ライフサイエンスコーパス: procapsid

1 d substantially in the context of the entire procapsid.

2 emeric DNA is cut and inserted into an empty procapsid.

3 nslocated by the packaging motor to fill the procapsid.

4 domain is to translocate the genome into the procapsid.

5 g of double-stranded DNA into a preassembled procapsid.

6 into a precursor capsid, referred to as the procapsid.

7 to translocate genomic DNA into a preformed procapsid.

8 rtion into a preformed capsid structure, the procapsid.

9 -6.1(+/-0.2)kcal/mol to the stability of the procapsid.

10 present on the initial capsid assembly, the procapsid.

11 ffected the morphology of the prolate-shaped procapsid.

12 sid much more strongly than to the pRNA-free procapsid.

13 that most likely form the pores in the viral procapsid.

14 iven motor translocates DNA into a preformed procapsid.

15 or "packaging" of viral DNA into a preformed procapsid.

16 NA into a preformed protein shell called the procapsid.

17 er in the icosahedral asymmetric unit of the procapsid.

18 tein P1, the major structural protein of the procapsid.

19 utilizing an intermediate capsid, known as a procapsid.

20 e complex analyzed in the absence of DNA and procapsid.

21 ing the assembly of an intermediate called a procapsid.

22 (CTS) directs virtually any protein into the procapsid.

23 gle-stranded RNA genomic precursors into the procapsid.

24 s binding sites for the motor ATPase and the procapsid.

25 ubunit prior to DNA translocation into viral procapsid.

26 association of 12 pentameric particles into procapsids.

27 n D organizes 12 of these intermediates into procapsids.

28 f scaffolding protein in solution and within procapsids.

29 rminally processed in both 80alpha and SaPI1 procapsids.

30 bute from the partial capsids and form whole procapsids.

31 ere mixed in varying ratios in vitro to form procapsids.

32 ere is a correspondingly low yield of proper procapsids.

33 the assembly of coat protein pentamers into procapsids.

34 induced by heat or chemical treatment of P22 procapsids.

35 r DNA can be packaged in vitro into purified procapsids.

36 In the phiX174 procapsid, 240 external scaffolding proteins form a nonq

37 The procapsid, a compact icosahedrally symmetric particle wi

38 ate in the assembly of the P22 virion is the procapsid, a preformed protein shell into which the vira

39 ze 12 pentameric assembly intermediates into procapsids, a reaction reconstituted in vitro In previou

40 To make procapsids accessible to live-cell imaging, we made a se

41 ging motor transports the viral DNA into the procapsid against a pressure difference of up to 40 +/-

42 nd pRNA, transports the viral DNA inside the procapsid against pressure differences of up to approxim

43 Packaging the viral genome into empty procapsids, an essential event in the life cycle of tail

44 particles have been characterized as a 480-A procapsid and a 410-A capsid, both with T=4 quasisymmetr

45 Here the authors present the CVA6 procapsid and A-particle cryo-EM structures and identify

46 lation of two forms of stable CVA6 particles-procapsid and A-particle-with excellent biochemical stab

47 ing protein, which forms inner shells in the procapsid and B capsid, is exceptionally bubbling-prone.

48 7.0 (XR(7.0)), to establish (1) how and why procapsid and capsid structures differ, (2) why lowering

49 as intermediate in size between those of the procapsid and capsid; one near the cleavage site exhibit

50 g machines that translocate viral DNA into a procapsid and compact it to near-crystalline density.

51 had an open flower-like conformation for the procapsid and genome-filled capsids, whereas the putativ

52 we report Calpha backbone models for the P22 procapsid and infectious virion derived from electron cr

53 bacteriophage P22 portal protein in both the procapsid and mature capsid conformations.

54 procapsid is enzymatically active within the procapsid and recircularizes linear plasmid DNA containi

55 otein forms thick-walled inner shells in the procapsid and the B capsid.

56 Unlike the phiX174 "closed" procapsid and the infectious virion, the alpha3 open pro

57 struction to determine the structures of the procapsid and the mature capsid of 80alpha, a bacterioph

58 directly across from each other both in the procapsid and the mature virion, suggesting their import

59 Comparison of the procapsid and the virion backbone models reveals coordin

60 conformational differences between the EV71 procapsid and virus, the presence of the procapsid in na

61 irus canyon is structurally different in the procapsid and virus.

62 ined by comparing the structures of virions, procapsids and aberrantly assembled particles.

63 labeled substrates and GFP portal-containing procapsids and between GFP portal and single dye-labeled

64 -electron microscopy of wild type and mutant procapsids and complemented these data with biochemical

65 r than intermolecular upon packaging of most procapsids and demonstrates that single-molecule detecti

66 yo-electron microscopy and image analysis of procapsids and find that it observes 8-fold symmetry.

67 e local dynamics of the coat protein in both procapsids and mature capsids was monitored by hydrogen/

68 Seven proteins, purified procapsids and tails, and mature lambda DNA are necessar

69 apable of driving correctly shaped and sized procapsids and that the lack of these proper protein-pro

70 trate the feasibility of imaging herpesvirus procapsids and their morphogenesis in living cells and i

71 rt to "package" a viral genome into an empty procapsid, and it is likely that terminase enzymes from

72 he RdRP (protein P2) is assembled within the procapsid, and it was thought that it should be located

73 Comparing mature virion, procapsid, and mutant particle structures led us to prop

74 tion to determine structures of PRD1 virion, procapsid, and packaging deficient mutant particles.

75 RNA, DNA, gp3, DNA-gp3, connector, pRNA-free procapsid, and procapsid/pRNA complex.

76 ex of a preformed viral protein shell called procapsid, and pumps the viral DNA into the procapsid th

77 olding proteins bind to coat proteins in the procapsid, and the conformational changes upon capsid ma

78 an expanded empty capsid, sometimes called a procapsid, and the infectious virus.

79 a putative precursor in virus assembly, the procapsid, and the mature virus capsid.

80 of particles-procapsids, scaffold-deficient procapsids, and expanded capsids.

81 pes simplex virus 1 (HSV-1) infection, empty procapsids are assembled and subsequently filled with th

82 These procapsids are assembled from a coat protein having the

83 Procapsids are assembled with specific CTS-directed exog

84 ncapsidation, herpes simplex virus 1 (HSV-1) procapsids are converted to DNA-containing capsids by a

85 ein interactions observed in the assembly of procapsids are likely important in the control of nuclea

86 Procapsids are round, porous particles (480 A diameter)

87 Phage P22 procapsids are the product of the co-assembly of 420 mol

88 ous empty capsid, sometimes referred to as a procapsid, are produced.

89 nding of pRNA to either the connector or the procapsid, as investigated by agarose gel electrophoresi

90 Procapsids assembled in the presence of a scaffolding pr

91 mino acids contained the portal protein, but procapsids assembled with the C-terminal 66 did not, sug

92 In this study we show that the L procapsid assembly and DNA packaging genes, which encode

93 The data further indicate that procapsid assembly and maturation are strongly conserved

94 ormational switching of subunits during both procapsid assembly and maturation.

95 to modulate disulfide bond formation during procapsid assembly and maturation.

96 required for conformational switching during procapsid assembly and maturation.

97 The essential features of procapsid assembly are conserved in both eukaryotic and

98 The relevance of this work with respect to procapsid assembly in the complex double-stranded DNA vi

99 Procapsid assembly is a process whereby hundreds of copi

100 We show that procapsid assembly minimizes the differences in quaterna

101 This fusion neither interfered with procapsid assembly nor affected the morphology of the pr

102 lytic maturation events are not required for procapsid assembly or for DNA packaging into the structu

103 Within this context, the lambda procapsid assembly pathway has been reported to be uniqu

104 sensitivity to protease digestion, decreased procapsid assembly rates, and impaired phage production

105 Here we have investigated whether P22 procapsid assembly reactions achieve equilibrium or are

106 acid in scaffolding protein required for P22 procapsid assembly, although others modulate affinity.

107 s are proposed to increase the efficiency of procapsid assembly, favoring correct folding over improp

108 X174 DNA pilot protein H is monomeric during procapsid assembly, it forms an oligomeric tube on the h

109 binding domain, residue R293 is required for procapsid assembly, while residue K296 is important but

110 The scaffolding proteins are essential to procapsid assembly.

111 l mature capsid, but is essential for proper procapsid assembly.

112 esents the state of the polypeptide prior to procapsid assembly.

113 ng the significance of the D-loops in proper procapsid assembly.

114 ge P22 is important in the process of proper procapsid assembly.

115 and, thus, is intimately involved in proper procapsid assembly.

116 likely to be the oligomer incorporated into procapsids: at a resolution of 16 A, it has an axial cha

117 al double-stranded region of pRNA is not for procapsid binding but for binding to gp16.

118 The data revealed that the procapsid binding domain contains two autonomous modules

119 tween two 4-nucleotide loops within the pRNA procapsid binding domain, multiple copies of pRNA form a

120 uration and present a structural model for a procapsid-bound protease dimer.

121 particles via an empty precursor capsid (or 'procapsid') built by multiple copies of coat and scaffol

122 ding protein is required for assembly of the procapsid but is not present in the mature virion.

123 structures shared some characteristics with procapsids but had a novel appearance by negative staini

124 implex virus type 1 capsid and its precursor procapsid by a cryoelectron microscopic tilting method.

125 ruses is the packaging of DNA into preformed procapsids by an ATP-powered molecular motor.

126 erization of radioactively labeled precursor procapsids by sucrose gradient centrifugation shows that

127 ny sequence can be packaged into empty viral procapsids by the phage T4 terminase with high efficienc

128 Viral genomes are packaged into "procapsids" by powerful molecular motors.

129 r, here we demonstrate that the phage lambda procapsid can be expanded with urea in vitro and that th

130 This structure-function study shows that the procapsid can sequester antibodies, thus enhancing EV71

131 own which material properties of the fragile procapsids change.

132 nificant structural differences for the 1095 procapsid compared to a structure solved in a previous s

133 electron microscopy reconstruction of the T4 procapsid complexed with gp17 shows that the packaging m

134 Purified procapsids composed of all of the su coat proteins showe

135 ector-pRNA complex at a unique vertex of the procapsid conclusively demonstrates the pentameric symme

136 Its polyprotein Gag assembles into spherical procapsids, concomitant with budding.

137 atic maturation in which the 490-A spherical procapsid condenses to a 400-A icosahedral-shaped capsid

138 Mg(2+) drives the expanded shell back to the procapsid conformation in a highly cooperative transitio

139 ucts, including tubes, are formed instead of procapsids, consequently phage production is affected, i

140 The procapsid consists of an icosahedrally symmetric shell o

141 In addition, SaPI1 procapsids contained at least one SaPI1-encoded protein

142 dsDNA viruses begins with the assembly of a procapsid, containing scaffolding proteins and a multisu

143 The procapsid contains an encoded chemical program that is e

144 llography and was used to interpret the open procapsid cryo-EM structure.

145 In the phiX174 procapsid crystal structure, 240 external scaffolding pr

146 We propose that interactions with the procapsid during DNA translocation conformationally rest

147 ves as the hole through which DNA enters the procapsid during particle assembly and exits during infe

148 ses package DNA through the portal ring of a procapsid during phage maturation.

149 viruses made possible the discrimination of procapsids during infection and monitoring of capsid she

150 rnal scaffolding protein B binding to faulty procapsid elongation reactions mediated by external scaf

151 h published biochemical data indicating that procapsid expansion exposes hydrophobic surface area and

152 ion to a general mechanism for DNA-triggered procapsid expansion in the complex double-stranded DNA v

153 aging rate at 30% packaging, suggesting that procapsid expansion occurs at this point following the b

154 we used both purified connector and purified procapsid for binding studies with in vitro transcribed

155 It was novel to discover that the procapsid form of EV71 was expanded and antigenically di

156 observed in the solution persisted into the procapsid form, but was lost upon maturation.

157 s two morphogenetic steps: the initiation of procapsid formation and DNA packaging.

158 ernal scaffolding domains needed to initiate procapsid formation and provide more evidence, albeit in

159 The kinetics of procapsid formation was analyzed in vitro using wild-typ

160 on the inner surface of the connector during procapsid formation, is retained in the mature virion, a

161 ernal scaffolding protein needed to nucleate procapsid formation.

162 terized B(-) mutants blocked assembly before procapsid formation.

163 ically trapped assembly intermediates before procapsid formation.

164 the same geometry as either prolate T=3 Q=5 procapsids formed in vivo or previously observed isometr

165 ot only guide assembly but also restrain the procapsid from premature expansion; their removal by pro

166 rmation of an intermediate complex, termed a procapsid, from which individual subunits can undergo th

167 lar machines that pump DNA into preassembled procapsids, generating internal capsid pressures exceedi

168 n) and 2) translocation of the duplex into a procapsid (genome packaging).

169 tion is reminiscent of that observed for the procapsid --> capsid transformation of P22.

170 d and the infectious virion, the alpha3 open procapsid has 30A wide pores at the 3-fold vertices and

171 Here, we demonstrate that the EV71 procapsid has different antigenic properties than the in

172 Thus, the procapsid has the capacity to sequester neutralizing ant

173 Assembly of bacteriophage P22 procapsids has long served as a model for assembly of sp

174 V71 procapsid and virus, the presence of the procapsid in natural virus infections should be consider

175 NA can be packaged into purified recombinant procapsid in vitro.

176 protein monomers are able to dissociate from procapsids in an active state, that assembly of procapsi

177 motors drive genome packaging into preformed procapsids in many double-stranded (ds)DNA viruses.

178 ded structural proteins in 80alpha and SaPI1 procapsids, including several that had not previously be

179 A-binding protein cannot be generated due to procapsid instability during DNA packaging.

180 us; (2) proceed through a fragile, spherical procapsid intermediate; and (3) result in incorporation

181 d to the same intermediate state as expanded procapsids (intermediate 1) or to a second, further expa

182 cyclic recombination (Cre) targeted into the procapsid is enzymatically active within the procapsid a

183 First, a procapsid is formed through coassembly of the surface sh

184 For both EV71 strains, the procapsid is significantly larger in diameter than the m

185 d package their genomic DNA into a preformed procapsid is still elusive.

186 The N-terminus of the subunits in the 13 MDa procapsid is sufficiently dynamic to be studied by solut

187 capsids in an active state, that assembly of procapsids is consistent with reactions at equilibrium a

188 Packaging of viral genomes inside empty procapsids is driven by a powerful ATP-hydrolyzing motor

189 Genome packaging into preformed viral procapsids is driven by powerful molecular motors.

190 In many viruses, a precursor particle, or procapsid, is assembled and undergoes massive chemical a

191 f scaffolding protein, resulting in dramatic procapsid lattice expansion.

192 To assemble a procapsid-like particle in vitro, pure coat protein mono

193 lding protein (gp8) are needed to assemble a procapsid-like particle, both in vivo and in vitro.

194 ing oligomers, most likely tetramers, formed procapsid-like particles in vitro, suggesting that the 1

195 protein is essential for proper assembly of procapsids, little is known about its structure beyond a

196 acterize the protease responsible for lambda procapsid maturation and present a structural model for

197 ll with an inner scaffolding shell; then the procapsid matures via a major structural transformation,

198 obacteria predate the enteric bacteria, this procapsid-mediated assembly pathway may have originated

199 the varphiX174 H protein is monomeric during procapsid morphogenesis, 10 proteins oligomerize to form

200 rmediate and validating the current model of procapsid morphogenesis.

201 independently of other proteins involved in procapsid morphogenesis.

202 us-like particles that possess a native-like procapsid morphology.

203 gp16 bound to the pRNA-containing procapsid much more strongly than to the pRNA-free proca

204 tually, all animal viruses transition from a procapsid noninfectious state to a mature infectious sta

205 the initial location of the RdRP inside the procapsid of bacteriophage Phi6, we performed cryo-elect

206 the presence (in A-particle) or absence (in procapsid) of capsid-RNA interactions, the two CVA6 part

207 into preformed polyhedral structures called procapsids or inner cores.

208 into preformed polyhedral structures called procapsids or inner cores.

209 oportion of the input protein assembled into procapsids or remaining as free subunits was determined

210 conformations: an asymmetric assembly in the procapsid (PC-portal) that is competent for high affinit

211 ithin the dimensions of the long axis of the procapsid portal.

212 Most viral procapsids possess a special vertex containing a dodecam

213 emble of data to indicate that (i) the viral procapsid possesses a degree of plasticity that is requi

214 length units and package them into preformed procapsid powered by ATP hydrolysis.

215 DNA-gp3, connector, pRNA-free procapsid, and procapsid/pRNA complex.

216 EM imaging of procapsid/pRNA complexes clearly revealed six ferritin p

217 The procapsid protease possesses autoproteolytic activity, i

218 ers of the precursor capsid protein gp5 into procapsids; proteolysis of their N-terminal Delta-domain

219 The cryo-EM map of the procapsid provides new structural information on portion

220 Our results indicate that the procapsid releases scaffolding proteins and expands its

221 The procapsid represents a kinetically accessible local mini

222 iophage phi29 genomic DNA into its preformed procapsid requires the DNA packaging motor, which is the

223 Packaging of viral genomes into preformed procapsids requires the controlled and synchronized acti

224 of the double-stranded DNA bacteriophage P22 procapsids requires the interaction of 415 molecules of

225 here appear to be three classes of particles-procapsids, scaffold-deficient procapsids, and expanded

226 the internal "scaffold" protein required for procapsid self-assembly, and it is responsible for prote

227 The procapsids self-assemble from monomeric precursors to af

228 tly translocates the duplex into a preformed procapsid shell (genome packaging).

229 rolling packaging-triggered expansion of the procapsid shell are discussed in relation to a general m

230 In these cases, viral DNA is packaged into a procapsid shell by a terminase enzyme.

231 The procapsid shell consists of 60 copies each of P1(A) and

232 e motor to pump their genome inside an empty procapsid shell during virus maturation.

233 here viral DNA is inserted into a pre-formed procapsid shell.

234 ging viral DNA into the confines of an empty procapsid shell.

235 , as well as in the context of the assembled procapsid shell.

236 he viral genome is inserted into a preformed procapsid shell.

237 When empty procapsid shells (procapsids with the scaffolding protei

238 age reconstructions of F170A and F170K empty procapsid shells showed that there is a decreased flexib

239 rminal domain was more flexible in the empty procapsid shells than in the mature capsids.

240 e two domains exchanged rapidly in the empty procapsid shells, but more slowly in the mature capsids.

241 ble to exchange with the subunits from empty procapsid shells.

242 ent in vitro but does not bind to unexpanded procapsid shells.

243 Three mutations of Glu to Gln that formed procapsids showed three different phenotypes on maturati

244 e initial assembly of scaffolding-containing procapsids, similar to the assembly pathways for the ent

245 proteins for its formation.The alpha3 "open" procapsid structural intermediate was determined to 15A

246 The procapsid structural model is in good agreement with pub

247 .0-A resolution, respectively, and the first procapsid structure at subnanometer resolution without i

248 ages its 19.3-kbp genome into a preassembled procapsid structure by using a transiently assembled pha

249 urprisingly, formation of the highly complex procapsid structure depends on a relatively simple inter

250 characterized at atomic resolution, no such procapsid structure is available for a dsDNA virus or ba

251 Hence, comparison with the procapsid structure provides a rare opportunity to follo

252 lude packaging of viral DNA into a preformed procapsid structure, catalyzed by terminase enzymes and

253 protein-mediated morphogenesis and the oX174 procapsid structure, in which external scaffolding-scaff

254 Based on the procapsid structure, we propose that the axial channels

255 es asymmetric dimers observed in the phiX174 procapsid structure.

256 The procapsid structures show the scaffolding protein intera

257 electron microscopy reconstructions of SaPI1 procapsids, suggesting that gp6 acts as an internal scaf

258 Assembly proceeds via a 108S empty procapsid that requires the external D and internal B sc

259 n and/or stability and for the production of procapsids that are capable of encapsidation.

260 Tailed DNA bacteriophages assemble empty procapsids that are subsequently filled with the viral g

261 infected honey bees, including the immature procapsid, the genome-filled virion, the putative entry

262 of the portal vertex of the bacteriophage T7 procapsid, the recipient of T7 DNA in packaging.

263 In procapsids, the N-terminus was no longer accessible to t

264 procapsid, and pumps the viral DNA into the procapsid through a conduit formed by the portal.

265 DNA is translocated into the empty procapsid through the portal ring channel to high densit

266 P8-genome complex is then packaged into the procapsid through the unique vertex while the genome ter

267 portal protein switches conformation from a procapsid to a mature phage state upon binding of gp4, t

268 ibility for switching spontaneously from the procapsid to the first intermediate state.

269 may involve an inward radial collapse of the procapsid to yield the native virion.

270 ined the structures of the 80alpha and SaPI1 procapsids to near-atomic resolution by cryo-electron mi

271 rform a scaffolding-like function during the procapsid-to- virion transition.

272 To investigate procapsid transformability, we induced expansion by acid

273 Procapsids transition to capsids when pH is lowered from

274 of the peripheral interface to the varphi29 procapsid turned out to be rather soft.

275 Because of the stability of the procapsid under near-neutral conditions and the reversib

276 sembly product of bacteriophage varphi6, the procapsid, undergoes major structural transformation dur

277 estigated the in vitro assembly of phage P22 procapsids using a quantitative model specifically devel

278 Many viruses package their genomes into procapsids using an ATPase machine that is among the mos

279 ric packaging terminase docked onto a unique procapsid vertex containing a portal ring.

280 NA-packaging models proposed that the 5-fold procapsid vertexes and 12-fold connector (or the hexamer

281 ecific binding of RNA to the exterior of the procapsid was dependent upon ATP, and a region that show

282 ific binding of pRNA to the connector in the procapsid was found by photoaffinity crosslinking.

283 1 proteins and tethered to microspheres, and procapsids were attached to separate microspheres.

284 d their abilities to bind to the exterior of procapsids were determined.

285 By cryo-electron microscopy, these procapsids were found to have a round shape and an inter

286 In this study, 80alpha and SaPI1 procapsids were produced by induction of phage mutants l

287 s of capsid proteins were synthesized, these procapsids were unable to initiate the encapsidation pro

288 eviously shown to result in the formation of procapsids when purified at pH 7.6.

289 ded RNA (ssRNA) segments into an icosahedral procapsid which serves as a compartment for genome repli

290 The P22 procapsid, which is the viral capsid precursor, is assem

291 that internal force can rupture the immature procapsid, which lacks an accessory protein (gpD).

292 oteins assemble in vitro into an icosahedral procapsid, which then expands during DNA packaging (matu

293 g and coat proteins that co-assemble to form procapsids, which are transient precursor structures lea

294 s the published model that pRNA binds to the procapsid with its central domain and extends its 5'/3'

295 r shell is first assembled as an icosahedral procapsid with recessed 5-fold vertices that subsequentl

296 main guides 420 copies of the subunit into a procapsid with T=7 laevo icosahedral symmetry named Proh

297 copy to localize P7 by difference mapping of procapsids with different protein compositions.

298 When empty procapsid shells (procapsids with the scaffolding protein stripped out) we

299 9K, whose capsomers reassemble in vitro into procapsids with vacant vertices called "whiffleballs".

300 UL17 and UL6 appear to be components of the procapsid, with UL25 being added subsequently.

301 Here we present a procapsid X-ray structure at 3.65 A resolution, termed p