ライフサイエンスコーパス: PGRP

1 PGRP had no tumor necrosis factor-like cytotoxicity for

2 PGRP inhibited phagocytosis of Gram-positive bacteria by

3 PGRP mRNA and protein were expressed in neutrophils and

4 PGRP was not a PGN-lytic or a bacteriolytic enzyme, but

5 PGRP-induced killing depended on the production of hydro

6 PGRP-L has no direct bacteriolytic activity.

7 PGRP-L is expressed in liver, PGRP-Ialpha and PGRP-Ibeta

8 PGRP-L, PGRP-Ialpha, and PGRP-Ibeta have 576, 341, and 3

9 PGRP-LC, PGRP-LE, and Imd each contain a motif with some

10 PGRP-LE, a cytosolic innate immune sensor in Drosophila,

11 PGRP-S is located with other antimicrobial proteins, suc

12 PGRP-S-/- mice have normal inflammatory responses and pr

13 PGRP-SA binding depended on the polymerization status of

14 PGRP-SC1a mutants also fail to activate the Toll/NF-kapp

15 PGRPs also bind the outer membrane of Escherichia coli a

16 PGRPs bind peptidoglycan, a ubiquitous component of bact

17 e report that a PGRP gene, BtPGRP, encodes a PGRP from the whitefly Bemisia tabaci (MEAM1) that binds

18 against infections in fish embryos and for a PGRP protein for survival in vertebrates.

19 of PGRP-S based on the known structure of a PGRP-Ialpha-PGN complex, we identified potential PGN-bin

20 signaling and the first known function of a PGRP-type receptor in the nervous system of any organism

21 Here, we report that a PGRP gene, BtPGRP, encodes a PGRP from the whitefly Bemi

22 f key PGN-contacting residues shows that all PGRPs employ this basic PGN-binding mode.

23 dues and interactions suggest that, although PGRPs may engage PGNs in a similar mode, structural diff

24 nd for an N-acetylmuramoyl-l-alanine amidase PGRP that cleaves peptidoglycan at the lactylamide bond

25 Consistent with sequence analysis, PGRP-SA does not contain the canonical zinc-binding resi

26 conformational differences between free and PGRP-bound PGN with respect to the relative orientation

27 t the physical interaction between GNBP1 and PGRP-SA using recombinant proteins.

28 GRP-L is expressed in liver, PGRP-Ialpha and PGRP-Ibeta in esophagus (and to a lesser extent in tonsi

29 ptidoglycan derivatives with PGRP-Ialpha and PGRP-S have been studied in real-time using surface plas

30 PGRP-L, PGRP-Ialpha, and PGRP-Ibeta have 576, 341, and 373 amino acids coded by f

31 novel human PGRPs (PGRP-L, PGRP-Ialpha, and PGRP-Ibeta) that together with the previously cloned PGR

32 an PGRP family, PGRP-Ialpha, PGRP-Ibeta, and PGRP-S, do not have the amidase activity.

33 issue-specific roles of PGRP-LC isoforms and PGRP-LE in the antibacterial response.

34 ther PGRPs, including Drosophila PGRP-LB and PGRP-SA and human PGRP-Ialpha.

35 Our results reveal that both PGRP-LC and PGRP-LE contribute to the intestinal immune response, wi

36 Instead, PGRP-LC and PGRP-LE signaled through a receptor-interacting protein

37 is recognized by two receptors, PGRP-LC and PGRP-LE, and activates a homolog of transcription factor

38 eptidoglycan binds the receptors PGRP-LC and PGRP-LE, which through interaction with the adaptor prot

39 complex with the ectodomains of PGRP-LCa and PGRP-LCx shows that TCT is bound to and presented by the

40 synergistic with lysozyme, and lysozyme and PGRP-S colocalize in neutrophil extracellular traps (NET

41 m-positive bacteria with unmodified PGN, and PGRP did not bind to other cell wall components or Gram-

42 an recognition proteins (PGRPs) PGRP-SB2 and PGRP-SC2 were selected for further study based on differ

43 n occurring between two genes, PGRP-SC1A and PGRP-SC1B.

44 iers of the Abeta phenotype, namely Sod3 and PGRP-SC1b.

45 a lesser extent in tonsils and thymus), and PGRP-S in bone marrow (and to a lesser extent in neutrop

46 Constitutive activation of Toll and PGRP-LC/IMD could mimic the synergistic stimulation.

47 absence bacterial virulence is impaired, as PGRPs can directly recognize leftover peptidoglycan exte

48 Bactericidal PGRP induced a rapid decrease in respiration, which sugg

49 ion of monomeric peptidoglycan involves both PGRP-LCa and -LCx.

50 Our results reveal that both PGRP-LC and PGRP-LE contribute to the intestinal immune

51 When both PGRP-LB and IMD immunity pathway functions are blocked,

52 Whereas both PGRP-S and lysozyme recognize PGN, the exact binding spe

53 recognition proteins (PGRPs), membrane-bound PGRP-LC and secreted/cytosolic PGRP-LE, which relay diam

54 Bovine PGRP-S can mediate direct lysis of heat-killed bacteria;

55 ng, and antimicrobial activities of a bovine PGRP ortholog termed bovine oligosaccharide-binding prot

56 mice, we demonstrate little contribution by PGRP-L to systemic challenge using gram-negative bacteri

57 The minimum PGN fragment hydrolyzed by PGRP-L is MurNAc-tripeptide.

58 Thus, only bacterial recognition by PGRP-S, but not its effector function, is conserved from

59 idoglycan fragment that can be recognized by PGRP-Ialpha.

60 ow a combination of extracellular sensing by PGRP-LC isoforms and intracellular sensing through PGRP-

61 esents a processed form of PG for sensing by PGRP-SA and that a tripartite interaction between these

62 to be essential for specific recognition by PGRPs.

63 d that PGN, GlcNAc, and MurNAc bind to camel PGRP-S (CPGRP-S) with affinities corresponding to dissoc

64 l homology between recognition and catalytic PGRPs.

65 cal zinc-binding residues found in catalytic PGRPs.

66 lifespan of metazoans and identify SC-class PGRPs as longevity-promoting factors.

67 ta) that together with the previously cloned PGRP-S, define a new family of human pattern recognition

68 nism for PGN hydrolysis by Zn(2+)-containing PGRPs.

69 By contrast, PGRP-induced thiol stress (depletion of thiols) and meta

70 the "active" configuration does not convert PGRP-S into an active amidase.

71 Using gene targeting to create PGRP-L-deficient mice, we demonstrate little contributio

72 sponse, with a predominant role of cytosolic PGRP-LE in the midgut, the central section of endodermal

73 embrane-bound PGRP-LC and secreted/cytosolic PGRP-LE, which relay diaminopimelic acid (DAP)-type pept

74 an recognition protein LC/immune deficiency (PGRP-LC/IMD) signaling pathways.

75 tertiary granules and that PGRP-S-deficient (PGRP-S-/-) mice have increased susceptibility to intrape

76 infection in vivo, and an ectodomain-deleted PGRP-LC lacking the PGRP domain is an active receptor.

77 infection in vivo, and an ectodomain-deleted PGRP-LC lacking the PGRP domain is an active receptor.

78 formation of heterodimers between different PGRP-LC isoforms, thereby potentially expanding the dive

79 d polymeric peptidoglycan required different PGRP-LC splice isoforms, while lipid A recognition requi

80 In Drosophila, distinct PGRPs bind to peptidoglycans on gram-positive or gram-ne

81 Downregulating PGRP-SB2 selectively in the fat body protected animals f

82 cts of overnutrition, whereas downregulating PGRP-SC2 produced InR-like phenotypes.

83 Drosophila PGRP-SA is a member of this family of pattern recognitio

84 Comparison with the catalytic Drosophila PGRP-LB reveals an overall structure conservation with a

85 to that of other PGRPs, including Drosophila PGRP-LB and PGRP-SA and human PGRP-Ialpha.

86 like the mammalian CD14 molecule, to enhance PGRP-LC-mediated peptidoglycan recognition on the cell s

87 ermore, totem mutants, which fail to express PGRP-LC, are susceptible to Gram-negative (E. coli), but

88 oglycan pattern recognition receptor family (PGRP-LC), is required for the induction and sustained ex

89 The other members of the human PGRP family, PGRP-Ialpha, PGRP-Ibeta, and PGRP-S, do not have the ami

90 t to its critical role in immunity in flies, PGRP-L is largely dispensable for mammalian immunity aga

91 elic acid as the specificity determinant for PGRP interaction.

92 e imd signaling protein was not required for PGRP-LC signaling.

93 d peptidoglycan on the bacterial surface for PGRP-SC1a mediated phagocytosis.

94 Four PGRPs, PGRP-L, -S, -Ialpha, and -Ibeta, are expressed fr

95 appear to be generated from ciliated Foxj1(+)PGRP-S(+) cells, indicative of a possible precommitted p

96 Peritoneal macrophages from PGRP-L-deficient mice produced decreased amounts of the

97 Neutrophils from PGRP-S-/- mice have normal phagocytic uptake of bacteria

98 ven peptidoglycan recognition protein genes (PGRPs) from 12 lines of Drosophila melanogaster and one

99 gene conversion occurring between two genes, PGRP-SC1A and PGRP-SC1B.

100 Where and how PGRPs act in vivo is not yet clear.

101 rect lysis of heat-killed bacteria; however, PGRP-S-mediated killing of bacteria is independent of th

102 ing Drosophila PGRP-LB and PGRP-SA and human PGRP-Ialpha.

103 In conclusion, human PGRP-L is an N-acetylmuramoyl-l-alanine amidase and this

104 f the C-terminal PGN-binding domain of human PGRP-I beta in complex with NAG-NAM-L-Ala-gamma-D-Glu-L-

105 f the C-terminal PGN-binding domain of human PGRP-Ialpha in complex with a muramyl tripeptide represe

106 f the C-terminal PGN-binding domain of human PGRP-Ialpha in two oligomeric states, monomer and dimer,

107 is present in the PGN-binding site of human PGRP-Ialpha.

108 e, we present the crystal structure of human PGRP-S at 1.70A resolution.

109 PGN, the exact binding specificity of human PGRP-S, its functional activity, and its potential syner

110 We report that human PGRP-L is a Zn2+-dependent N-acetylmuramoyl-l-alanine am

111 Here we show that human PGRP-S binds to and inhibits the growth of Staphylococcu

112 together, these results indicate that human PGRP-S plays a role in innate immunity in the context of

113 The other members of the human PGRP family, PGRP-Ialpha, PGRP-Ibeta, and PGRP-S, do not

114 All four human PGRPs bind peptidoglycan and Gram-positive bacteria.

115 We report cloning of three novel human PGRPs (PGRP-L, PGRP-Ialpha, and PGRP-Ibeta) that togethe

116 hts into the bactericidal mechanism of human PGRPs.

117 mbers of the human PGRP family, PGRP-Ialpha, PGRP-Ibeta, and PGRP-S, do not have the amidase activity

118 These porcine isoforms share identical PGRP domains at their C terminus, which are highly conse

119 The Zn2+ binding amino acids (conserved in PGRP-L and T7 amidase) and Cys-419 (not conserved in T7

120 proteins, is less hydrophobic and deeper in PGRP-S than in PGRP-IalphaC, whose PGRP-specific segment

121 ion of the catalytic water molecule found in PGRP-LB, tantalizingly suggests some hydrolytic function

122 identified potential PGN-binding residues in PGRP-S.

123 ess hydrophobic and deeper in PGRP-S than in PGRP-IalphaC, whose PGRP-specific segments vary consider

124 All mammalian and insect PGRPs have at least three highly conserved C-terminal PG

125 In insects PGRPs activate antimicrobial pathways in the hemolymph a

126 In insects, PGRP recognizes bacterial cell wall peptidoglycan (PGN)

127 Instead, PGRP-LC and PGRP-LE signaled through a receptor-interact

128 an-docking groove present in all other known PGRP structures.

129 PGRP-L, PGRP-Ialpha, and PGRP-Ibeta have 576, 341, and 373 amino

130 cloning of three novel human PGRPs (PGRP-L, PGRP-Ialpha, and PGRP-Ibeta) that together with the prev

131 ophila peptidoglycan recognition protein LC (PGRP-LC), a transmembrane protein required for the respo

132 eptor, Peptidoglycan recognition protein LC (PGRP-LC), is involved in phagocytosis of Gram-negative b

133 PGRP-LC, PGRP-LE, and Imd each contain a motif with some resembla

134 The peptidoglycan-recognition protein LCa (PGRP-LCa) is a transmembrane receptor required for activ

135 We also show that full-length PGRP-Ialpha comprises two tandem PGN-binding domains.

136 Here we show that full-length PGRP-LE acted as an intracellular receptor for monomeric

137 PGRP-L is expressed in liver, PGRP-Ialpha and PGRP-Ibeta in esophagus (and to a lesser

138 Therefore, mammalian PGRP binds to PGN and Gram-positive bacteria with nanomo

139 Therefore, mammalian PGRP-S functions in intracellular killing of bacteria.

140 Mammalian PGRPs do not have a single antimicrobial activity agains

141 ely little is known about the four mammalian PGRPs.

142 Larvae that receive less maternal PGRP-LB give rise to adults with fewer Wigglesworthia an

143 ect evidence that the longest family member, PGRP-L, is a secreted serum protein with the capacity to

144 Using Immunogold electron microscopy, PGRP-S was localized to the dense/large granules of naiv

145 ggesting a possible mechanism for modulating PGRP activity through the formation of multivalent adduc

146 Mouse PGRP bound to PGN with fast kinetics and nanomolar affin

147 We show that mouse PGRP-S is present in neutrophil tertiary granules and th

148 ype or a noncatalytic cysteine-serine mutant PGRP-SC1a, we find that PGRP-SC1a amidase activity is no

149 ents may mediate the antimicrobial action of PGRP family members.

150 d and sufficient for the amidase activity of PGRP-L, although its activity (in the N-terminal delta1-

151 se) are required for the amidase activity of PGRP-L, whereas three other amino acids, needed for the

152 midase, are not required for the activity of PGRP-L.

153 affinity and thus antimicrobial activity of PGRP-S is determined by the third amino acid in the PGN

154 The deficient binding of PGRP-LCa to monomeric peptidoglycan was confirmed by bio

155 In the case of PGRP-LC, differential splicing of PGRP domain-encoding e

156 g a PGN ligand into the PGN-binding cleft of PGRP-S based on the known structure of a PGRP-Ialpha-PGN

157 We also highlight the contribution of PGRP-LCa/x heterodimers to the systemic immune response

158 required for the proper hormonal control of PGRP-LC expression.

159 demonstrate sodium-dependent dimerization of PGRP-Ialpha in solution, suggesting a possible mechanism

160 Dimerization of PGRP-Ialpha, which occurs through three-dimensional doma

161 peptidoglycan to the extracellular domain of PGRP-LC activates intracellular signaling because its cy

162 d the crystal structure of the ectodomain of PGRP-LCa at 2.5-A resolution and found two unique helica

163 bound to and presented by the ectodomain of PGRP-LCx.

164 on of TCT in complex with the ectodomains of PGRP-LCa and PGRP-LCx shows that TCT is bound to and pre

165 Furthermore, the antimicrobial effect of PGRP-S against E coli is synergistic with lysozyme, and

166 f this study was to identify the function of PGRP in mammals.

167 monitored through the receptor integrity of PGRP-LC after host and pathogen are engaged via pattern

168 monitored through the receptor integrity of PGRP-LC after host and pathogen are engaged via pattern

169 te fly lines expressing specific isoforms of PGRP-LC and assessed the tissue-specific roles of PGRP-L

170 es, pointing to constraints in the number of PGRP-SA molecules bound for signaling initiation.

171 Infection-induced proteolysis of PGRP-LC controls the IMD activation and melanization cas

172 Reduction of PGRP-LB experimentally diminishes female fecundity and d

173 The C-terminal region of PGRP-L, homologous to bacteriophage and bacterial amidas

174 irreversible cleavage or down-regulation of PGRP-LC may provide an additional cue for the host to di

175 irreversible cleavage or down-regulation of PGRP-LC may provide an additional cue for the host to di

176 component system was a negative regulator of PGRP-induced oxidative stress.

177 in vivo studies demonstrate the key role of PGRP-LCx in sensing DAP-type peptidoglycan-containing Gr

178 LC and assessed the tissue-specific roles of PGRP-LC isoforms and PGRP-LE in the antibacterial respon

179 he case of PGRP-LC, differential splicing of PGRP domain-encoding exons to a common intracellular dom

180 recently reported x-ray crystal structure of PGRP-Ialpha with the lysine-containing muramyltripeptide

181 The overall structure of PGRP-S, which participates in intracellular killing of G

182 We report here the crystal structure of PGRP-SA at 1.56 A resolution, which represents the first

183 e rPGRP-LC, an alternative splice variant of PGRP-LC that selectively dampens immune response activat

184 onomeric peptidoglycan, whereas a version of PGRP-LE containing only the PGRP domain functioned extra

185 We asked what the functions of PGRPs in fish are and whether they are indispensable for

186 ter understand the bactericidal mechanism of PGRPs, we determined the crystal structure of the C-term

187 To pinpoint the site of PGRPs that mediates discrimination, we engineered struct

188 re, we describe recent structural studies of PGRPs that reveal the basis for PGN recognition and prov

189 In mammals one PGRP is an antibacterial neutrophil protein.

190 tidoglycan-docking groove conserved in other PGRPs.

191 sitive bacteria, is similar to that of other PGRPs, including Drosophila PGRP-LB and PGRP-SA and huma

192 e report cloning of three novel human PGRPs (PGRP-L, PGRP-Ialpha, and PGRP-Ibeta) that together with

193 e peptidoglycan recognition proteins (PGRPs) PGRP-SB2 and PGRP-SC2 were selected for further study ba

194 Four PGRPs, PGRP-L, -S, -Ialpha, and -Ibeta, are expressed from thre

195 acterization of two long isoforms of porcine PGRP.

196 ctively, these findings suggest that porcine PGRPs are involved in antimicrobial peptide expression.

197 f the Drosophila pattern recognition protein PGRP-LCx induces DIAP2-dependent polyubiquitylation of t

198 o known as peptidoglycan recognition protein PGRP-S, PGLYRP1), an innate immunity protein, interacts

199 Peptidoglycan recognition protein (PGRP) is conserved from insects to mammals.

200 t affects peptidoglycan recognition protein (PGRP) SC1a and impairs the ability to phagocytose the ba

201 a-la) and peptidoglycan recognition protein (PGRP) were not detected while camel serum albumin (CSA)

202 action of peptidoglycan recognition protein (PGRP)-Ialpha with the lysine-containing muramyl pentapep

203 a tsetse peptidoglycan recognition protein (PGRP-LB) is crucial for symbiotic tolerance and trypanos

204 the host Peptidoglycan Recognition Protein (PGRP-LB) is expressed only in adults and is a major comp

205 -spanning peptidoglycan recognition protein, PGRP-LC, functions as the receptor for the IMD pathway.

206 -spanning peptidoglycan recognition protein, PGRP-LC, functions as the receptor for the IMD pathway.

207 ow that a peptidoglycan recognition protein, PGRP-LC, is absolutely required for the induction of ant

208 Peptidoglycan recognition proteins (PGRPs or PGLYRPs) are pattern recognition molecules that

209 ave four peptidoglycan recognition proteins (PGRPs or PGLYRPs), which are secreted innate immunity pa

210 Peptidoglycan recognition proteins (PGRPs) are a group of newly identified proteins with eme

211 The peptidoglycan recognition proteins (PGRPs) are a large group of proteins found in insects an

212 Peptidoglycan recognition proteins (PGRPs) are highly conserved pattern-recognition molecule

213 Peptidoglycan recognition proteins (PGRPs) are multifunctional pattern recognition proteins.

214 Peptidoglycan recognition proteins (PGRPs) are pattern recognition molecules coded by up to

215 Peptidoglycan (PGN) recognition proteins (PGRPs) are pattern recognition molecules of innate immun

216 Peptidoglycan recognition proteins (PGRPs) are pattern recognition receptors of the innate i

217 Peptidoglycan recognition proteins (PGRPs) are pattern recognition receptors of the innate i

218 Peptidoglycan (PGN) recognition proteins (PGRPs) are pattern-recognition receptors of the innate i

219 Peptidoglycan recognition proteins (PGRPs) are structurally conserved through evolution, but

220 Peptidoglycan recognition proteins (PGRPs) constitute a family of innate immune recognition

221 Peptidoglycan recognition proteins (PGRPs) constitute a recently characterized family of pat

222 Peptidoglycan recognition proteins (PGRPs) form a recently discovered protein family, which

223 ammalian Peptidoglycan Recognition Proteins (PGRPs) kill both Gram-positive and Gram-negative bacteri

224 ors, the peptidoglycan recognition proteins (PGRPs) LCa and LCx, which activates the immune deficienc

225 ition by peptidoglycan recognition proteins (PGRPs) of the host.

226 The peptidoglycan recognition proteins (PGRPs) PGRP-SB2 and PGRP-SC2 were selected for further s

227 ly of 12 peptidoglycan recognition proteins (PGRPs) that recognize peptidoglycan, a ubiquitous compon

228 via two peptidoglycan recognition proteins (PGRPs), membrane-bound PGRP-LC and secreted/cytosolic PG

229 ammalian peptidoglycan recognition proteins (PGRPs), similar to antimicrobial lectins, bind the bacte

230 ins, and peptidoglycan recognition proteins (PGRPs).

231 d insect peptidoglycan recognition proteins (PGRPs).

232 osophila peptidoglycan recognition proteins (PGRPs).

233 eria using the single peptidoglycan receptor PGRP-LC is unknown.

234 pression of the pattern recognition receptor PGRP-LC in Drosophila, thereby tightly regulating innate

235 In this article, we show that the receptor PGRP-LC is down-regulated in response to Salmonella/Esch

236 In this article, we show that the receptor PGRP-LC is down-regulated in response to Salmonella/Esch

237 We show that the receptor PGRP-LC regulates and integrates two host defense system

238 We show that the receptor PGRP-LC regulates and integrates two host defense system

239 gram-negative peptidoglycan and the receptor PGRP-LC.

240 rolytic function for this member of receptor PGRPs.

241 acid-type peptidoglycan binds the receptors PGRP-LC and PGRP-LE, which through interaction with the

242 ve bacteria, is recognized by two receptors, PGRP-LC and PGRP-LE, and activates a homolog of transcri

243 resents the first example of a "recognition" PGRP.

244 Restoring PGRP-SC2 expression in enterocytes of the intestinal epi

245 on of a peptidoglycan recognition protein-S (PGRP-S) transgene reporter.

246 Insect peptidoglycan recognition protein-S (PGRP-S), a member of a family of innate immunity pattern

247 1) and peptidoglycan recognition protein SA (PGRP-SA).

248 on of peptidoglycan recognition protein SC2 (PGRP-SC2), a negative regulator of IMD/Relish innate imm

249 studies demonstrate that neutrophils secrete PGRP-S when exposed to bacteria.

250 In Bacillus subtilis, PGRPs activate the CssR-CssS two-component system that d

251 Surprisingly, PGRP-S derived significantly higher affinities for the D

252 e at least three highly conserved C-terminal PGRP domains located either in the extracellular or in t

253 ent in neutrophil tertiary granules and that PGRP-S-deficient (PGRP-S-/-) mice have increased suscept

254 Here, we demonstrate that PGRP-LC binds Imd and that its cytoplasmic domain is cri

255 Our results demonstrate that PGRP-LC is an essential component for recognition and si

256 steine-serine mutant PGRP-SC1a, we find that PGRP-SC1a amidase activity is not necessary for Toll sig

257 reports, Iatsenko et al. (2016) reveal that PGRP-SD regulates the Imd signaling pathway rather than

258 Here we show that PGRP-LC is important for antibacterial peptide synthesis

259 ges in these bacteria, our data suggest that PGRP-SC1a is necessary for recognition of the Lys-type p

260 s critical for its activity, suggesting that PGRP-LC acts as a signal-transducing receptor.

261 induction of immune response, suggests that PGRP-LCa recognizes the exposed structural features of a

262 The structure reveals that PGRPs exhibit extensive topological variability in a lar

263 We show that PGRPs enter the Gram-positive cell wall at the site of d

264 The PGRP-LC cytoplasmic domain can mediate formation of hete

265 The PGRP-LC cytoplasmic domain is also essential for the for

266 PGN-binding site and a groove formed by the PGRP-specific segment on the opposite face of the molecu

267 nd an ectodomain-deleted PGRP-LC lacking the PGRP domain is an active receptor.

268 nd an ectodomain-deleted PGRP-LC lacking the PGRP domain is an active receptor.

269 The plasticity of the PGRP-binding site revealed by these mutants suggests an

270 eas a version of PGRP-LE containing only the PGRP domain functioned extracellularly, like the mammali

271 ligand) and gram-negative peptidoglycan (the PGRP-LC ligand) together caused synergistic activation o

272 molecules challenges the assumption that the PGRP family of proteins recapitulates the evolution of T

273 Furthermore, we find that the PGRP-SC1a amidase activity can be substituted by exogeno

274 ric peptidoglycan (DAP-type PGN) through the PGRP ectodomain.

275 ric peptidoglycan (DAP-type PGN) through the PGRP ectodomain.

276 he developing zebrafish embryo, one of these PGRPs is essential for defense and survival during bacte

277 Thus, these PGRPs may play a role in recognition of bacteria in thes

278 However, comparison with these PGRPs reveals important differences in both the PGN-bind

279 C isoforms and intracellular sensing through PGRP-LE provides sophisticated mechanisms to detect and

280 Thus, PGRP-LB plays a pivotal role in tsetse's fitness by prot

281 Thus, PGRP-LC is a candidate receptor for retrograde, trans-sy

282 sulted in increased resistance of E. coli to PGRP killing.

283 In contrast to PGRPs with PGN-lytic amidase activity, no zinc ion is pr

284 In addition, tsetse PGRP-LB may have an anti-protozoal activity that confers

285 resence of conserved amidase domains, tsetse PGRP-LB may scavenge the peptidoglycan (PGN) released by

286 glycopeptide antibiotics (e.g., vancomycin), PGRPs kill bacteria by directly interacting with their c

287 Various PGRPs are reported to have diverse functions: they bind

288 e central section of endodermal origin where PGRP-LE is enriched.

289 sensing of tracheal cytotoxin (TCT), whereas PGRP-LCy may have a minor role in antagonizing the immun

290 However, metabolic pathways through which PGRPs induce these bactericidal stress responses are unk

291 lyze Gram-positive peptidoglycan (PG), while PGRP-SA bound highly purified PG fragments (muropeptides

292 deeper in PGRP-S than in PGRP-IalphaC, whose PGRP-specific segments vary considerably in amino acid s

293 The amidase activity associated with PGRP-LB may scavenge the symbiotic peptidoglycan and pre

294 of synthetic peptidoglycan derivatives with PGRP-Ialpha and PGRP-S have been studied in real-time us

295 However, only the interaction of PGN with PGRPs, which are highly conserved from insects to mammal

296 Zebrafish PGRPs have both peptidoglycan-lytic amidase activity and

297 We identified and cloned three zebrafish PGRPs and showed that they are highly expressed in eggs,