantigens,

39 rated decreased expression of beta-hemolysin/cytolysin, an important cytotoxin implicated in facilita

40 ked increase in production of beta-hemolysin/cytolysin and a striking decrease in production of CAMP

41 To delineate the contributions of the cytolysin and lectin domains in pore formation, we used

42 Fur coordinates the reciprocal expression of cytolysins and a subset of immunomodulatory proteins.

43 ) family of proteins classically consists of cytolysins and hemolysins.

44 e microscopy images of cholesterol-dependent cytolysins and related proteins that form large pores in

45 ar chaperones, acid-resistance proteins, and cytolysin, and down-regulate several biosynthetic enzyme

46 Cholesterol-dependent cytolysins are a family of poreforming proteins that hav

47 , fsr, a putative quorum-sensing system, and cytolysin, are also important for nematode killing.

48 ember of the family of cholesterol-dependent cytolysins because it binds to human CD59 (hCD59) rather

49 f group B Streptococcus (GBS) beta-hemolysin/cytolysin (beta h/c) in a neonatal-rabbit model of GBS p

50 Production of a beta-hemolysin/cytolysin (beta-h/c) encoded by the cylE gene is associa

51 ranscription of a cytotoxin, beta-haemolysin/cytolysin (beta-H/C) that is critical for survival of GB

52 sion and the GBS pore-forming beta-hemolysin/cytolysin (beta-h/c) trigger autophagic activation.

53 nd related factors, including beta-hemolysin/cytolysin (beta-h/c), surface-anchored adhesin HvgA, and

54 rs including the pluripotent beta-haemolysin/cytolysin (beta-H/C).

55 The pore-forming GBS beta-hemolysin/cytolysin (betaH/C) encoded by cylE is an important viru

56 ution of the pore-forming GBS beta-hemolysin/cytolysin (betaH/C) to vaginal colonization, ascension,

57 resembles those of the cholesterol-dependent cytolysins but is distinct from that recently proposed f

58 steine protease and the streptolysin O (SLO) cytolysin, but not SIC, a protein that protects S. pyoge

59 asis of a model for the autoinduction of the cytolysin by a quorum-sensing mechanism involving a two-

60 Pore formation itself was examined for both cytolysins by encapsulating fluorescein-labeled peptides

61 acterial pathogen secreting a human-specific cytolysin called intermedilysin (ILY) as a major pathoge

62 Intermedilysin (ILY) has been shown to be a cytolysin capable of generating pores in the cell membra

63 Chiral GC-MS analysis revealed that, like cytolysin, carnolysin contained lanthionine and methylla

64 Upon histological examination, both cytolysins caused damage to the uppermost layers of the

65 Pneumolysin is a cholesterol-dependent cytolysin (CDC) and virulence factor of Streptococcus pn

66 e-forming toxin of the cholesterol-dependent cytolysin (CDC) family and a primary virulence factor of

67 FO) is a member of the cholesterol-dependent cytolysin (CDC) family of membrane-penetrating toxins.

68 hat is a member of the cholesterol-dependent cytolysin (CDC) family, most closely related to intermed

69 racis, a member of the cholesterol-dependent cytolysin (CDC) family, which includes listeriolysin O,

70 (ALO), a member of the cholesterol-dependent cytolysin (CDC) family.

71 ctivity encoded by the cholesterol-dependent cytolysin (CDC) listeriolysin O (LLO) acts within the in

72 The assembly of the cholesterol-dependent cytolysin (CDC) oligomeric pore complex requires a compl

73 The cholesterol-dependent cytolysin (CDC) pneumolysin (Ply) is a key virulence fac

74 LO) is a pore-forming, cholesterol-dependent cytolysin (CDC) secreted by Bacillus anthracis, the etio

75 Pneumolysin is a cholesterol-dependent cytolysin (CDC) toxin that forms lytic pores in host mem

76 (ILY), a pore forming cholesterol-dependent cytolysin (CDC), specifically binds to human CD59 (hCD59

77 nosis (BV), produces a cholesterol-dependent cytolysin (CDC), vaginolysin (VLY).

78 Cholesterol-dependent cytolysins (CDCs) are a large family of bacterial toxins

79 The cholesterol-dependent cytolysins (CDCs) are a large family of pore-forming tox

80 The cholesterol-dependent cytolysins (CDCs) are pore-forming toxins that have been

81 Cholesterol-dependent cytolysins (CDCs) are secreted, pore-forming toxins that

82 mechanism by which the cholesterol-dependent cytolysins (CDCs) assemble their giant beta-barrel pore

83 The pore-forming cholesterol-dependent cytolysins (CDCs) contribute to the pathogenic mechanism

84 rming mechanism of the cholesterol-dependent cytolysins (CDCs) exhibits an absolute requirement for m

85 haracterized bacterial cholesterol-dependent cytolysins (CDCs) is not detectable by sequence analysis

86 f domain 4 (D4) of the cholesterol-dependent cytolysins (CDCs) mediate the binding of the CDC monomer

87 Cholesterol-dependent cytolysins (CDCs) represent a family of homologous pore-

88 Pore formation by the cholesterol-dependent cytolysins (CDCs) requires the presence of cholesterol i

89 The majority of cholesterol-dependent cytolysins (CDCs) utilize cholesterol as a membrane rece

90 PLY is a member of the cholesterol-dependent cytolysins (CDCs), a family of pore-forming toxins that

91 ch as perforin and the cholesterol-dependent cytolysins (CDCs), all of which require the membrane for

92 (Ply), a member of the cholesterol-dependent cytolysins (CDCs), is produced by virtually all clinical

93 ve bacteria depends on cholesterol-dependent cytolysins (CDCs), which form pores in eukaryotic cell p

94 bacterial pore-forming cholesterol-dependent cytolysins (CDCs).

95 family of pore-forming cholesterol-dependent cytolysins (CDCs).

96 The cytolysin consists of two structural subunits, CylLL and

97 However, coproduction of gelatinase and cytolysin did not increase virulence additively, account

98 Apart from the cytolysin domain, VCC harbors two lectin-like domains: t

99 e binding and pore formation of a eukaryotic cytolysin, Equinatoxin II (EqtII).

100 Pyolysin (PLO), a cholesterol-dependent cytolysin expressed by Arcanobacterium pyogenes, is an i

101 iption of genes important for beta-hemolysin/cytolysin expression and export is similar to the wild t

102 An understanding of conditions that regulate cytolysin expression has advanced little since its initi

103 Cytolysin expression is regulated by one of the subunits

104 serine hydroxamate increased beta-hemolysin/cytolysin expression.

105 or the function of the cholesterol-dependent cytolysin family and its wide distribution suggests that

106 pyogenes, is a member of the thiol-activated cytolysin family of bacterial toxins.

107 (PFO), a member of the cholesterol-dependent cytolysin family of pore-forming toxins, forms large oli

108 l other members of the cholesterol-dependent cytolysin family, Ply lacks a signal peptide for export.

109 fringolysin O (PFO), a cholesterol-dependent cytolysin, forms large oligomeric pore complexes compris

110 68.4% similarity), the cholesterol-dependent cytolysins from Streptococcus intermedius and Gardnerell

111 vided into (1) control of metabolism and PSM cytolysin genes, which occurs independently of the small

112 n, work together to repress transcription of cytolysin genes.

113 tant with the influx of cells expressing the cytolysins granzymes A and B.

114 forin (also known as pore-forming protein or cytolysin), has been shown to be capable of undergoing p

115 Vibrio cholerae cytolysin/hemolysin (VCC) is an amphipathic 65-kDa beta-

116 s, and the localization of one of these (the cytolysin/hemolysin) to the periplasmic space indicates

117 A novel cytolysin immunity determinant at the 3' end of the pAD1

118 fic mutagenesis experiments demonstrate that cytolysin immunity is unrelated to cytolysin activator (

119 Cytolysin immunity is, however, encoded on the same tran

120 llows the organism to express high levels of cytolysin in response.

121 odel studies have established a role for the cytolysin in the pathogenesis of enterococcal disease.

122 suilysin, a member of cholesterol-dependent cytolysins, in differential pathogenicity between ST1 an

123 e to perfringolysin O transformed this toxic cytolysin into a nontoxic derivative that facilitated in

124 were sufficient to convert an extracellular cytolysin into a vacuole-specific lysin which mediated g

125 The enterococcal cytolysin is a virulence factor consisting of two post-t

126 In addition to its toxin activity, the cytolysin is bactericidal for nearly all Gram-positive o

127 However, unlike lantibiotics, the cytolysin is lytic for eukaryotic as well as prokaryotic

128 ion reactions during the biosynthesis of the cytolysin large subunit.

129 mouse-derived cells tested, the pore-forming cytolysin listeriolysin O (LLO) is absolutely required f

130 tion factor PrfA, including the pore-forming cytolysin listeriolysin O (LLO), two phospholipases C (P

131 to the cytosol by secreting the pore-forming cytolysin listeriolysin O (LLO).

132 irulence gene hly (encoding the pore-forming cytolysin listeriolysin) is under negative regulation by

133 The pore-forming cholesterol-dependent cytolysin, listeriolysin O (LLO), mediates bacterial esc

134 lular pathogen which secretes a pore-forming cytolysin, listeriolysin O (LLO), necessary for intracel

135 escapes from the phagosome using a secreted cytolysin, listeriolysin O (LLO).

136 The invertebrate cytolysin lysenin is a member of the aerolysin family of

137 ttack complex/perforin/cholesterol-dependent cytolysin (MACPF/CDC) proteins constitute a major superf

138 ttack Complex-Perforin/Cholesterol-Dependent Cytolysin (MACPF/CDC) superfamily.

139 ins produced by many Gram-positive bacteria, cytolysin-mediated evasion of lysosomal killing may be a

140 Cytolysin-mediated translocation (CMT) is a recently des

141 mily and its wide distribution suggests that cytolysin-mediated translocation (CMT) may be the equiva

142 The mechanism by which the cytolysin-mediated translocation (CMT) pathway of the Gr

143 Cytolysin-mediated translocation (CMT), performed by Str

144 A recent model for cytolysin-mediated translocation in Streptococcus pyogen

145 ripts encoding virulence factors involved in cytolysin-mediated translocation of NAD-glycohydrolase,

146 e cytosol of an infected host cell using the cytolysin-mediated translocation pathway.

147 e cluster was also present in gelatinase-and-cytolysin-negative strain E. faecalis JH2-2.

148 The cytolysin of E. faecalis is a novel bacterial toxin that

149 Listeriolysin O (LLO), a cholesterol-binding cytolysin of Listeria monocytogenes, exhibits cytokine-i

150 Pneumolysin, the cholesterol-dependent cytolysin of Streptococcus pneumoniae, induces inflammat

151 Insensitivity to NLP cytolysins of monocot plants may be explained by the len

152 munity determinant at the 3' end of the pAD1 cytolysin operon is described in the present study.

153 The cholesterol-dependent cytolysin Perfringolysin O (PFO) constitutes a powerful

154 r of the pore-forming, cholesterol-dependent cytolysin perfringolysin O (PFO).

155 ble" to binding by a modified version of the cytolysin perfringolysin O (PFO*), whereas another pool

156 racellular pathogen which secretes a related cytolysin, perfringolysin O (PFO).

157 The enterococcal, conjugative, cytolysin plasmid pAD1 confers a mating response to the

158 red blood cells to the cholesterol-dependent cytolysin pneumolysin, a key virulence factor of Strepto

159 f pneumolysin (Ply), a cholesterol-dependent cytolysin produced by pneumococcus.

160 eptolysin O (SLO) is a cholesterol-dependent cytolysin produced by the important human pathogen, grou

161 LO is the prototype of cholesterol-dependent cytolysins produced by many Gram-positive bacteria, cyto

162 irulence traits revealed that gelatinase and cytolysin production accounted for 40.8% and 36.5% of th

163 mammals by secreting a cholesterol-dependent cytolysin, pyolysin (PLO), which targets stromal cells.

164 , two aminopeptidases, TagA-related protein, cytolysin, RbmC, three hypothetical proteins encoded by

165 In addition to its well-recognized role as a cytolysin, recent evidence has indicated that SLS may in

166 ccination against secreted superantigens and cytolysins resulted in protection of 86 of 88 rabbits wh

167 een SLO and homologous cholesterol-dependent cytolysins revealed that membrane binding by SLO is nece

168 ingolysin O (PFO), a water-soluble monomeric cytolysin secreted by pathogenic Clostridium perfringens

169 in peptidase required for pilus assembly and cytolysin secretion in V. vulnificus.

170 Mutation of the genes encoding the cytolysin ShlA and its transporter ShlB resulted in atte

171 ophage apoptosis induced by the pore-forming cytolysin SLO contributes to GAS immune evasion and viru

172 ed toxin studies identified the pore-forming cytolysin streptolysin O (SLO) as necessary and sufficie

173 es, which utilizes the cholesterol-dependent cytolysin Streptolysin O (SLO) to translocate the NAD(+)

174 pyogenes, utilizes the cholesterol-dependent cytolysin Streptolysin O (SLO) to translocate the NAD(+)

175 cytolysin alpha-toxin and the streptococcal cytolysin streptolysin O enhanced penetration of toxic s

176 GAS virulence factors, including the potent cytolysin streptolysin S.

177 e, including the immunity factor IFS and the cytolysin (streptolysin O [SLO]), were more abundant in

178 the purification and characterization of the cytolysin subunits and detection of lanthionine-type pos

179 Genetic evidence also suggests that the cytolysin subunits are related to the rapidly growing cl

180 s at a specific cell density when one of the cytolysin subunits reaches an extracellular threshold co

181 atively results from cleavage of one or both cytolysin subunits.

182 Cytolysins, superantigens, and proteases were identified

183 30 to 40% identity with the thiol-activated cytolysins (TACYs) of a number of gram-positive bacteria

184 nterococcus faecalis more commonly produce a cytolysin than do commensal isolates.

185 rococcus faecalis produce an exotoxin called cytolysin that contributes to bacterial virulence.

186 streptococci (GBS) express a beta-haemolysin/cytolysin that contributes to disease pathogenesis.

187 eriolysin O (LLO) is a cholesterol-dependent cytolysin that is an essential virulence factor of Liste

188 Listeriolysin O (LLO) is a pore-forming cytolysin that mediates lysis of L. monocytogenes-contai

189 Intermedilysin is a cholesterol-dependent cytolysin that requires the human immune receptor CD59,

190 olysaccharide capsule and the beta-hemolysin/cytolysin toxin (beta-h/c).

191 Vibrio cholerae cytolysin (VCC) is a potent membrane-damaging cytolytic

192 Vibrio cholerae cytolysin (VCC) is a prominent member in the family of b

193 Vibrio cholerae cytolysin (VCC) is a toxin secreted by the human pathoge

194 re of the 450-kDa heptameric Vibrio cholerae cytolysin (VCC) toxin purified and crystallized in the p

195 thogenic Vibrio cholerae secrete V. cholerae cytolysin (VCC), an 80 kDa pro-toxin that assembles into

196 ae secretes a pore-forming toxin, V.cholerae cytolysin (VCC), which contains two domains that are str

197 acterized strain expressing the enterococcal cytolysin was found to be detrimental to Drosophila comp

198 Carnolysin, unlike cytolysin, was shown to contain d-alanine and unpreceden

199 The active cytolysin, when compared with heat-inactivated ILY, did

200 Here we show that superantigens and cytolysins, when used in vaccine cocktails, provide prot

201 nriched for the expression of a known toxin, cytolysin, which is plasmid encoded.

202 We have detected a cholesterol-dependent cytolysin, which we have named mitilysin, in a small num