ライフサイエンスコーパス: capsomer

1 licit interaction between protein multimers (capsomers).

2 additional contact point on the side of the capsomer.

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

4 unit to the adjacent subunit within the same capsomer.

5 cule binds near the center of each hexameric capsomer.

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

7 to depend on specific ionic contacts between capsomers.

8 tion of covalent crosslinks between adjacent capsomers.

9 isting of pseudohexagonal arrays of trimeric capsomers.

10 gle between the planes of adjacent hexameric capsomers.

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

12 t contacts between coat proteins in adjacent capsomers.

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

14 are 260 trimeric capsomers and 12 pentameric capsomers.

15 isn't dependent on the crosslinking between capsomers.

16 particle that does not readily lose further capsomers.

17 erconnects 12 pentameric and 30 hexameric CP capsomers.

18 oc trimers act as clamps between neighboring capsomers.

19 at the threefold axes that interlinked three capsomers.

20 ify the interactions between monomers within capsomers.

21 an interconnected network within and across capsomeres.

22 tiple domains capable of interacting with L1 capsomeres.

23 s, respectively, which compose the hexameric capsomeres.

24 tained one monomer from each of two adjacent capsomeres.

25 g the local symmetry axes of the surrounding capsomeres.

26 molecules of both pentavalent and hexavalent capsomeres.

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

28 igenic domains are contained entirely within capsomeres.

29 americ capsomeres and capsids composed of 72 capsomeres.

30 apsomeres and flexible links that form among capsomeres.

31 ting the cytoplasmic assembly of papovavirus capsomeres.

32 l hollow spikes that clustered into distinct capsomeres.

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

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

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

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

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

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

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

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

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

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

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

44 = 27 lattice in which there are 260 trimeric capsomers and 12 pentameric capsomers.

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

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

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

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

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

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

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

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

53 The capsomers are assembled into arrays that have either p6

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

55 Its capsomers are hexamers and pentamers of the major capsid

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

81 HPV16 L1 capsomeres formed complexes with Kap alpha2beta1 heterod

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

98 8, but not to predominately disordered HPV16 capsomers, induced acute phenotypic maturation of BMDCS:

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

122 from particles that retained the ORF65 small capsomer protein.

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

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

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

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

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

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

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

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

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

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

133 during maturation despite radical changes in capsomer shape.

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

135 jor capsid proteins creating pseudohexameric capsomer symmetry.

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

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

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

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

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

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

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

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

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

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

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

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

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

149 Capsomeres were used to generate high-titer polyclonal i

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

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

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

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

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

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

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

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

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

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