ライフサイエンスコーパス: capsomer

1 licit interaction between protein multimers (capsomers).

2 unit to the adjacent subunit within the same capsomer.

3 eric coiled-coil towers, two per surrounding capsomer.

4 additional contact point on the side of the capsomer.

5 (extended loop) of a subunit on an adjacent capsomer.

6 cule binds near the center of each hexameric capsomer.

7 c density beneath the axial lumen of each L1 capsomer.

8 ith A91 and L401 of a subunit in an adjacent capsomer.

9 harides bind to recessed regions between VP1 capsomers.

10 at the threefold axes that interlinked three capsomers.

11 ify the interactions between monomers within capsomers.

12 tion of covalent crosslinks between adjacent capsomers.

13 isting of pseudohexagonal arrays of trimeric capsomers.

14 CP), and works by altering the angle between capsomers.

15 arranged in trimers forming pseudo-hexameric capsomers.

16 ptation hot-spots located within and between capsomers.

17 to depend on specific ionic contacts between capsomers.

18 gle between the planes of adjacent hexameric capsomers.

19 c L1 invading arms between five-fold related capsomers.

20 t contacts between coat proteins in adjacent capsomers.

21 are 260 trimeric capsomers and 12 pentameric capsomers.

22 isn't dependent on the crosslinking between capsomers.

23 particle that does not readily lose further capsomers.

24 erconnects 12 pentameric and 30 hexameric CP capsomers.

25 oc trimers act as clamps between neighboring capsomers.

26 an interconnected network within and across capsomeres.

27 s, respectively, which compose the hexameric capsomeres.

28 tained one monomer from each of two adjacent capsomeres.

29 g the local symmetry axes of the surrounding capsomeres.

30 molecules of both pentavalent and hexavalent capsomeres.

31 es for the 5B6 epitope in the 12 pentavalent capsomeres.

32 igenic domains are contained entirely within capsomeres.

33 americ capsomeres and capsids composed of 72 capsomeres.

34 apsomeres and flexible links that form among capsomeres.

35 tiple domains capable of interacting with L1 capsomeres.

36 ting the cytoplasmic assembly of papovavirus capsomeres.

37 l hollow spikes that clustered into distinct capsomeres.

38 ions that change the angles between adjacent capsomers affect the positions of the pentameric vertice

39 propose that the axial channels of hexameric capsomers afford the pathway via which the scaffolding p

40 omogeneity as pentamers (equivalent to viral capsomeres), after thrombin cleavage from the GST moiety

41 Remarkably, HPV16 L1 capsomeres also interacted with Kap beta2 and binding of

42 meter analysis and local movement with inter-capsomer analysis.

43 ) is present at the centre of each hexameric capsomer and provides a good platform for surface displa

44 gthened association between the two types of capsomeres and an, apparently, more stable capsid.

45 n the cytoplasm, L1 and VP1 pentamerize into capsomeres and are then imported into the nucleus using

46 tein denoted L1, which forms both pentameric capsomeres and capsids composed of 72 capsomeres.

47 equence of stable contacts that occur within capsomeres and flexible links that form among capsomeres

48 The absence of mAb 5B6 from the pentavalent capsomeres and its inability to prevent viral binding to

49 nsition could occur by shedding of hexameric capsomeres and restructuring of remaining pentamers acco

50 = 27 lattice in which there are 260 trimeric capsomers and 12 pentameric capsomers.

51 rths-complete capsid lacking one pentamer of capsomers and a free, stable pentamer were obtained.

52 d structures on the interior surfaces of all capsomers and is further stabilized around the portal, f

53 The links also prevent flattening of capsomers and premature maturation.

54 mination should be applicable to other viral capsomers and protein-protein complexes in general.

55 The protein subunits forming hexameric capsomeres, and particularly dimers, appear to interact

56 sid is icosahedral in shape, composed of 162 capsomers, and assembled in the infected cell nucleus.

57 ne capsomer, capsids missing one pentamer of capsomers, and free pentamers of capsomers) had been pre

58 and partially degraded capsids with missing capsomeres; and 5) the DNA extruded from damaged virions

59 ly and bivalently to the sides of hexavalent capsomeres approximately two-thirds of the way down from

60 The capsomers are assembled into arrays that have either p6

61 The hexameric and pentameric capsomers are composed of the major capsid protein (MCP)

62 Its capsomers are hexamers and pentamers of the major capsid

63 coli bacteriophage HK97 and other phages, 60 capsomers are hexons, while the rest are pentons that ar

64 In polyomaviruses the pentameric capsomers are interlinked by the long C-terminal arm of

65 Individual VP1 capsomers are tethered to one another by an extensive di

66 avirus family) are composed of 72 pentameric capsomeres arranged on a skewed icosahedral lattice (tri

67 diameter of 220 nm and is composed of 2,192 capsomers arranged with T=219 quasisymmetry.

68 otein spike cross-links three neighboring CP capsomers as might occur during initiation of virus budd

69 Both forms have star-shaped capsomeres, as do BPV-1 and HPV-1, but the open CRPV cap

70 first oligomerizes into pentamers, and these capsomers assemble into virus-like particles (VLPs) that

71 americ capsomers on the faces and pentameric capsomers at all but one vertex where a 12-fold portal i

72 are situated between sets of three adjacent capsomers at the boundary between neighboring trisymmetr

73 found that recombinant MCPyV VP1 pentameric capsomeres both hemagglutinated sheep red blood cells an

74 Both VP1 and L1 capsomeres bound by karyopherin alpha2beta1 were unable

75 and human papillomavirus type 11 (HPV11) L1 capsomeres bound the karyopherin heterodimer alpha2beta1

76 ia its C-terminal 85 residues to purified L1 capsomers, but not with intact L1 virus-like particles i

77 vide a model for a hyperstabilization of the capsomer by H16.V5 Fab and showed that the Fab distingui

78 t frequently identified (capsids missing one capsomer, capsids missing one pentamer of capsomers, and

79 the conformation of phlebovirus glycoprotein capsomers changes from the native conformation toward a

80 characterised by conserved pseudo-hexameric capsomers composed of three copies of a single major cap

81 along with fragments of the membrane; 3) the capsomeres composing the capsid and their surface arrang

82 ple many independent trajectories at various capsomer concentrations, allowing for statistically mean

83 The pentameric capsomers consist of five single jelly-roll proteins.

84 The trimeric capsomers consist of three double "jelly-roll" major cap

85 VP1 and L1 capsomeres could bind both karyopherin alpha2 and DNA si

86 y of purified HPV-11 L1 VLPs to the level of capsomeres, demonstrating that disulfide bonds alone are

87 ighboring subunit to stabilize homo-trimeric capsomeres during assembly.

88 Inter-capsomer expansion or contraction, governed by the conne

89 ical arrangements of the VP5 subunits in the capsomeres exposes different residues, resulting in the

90 nd fitted into densities that either cap the capsomers externally or stabilize them internally.

91 he larger particle, 50.6 nm in diameter, the capsomers form a T=7 icosahedral shell with three unique

92 article, 26.4 nm in diameter, the pentameric capsomers form an icosahedral T=1 surface lattice with m

93 he B and C subunits comprising the hexameric capsomeres formed an annulus about the interior of the c

94 HPV16 L1 capsomeres formed complexes with Kap alpha2beta1 heterod

95 ct as a "glue" between neighboring hexameric capsomers, forming a "cage" that stabilizes the T4 capsi

96 Furthermore, CyPs released L1 capsomeres from partially disassembled HPV16 pseudovirio

97 The particles are composed of pentameric capsomeres from the wild-type virions which have reorien

98 /or neutralizing monoclonal antibodies, both capsomeres generated by disulfide reduction of purified

99 Depending on subunit (i.e., capsomer) geometries, successful assembly proceeds by se

100 es exposed in the capsid valley between each capsomer, H16.U4 Fab bound only to epitopes located arou

101 HPV6 L1 capsomers had one to six regions mutated, including the

102 pentamer of capsomers, and free pentamers of capsomers) had been predicted in theoretical studies of

103 adjacent subunits at the outer periphery of capsomers, has been implicated in capsid stability.

104 One specific capsomer in each asymmetric unit contains a fiber-like p

105 highly immunoreactive with trypsin-generated capsomeres in an enzyme-linked immunosorbent assay (ELIS

106 Based on the orientation of capsomers in the cryo-EM reconstruction, we propose that

107 ment of the hexameric and pentameric protein capsomers in the growing shell during assembly.

108 ity extends continuously between neighboring capsomers in the inner "floor" layer.

109 m, and show that Ccm occupies the pentameric capsomers in the isometric SaPIbov5 procapsids, suggesti

110 ons, whereas they are tightly clustered into capsomers in the mature state; the axial channels, which

111 unit, which extends from beneath one of the capsomers in the pentasymmetron to the internal leaflet

112 ging, we determined the structures of native capsomers in the presence and absence of inositol hexaki

113 hen the mutant structure is dissociated into capsomers in vitro, only hexamers are found.

114 8, but not to predominately disordered HPV16 capsomers, induced acute phenotypic maturation of BMDCS:

115 Significantly, HPV16 L1 capsomeres inhibited the nuclear import of Kap beta2 and

116 e are no direct contacts between neighboring capsomers; instead, interactions between them are mediat

117 he region of maximum contact, papillomavirus capsomeres interact in a manner similar to that found in

118 s attributed to the Ta triplex and the small capsomer-interacting protein (SCIP or ORF65), exhibit pr

119 Capsomer interactions in the expanded capsid are reinfor

120 ction and by their ability to assemble viral capsomeres into capsids in vitro.

121 e P domain of a neighboring subunit within a capsomer, into which W61 fits like a peg.

122 Each capsomer is composed of three molecules of the major cap

123 e conventional penta-symmetron formed by the capsomeres is replaced by a large vertex complex in the

124 The angle between adjacent hexameric capsomers is greatest around the fivefold vertices, wher

125 , a mutant of adenovirus type 2 whose vertex capsomers lack an Arg-Gly-Asp (RGD) sequence which media

126 teractions with other assembly units, called capsomers, leading to gaps in the particle surface.

127 e H16.V5 Fab preferentially bound hexavalent capsomers likely with a stabilizing effect that directly

128 Thus, capsomeres may be viable vaccine candidates for the prev

129 by displacing one or more of the pentameric capsomers may be the result of a low-pH environment.

130 that papillomavirus capsids are dynamic and capsomers move as rigid bodies connected by flexible lin

131 wed no bias in the magnitude or direction of capsomer movement.

132 L1/L2 capsomers, obtained from the disassembly of virus-like p

133 to enhance the interactions of the hexameric capsomeres of gp27, for other phages encoding decoration

134 Capsomeres of L1, but not VP1, bound by karyopherin alph

135 rus (papovavirus) capsids are composed of 72 capsomeres of their major capsid proteins, VP1 and L1, r

136 contacts are not preserved in the flattened capsomers of the mature capsid.

137 of the particles, exhibited arrangements of capsomeres on their surfaces which were consistent with

138 assemble icosahedral capsids with hexameric capsomers on the faces and pentameric capsomers at all b

139 both VP6 and bluetongue VP7 assemble as 260 capsomers on the surface of the inner capsid.

140 composed of upright standing pseudohexameric capsomers organized on a T = 49 icosahedral lattice.

141 of minor capsid proteins associated with the capsomers outside the lipid membrane.

142 e the V5 and E70 epitopes at the apex of the capsomer overlap the ECM-binding sites.

143 actions (slightly different contacts between capsomeres), papovavirus capsids have a conserved, 72-pe

144 yoEM density for each of the 25 trimeric CIV capsomers per icosahedral asymmetric unit.

145 suggest that these effects propagate to the capsomer periphery in such a way as to differentially af

146 from particles that retained the ORF65 small capsomer protein.

147 various lengths, made up of trapezoid-shape capsomeres, provide a basis for icosahedral T = 4 and T

148 We also analyzed the mutant E219K, whose capsomers reassemble in vitro into procapsids with vacan

149 In contrast, 5B6 binds only to hexavalent capsomeres, reflecting the significant structural or env

150 intact L1 protein, likely still arranged as capsomeres, remains associated with the incoming viral g

151 nomer and the pseudo-sixfold symmetry of the capsomer resembles that of the major coat proteins in th

152 ired to form both pentavalent and hexavalent capsomeres result in structures that exhibit very differ

153 e was transmitted to the lower region of the capsomer, resulting in enhanced intercapsomeric interact

154 onent of the triplexes that connect adjacent capsomeres), results in the formation of spherical parti

155 6)) binds to a positively charged pore of CA capsomers rich in arginine and lysine residues mediated

156 though there are breakages among neighboring capsomers, RNA-capsid protein interaction prevents the r

157 gene 23 that affect capsid shape map to the capsomer's periphery, whereas mutations that allow gp23

158 el in which flexible E153-R210 links mediate capsomer shape changes that control where pentons are pl

159 during maturation despite radical changes in capsomer shape.

160 pose that the L1 protein, likely arranged as capsomeres, stabilizes the viral genome within the subvi

161 jor capsid proteins creating pseudohexameric capsomer symmetry.

162 t-subunit interactions within and across the capsomeres that are required to stabilize the virus.

163 t it forms pentameric units resembling viral capsomeres that assemble into larger capsid-like structu

164 n can be trypsinized to generate recombinant capsomeres that retain HPV genotype-restricted capsid an

165 escribe additional ionic interactions within capsomers that also regulate assembly.

166 s (HPV) major structural protein L1 composes capsomers that are linked together through interactions

167 capsid (CA) protein hexamers and pentamers (capsomers) that contain a central pore hypothesised to r

168 ized HeLa cells were incubated with HPV16 L1 capsomeres, the L1 protein was imported into the nucleus

169 91 and L401 in P-domain loops of an adjacent capsomer, thereby linking the entire capsid together wit

170 s as a molecular staple between neighbouring capsomeres to ensure the particle's stability.

171 mation on the local interactions between the capsomers to infer the geometric construction principle

172 s appear to form early in assembly to enable capsomers to make programmed changes in their shape duri

173 plays a distinctive skewing of the hexameric capsomeres, to the mature virion, which is larger and mo

174 compensate for release of SPs that clasp MCP capsomeres together.

175 tabilizing the capsid by binding neighboring capsomers together.

176 nitiated by loss of one of the 20 equivalent capsomers (trimers of capsid protein subunits) leading t

177 rified VLPs and reassembled VLPs formed from capsomeres upon removal of reducing agents exhibited epi

178 Accordingly, nuclear import of HPV16 L1 capsomeres was mediated by Kap alpha2beta1 heterodimers,

179 to these epitopes and requires assembly into capsomeres, we propose that L1 protein is present in the

180 was resolved to a resolution of 6.1 nm, and capsomeres were observed to be arranged on the virus sur

181 Capsomeres were used to generate high-titer polyclonal i

182 difference map, in which the fitted CIV MCP capsomers were subtracted from the CIV cryoEM reconstruc

183 After verifying proper conformation, hybrid capsomers were used in enzyme-linked immunosorbent assay

184 the coat protein subunits together within a capsomer, where the E-loop hydrophobic residue W61 of on

185 hat mAb #9 binds monovalently to the tips of capsomeres whereas 5B6 binds both monovalently and bival

186 ull-length L1 protein appeared as pentameric capsomeres which self-assembled into capsid-like particl

187 r particle at the center of the 20 hexameric capsomeres, which are a direct result of the K42R mutati

188 We show that the outer face of the dimeric capsomeres, which contains the receptor binding site and

189 an assembly of loosely associated hexameric capsomeres, which may be the basis for the swelling and

190 and propensity to move freely from the other capsomers, which facilitates the shape adaptation that m

191 imited pathway of accumulation of individual capsomers while HBV and CCMV capsids fit similar but sub

192 f 195 A, is made from distinctive pentameric capsomeres with large holes along the 3-fold axis, while

193 ot all, of the spaces between three adjacent capsomers within each trisymmetron, and "zip" proteins a