ライフサイエンスコーパス: acta

1 (PLCs; PlcA and PlcB) and a surface protein (ActA).

2 nd member of the TGF-beta family, activin A (ActA).

3 ), two phospholipases C (PlcA and PlcB), and ActA.

4 mplex for its upstream activators N-WASP and ActA.

5 in L. monocytogenes by the bacterial protein ActA.

6 d motility mediated by the bacterial protein ActA.

7 e http://www.epcc.ed.ac.uk/software-products/acta.

8 ted with invasion, including InlA, InlB, and ActA.

9 ated with the Listeria monocytogenes protein ActA.

10 Complete gene sequences for actA (1,929 bp) and inlA (2,235 bp) provided the highest

11 ation in vitro, which is further enhanced by ActA [6] [7].

12 Here we show that activin A (rh-ActA), a known regulator of follicle formation and growt

13 s on the mlp-actA-plcB operon, which encodes ActA, a bacterial nucleation-promoting factor that media

14 aments, and this capacity can be enhanced by ActA, a protein used by Listeria to polymerize actin.

15 ActA accumulated more efficiently at younger, less inert

16 e rate of expression increase was changed in actA, actB, actC, or actD mutant strains.

17 A modified model of Nielsen et al. (Acta Agriculturae Scand Section A, 63, 2013 and 126) usi

18 found to cluster into these three lineages, actA alleles segregated independently.

19 polymorphisms revealed 8 hly, 11 inl4, and 2 actA alleles.

20 Surprisingly, our ActA allelic series enabled us to uncouple L. monocytoge

21 We generated an ActA allelic series within the defined Ena/VASP-binding

22 Expression of the cell surface protein ActA allows L. monocytogenes to activate host actin regu

23 binary solution containing profilin and the ActA analogue increased the observed rates of intracellu

24 Recent evidence suggests the ActA analogue may act by displacing the profilin-binding

25 ar concentration = 80 nM profilin plus 80 nM ActA analogue).

26 The actA and actB null mutations substantially decreased the

27 ame deletion of actB decreased expression of actA and actE to the same extent.

28 We propose that ActA and endogenous WASP family proteins promote Arp2/3-

29 follistatin (FS288) and its complexes (FS288-ActA and FS288-Mstn).

30 Collectively, these results indicate that actA and hly are differentially regulated in response to

31 ter gene system to compare the expression of actA and hly during intracellular growth to that during

32 Transcription of actA and hly, encoding LLO, is regulated by PrfA and inc

33 Several actA and hlyA alleles appeared to be predominantly assoc

34 PPPX(D/E), X = P or T] contained in Listeria ActA and in the p90 host-cell vinculin fragment generate

35 urce, based on the phylogenies inferred from actA and inlA (P = 0.02 and P = 0.07, respectively; Sour

36 actA and inlA also showed evidence of positive selection

37 actA and inlA as well as prs and the hypervariable house

38 sponse gene (sigB), and two virulence genes (actA and inlA) revealed between 11 (gap) and 33 (inlA) a

39 s response gene (sigB), two virulence genes (actA and inlA), and two intergenic regions (hly-mpl and

40 However, quantitative immunoprecipitation of ActA and LLO from infected J774 cells demonstrated appro

41 utant strain bearing double deletions in the actA and plcB virulence genes for an initial clinical sa

42 The 5' untranslated regions (5' UTRs) of actA and prfA have been shown to upregulate expression o

43 genes requires the bacterial surface protein ActA and protein components present in host cell cytopla

44 nine mutations in the NH2-terminal domain of ActA and replaced the endogenous actA gene with these mo

45 L. monocytogenes primarily involves PlcA and ActA and that either one of these factors must be presen

46 s the actin-nucleating activity of wild-type ActA and the Arp2/3 complex while also reducing the freq

47 differently to nucleation and stimulation by ActA and WASP, whereas p34/p20 bind actin filaments and

48 Both Bcl-2(ActA) and Bcl-2(Cytob5) suppressed p53-mediated transact

49 We investigated the roles of actin (ActA) and fimbrin (FimA) in hyphal growth in Aspergillus

50 allelic analysis of the virulence genes hly, actA, and inlA to uncover linkages between independent p

51 propose a model in which the polarization of ActA, and possibly other Gram-positive cell wall-associa

52 which ActB is activated by the C signal via ActA, and the act operon activates transcription of the

53 against the FEFPPPPTDE sequence of Listeria ActA, and this antibody: (a) localized at the trailing e

54 d not persist into puberty and both adult rh-ActA- and vehicle-treated animals demonstrated normal fe

55 endent on the long repeats and the amount of ActA; and (3) movement rate dependent on the PRRs.

56 ActA appears to control at least four functions that col

57 Furthermore, intracellular induction of actA appears to require additional steps or factors beyo

58 Listeriolysin O (LLO) and ActA are essential virulence determinants for Listeria m

59 the Listeria monocytogenes virulence factor ActA are propelled by actin polymerization.

60 erial pole expressing the highest density of ActA as a tail formed.

61 The accumulation of ActA at the bacterial poles displayed slower kinetics, o

62 timulated phosphoprotein (VASP), which binds ActA at the surfaces of Listeria cells and enhances bact

63 ocus sequence typing (MLST) based on loci in actA, betL, hlyA, gyrB, pgm, and recA.

64 e mapped an Mpl-dependent processing site in ActA between amino acid residues 207 to 238.

65 ActA binds Arp2/3 with a K(d) of 0.6 microm and competes

66 ActA/BMP chimeras can be useful in the study of receptor

67 comparable with wild type activin A, whereas ActA/BMP2 chimera showed a slightly reduced affinity tow

68 ActA/BMP7 chimera retained Act RII binding affinity comp

69 contribute to the extracellular induction of actA but did not affect intracellular levels of expressi

70 tro binding assays show that SH2-Bbeta binds ActA but not VASP; however, binding to ActA is greater i

71 y be explained by acid-dependent cleavage of ActA by the bacterial metalloprotease, Mpl.

72 n polymerization-based motility generated by ActA can be used to move nonbiological cargo, as has bee

73 mulated phosphoprotein (VASP) recruitment by ActA can bypass defects in actin monomer-binding.

74 uss "symmetry breaking" dynamics observed in ActA-coated bead experiments, and the implications of th

75 SH2-Bbeta enhances actin-based movement of ActA-coated beads in a biomimetic actin-based motility a

76 le symmetry breaking previously observed for ActA-coated spherical beads.

77 promoter is located immediately upstream of actA coding sequences, while the second promoter is cont

78 ion, the relative abundance of intracellular ActA compared to that of intracellular LLO is a function

79 The binding of heparin to the FS288-ActA complex was disrupted at 500 mM salt, whereas it wa

80 s, binding of heparin to FS288 and the FS288-ActA complex was enhanced.

81 est binding activity for FS288 and the FS288-ActA complex, whereas smaller heparin molecules could in

82 Challenges of immune mice with actA-deficient and with wild-type recombinant L. monocyt

83 Although mice immunized with low-dose actA-deficient L. monocytogenes had a substantial recall

84 contrast, mice immunized with a low dose of actA-deficient L. monocytogenes had approximately 10-fol

85 High-dose immunization with actA-deficient L. monocytogenes resulted in substantial

86 ty, elicited by immunization with attenuated actA-deficient Listeria monocytogenes, on the CD8(+)-T-c

87 CD8 T cell response following infection with ActA-deficient LM.

88 selectively deleting two virulence factors, ActA (DeltaactA) and Internalin B (DeltainlB), the immun

89 ed version, Advanced Complex Trait Analysis (ACTA), demonstrating dramatically improved performance.

90 The pure complex is sufficient to initiate ActA-dependent actin polymerization at the surface of L.

91 y, we compared the biochemical activities of ActA derivatives with the phenotypes of corresponding mu

92 We have synthesized and characterized an ActA dimer and provide evidence that the two ActA molecu

93 of actin nucleation mimic that of synthetic ActA dimers.

94 te bacterial movement rates both depended on ActA distribution, which in turn was tightly coupled to

95 To directly correlate ActA distributions to actin dynamics and motility of liv

96 etic lineages were confirmed when 22 partial actA DNA sequences were analyzed.

97 ocytogenes mutants expressing high levels of actA during in vitro growth were selected after chemical

98 he observation that L. monocytogenes lacking ActA Ena/VASP-binding sites were up to 400-fold less vir

99 plcB, cotranscribed with actA, encodes a broad-specificity phospholipase C that c

100 stly, a mutant which expressed low levels of ActA exhibited a phenotype indicative of a threshold; th

101 m of PrfA, known as PrfA*, increased overall actA expression in broth-grown cultures of both wild-typ

102 ng mutant isolates displayed a wide range of actA expression levels, and many were less sensitive to

103 ults indicate that the dramatic induction of actA expression that occurs in the host cell cytosol is

104 iptional activation; however, no increase in actA expression was detected following the introduction

105 The intracellular induction of actA expression was found to be dependent upon the actA

106 articipate in the intracellular induction of actA expression, L. monocytogenes mutants expressing hig

107 oter elements have been reported to regulate actA expression.

108 ributions of individual promoter elements to actA expression.

109 mally, a double mutant lacking both PlcA and ActA failed to grow in wild-type macrophages and colocal

110 Interestingly, profilin competes with ActA for binding of Arp2/3, but actophorin (cofilin) doe

111 lthough prior in vivo work has proposed that ActA forms dimers on the surface of L. monocytogenes, di

112 icial lipid vesicles coated with the protein ActA from the bacterial pathogen Listeria monocytogenes

113 ical staining pattern observed with the anti-ActA FS-1 antibody), indicating that motile bacteria att

114 of actin polymerization, (2) polarization of ActA function, (3) transformation of actin polymerizatio

115 sual phenotypes illustrate the complexity of ActA functions that control the actin-based motility of

116 expression of the hly fusion relative to the actA fusion in LB broth.

117 tosol of J774 cells, and the activity of the actA fusion was approximately 3-fold higher than that of

118 ay indicated that the hly fusion but not the actA fusion was significantly activated in Luria-Bertani

119 veral isolates contained mutations affecting actA gene expression that mapped at least 40 kb outside

120 l domain of ActA and replaced the endogenous actA gene with these molecular variants.

121 rized strain of L. monocytogenes lacking the actA gene.

122 pPL1 was used to introduce the hly and actA genes at comK-attBB' in deletion strains derived fr

123 The hly and actA genes were transcriptionally fused to Escherichia c

124 We examined the localization of ActA::GFP and FimA::GFP in live cells, and each displaye

125 In actively growing hyphae, cortical ActA::GFP and FimA::GFP patches were highly mobile throu

126 onocytogenes strain containing a chromosomal actA-gfpuv-plcB transcriptional fusion showed that blood

127 fA-dependent virulence factor PlcA, PlcB, or ActA grew normally, a double mutant lacking both PlcA an

128 n of actin polymerization in vitro, but pure ActA had no effect.

129 of Listeria monocytogenes virulence protein ActA have typically focused on the behavior of bacteria

130 Two actA in vitro expression mutants contained novel mutatio

131 or many of the unique physical properties of ActA including its extended structure, aberrant mobility

132 Ena/VASP F-actin-binding region did so in an ActA-independent manner.

133 After induction of expression, ActA initially appeared at distinct sites along the side

134 , L. monocytogenes mutants with deletions of actA, inlA, inlB, inlAB, plcA, and plcB resembled their

135 ActA is a bacterially encoded protein that enables Liste

136 We also present observations indicating that ActA is a natively unfolded protein, largely random coil

137 n vitro, the actin monomer-binding region of ActA is critical for stimulating Arp2/3-dependent actin

138 binds ActA but not VASP; however, binding to ActA is greater in the presence of VASP.

139 mal activity at saturating concentrations of ActA is identical to the most active domains of the WASP

140 olar lysis and entry into the cytosol, while ActA is required for bacterial spread to adjacent cells.

141 coated with a fluid lipid bilayer rendering ActA laterally mobile, beads predominantly migrated with

142 th, and this finding correlated with LLO and ActA levels detectable in broth cultures.

143 tion of oligoproline sequences in ActA or an ActA-like host protein to induce host cell actin assembl

144 odel in which proteolysis unmasks vinculin's ActA-like oligoproline sequence.

145 cells, such as hepatocytes, and the indirect ActA-mediated infection by cell-to-cell spread from adja

146 The Listeria monocytogenes surface protein ActA mediates actin-based motility by interacting with a

147 ins of CD2AP fused to Listeria monocytogenes ActA mitochondria-targeting sequence) inhibited REF52 ce

148 ActA dimer and provide evidence that the two ActA molecules do not interact with each other even when

149 the close packing ( approximately 19 nm) of ActA molecules on the surface of L. monocytogenes is so

150 s were transformed into the L. monocytogenes actA mutant DP-L1942.

151 y of the glcV mutant compared to an isogenic actA mutant reference strain was next tested in an exper

152 Surprisingly, Listeria ActA mutant strains lacking the putative phosphoinositid

153 although, in fetal infection, the number of ActA- mutant bacteria was 100-fold lower, compared with

154 The ActA- mutant, which is impaired in cell-to-cell spread a

155 s shared by other immunogenic mutants (e.g., actA mutants), our glcV mutant was tested for vaccine ef

156 hly promoter (h30) or linked in frame to the ActA N-terminal 100 amino acids and driven by the actA p

157 By chemical cross-linking, ActA, N-WASP, and Scar1 contact the same three subunits

158 d oral colonization with one of the mutants, actA-negative (DeltaactA) L. monocytogenes, to restrict

159 roinjection of a peptide matching the second ActA oligoproline repeat (FEFPPPPTDE) stops Listeria loc

160 monocytogenes requires polar distribution of ActA on its surface to move.

161 207-238 strain displayed increased levels of ActA on the bacterial surface in protrusions.

162 eltampl strain displayed increased levels of ActA on the bacterial surface in protrusions.

163 ytosolic mutants revealed that all expressed ActA on their cell surface and formed actin tails with a

164 ASP recognition of oligoproline sequences in ActA or an ActA-like host protein to induce host cell ac

165 the Bnip3 transmembrane domain with that of Acta or cytochrome b(5).

166 brane domains from the mitochondrial protein ActA or the endoplasmic reticulum protein cytochrome b5.

167 been given to the surface environment where ActA performs its pivotal role in bacterial actin-based

168 truction of a transcriptional fusion between actA-plcB and the green fluorescent protein gene of Aequ

169 This dissemination process relies on the mlp-actA-plcB operon, which encodes ActA, a bacterial nuclea

170 stream mpl gene via the generation of an mpl-actA-plcB transcript.

171 ape from host cell vacuoles, did not express actA/plcB at detectable levels within infected tissue cu

172 actA/plcB expression began approximately 30 min postinfe

173 ated the detailed examination of patterns of actA/plcB expression within infected tissue culture cell

174 teria into the host cytoplasm and subsequent actA/plcB expression.

175 We have directly examined the de novo ActA polarization process in vitro by using an ActA-RFP

176 nt with our in vitro observations of de novo ActA polarization.

177 ape, the metalloprotease Mpl is required for ActA processing and protrusion resolution.

178 interacting peptides and found that, as with ActA, proline-rich sequences were the sole zyxin sequenc

179 eterologous dal gene tightly regulated by an actA-promoted resolvase recombination system.

180 N-terminal 100 amino acids and driven by the actA promoter (a30).

181 The actA promoter is dependent upon a regulatory factor know

182 n broth-grown cultures of both wild-type and actA promoter mutant strains, but the levels of inductio

183 a high-affinity PrfA binding site within the actA promoter.

184 or the activation and binding of PrfA to the actA promoter.

185 The Listeria monocytogenes ActA protein acts as a scaffold to assemble and activate

186 Polystyrene beads coated with purified ActA protein can undergo directional movement in an acti

187 These results indicate that the ActA protein directs at least three separable events: (1

188 The Listeria monocytogenes ActA protein induces actin-based motility by enhancing t

189 The ActA protein is an essential determinant of pathogenicit

190 The ActA protein is responsible for the actin-based movement

191 The Listeria monocytogenes ActA protein mediates actin-based motility by recruiting

192 s coated uniformly with the L. monocytogenes ActA protein migrated equally well in either of two dist

193 The ActA protein of Listeria monocytogenes is an essential v

194 t is similar to the C-terminal domain in the ActA protein of the bacteria, Listeria monocytogenes.

195 ation is associated with polarization of the ActA protein on the fluid vesicle surface, which may rei

196 The polar distribution of the ActA protein on the surface of the Gram-positive intrace

197 Once in the cytosol, the L. monocytogenes ActA protein recruits host cell Arp2/3 complexes and ena

198 factor that promoted the ability of Listeria ActA protein to activate the Arp2/3 complex to trigger a

199 of the variable surface distribution of the ActA protein to initiation and steady-state movement.

200 L. monocytogenes mutants lacking the ActA protein, which is essential for intracellular movem

201 the bacterial cell surface by the listerial ActA protein.

202 oline-rich repeat region of L. monocytogenes ActA protein.

203 xpression was found to be dependent upon the actA proximal promoter; the mpl promoter appeared to con

204 of L. monocytogenes must be due to polarized ActA rather than intrinsic actin network forces.

205 l junction assembly through the VASP-binding ActA repeat region.

206 triction of bacteria lacking PlcA, PlcB, and ActA required FIP200 and TBK1, both involved in the engu

207 The minimal Arp2/3-binding site of ActA (residues 144-170) is C-terminal to both actin-bind

208 Here we show that two domains of ActA (residues 85-104 and 121-138) with sequence similar

209 in O (LLO) and ActA, the products of hly and actA, respectively, to establish a productive intracellu

210 and 38 alleles were identified for hlyA and actA, respectively.

211 Importantly, introduction of exogenous rh-ActA revealed an intrinsic ovarian quorum sensing mechan

212 tA polarization process in vitro by using an ActA-RFP (red fluorescent protein) fusion.

213 actA, ribC, and purM demonstrated the highest levels of

214 d suggest that the actin-binding sequence of ActA spans 40 amino acids.

215 ActA spans both the bacterial membrane and the peptidogl

216 These data suggest that ActA stimulates the Arp2/3 complex by both VASP-dependen

217 isteria monocytogenes requires the bacterial ActA surface protein and the host cell Arp2/3 complex.

218 The Listeria surface protein ActA synergises with recruited host proteins to induce a

219 wever, when combined, the Arp2/3 complex and ActA synergistically stimulated the nucleation of actin

220 strated approximately 70-fold more cytosolic ActA than cytosolic LLO.

221 ther, while the lower level of production of ActA than of LLO in broth can be accounted for by transc

222 a peptide derived from the Listeria protein ActA that undergoes a random coil to helix transition up

223 gy, several genes were identified, including actA, that exhibited such an expression profile.

224 cytogenes requires listeriolysin O (LLO) and ActA, the products of hly and actA, respectively, to est

225 actA, the protein product of which is required for cell-

226 in lacks the oligoproline sequences found in ActA, the surface protein required for locomotion of the

227 All act genes, actA to actE, are expressed together and constitute an o

228 tosol, WT L. monocytogenes utilized PLCs and ActA to avoid subsequent xenophagy.

229 ent with the empirical data, the k(A) for rh-ActA-treated was twice that of vehicle-treated animals.

230 day 19 were also derived for vehicle and rh-ActA treatment conditions.

231 the tightly bound bacterial surface protein ActA uses its multiple oligoproline registers [consensus

232 ctin dynamics and motility of live bacteria, ActA was fused to a monomeric red fluorescent protein (m

233 n comparison to induction in broth cultures, actA was highly induced (226-fold) and hly was moderatel

234 rene beads coated with the bacterial protein ActA, we have systematically varied a series of biophysi

235 The expression of actA, whose protein product is required for L. monocytog