ライフサイエンスコーパス: CCMV

1 CCMV-VLPs can be easily expressed in an E. coli host sys

2 le size conversion of the empty capsids of a CCMV capsid protein functionalized with a hydrophobic el

3 had an intermediate level of diversity, and CCMV had no measurable level of diversity in N. benthami

4 lation of individual capsomers while HBV and CCMV capsids fit similar but subtly different models of

5 ation in cowpea chlorotic mottle bromovirus (CCMV) resulted in the recovery of an unusual recombinant

6 is packaged three times more efficiently by CCMV CP than is RNA1 of CCMV, even though the two RNAs h

7 or packaging by the T=3 capsids preferred by CCMV CP.

8 demonstrate that chimpanzee cytomegalovirus (CCMV) US6 binds, but does not inhibit, human TAP.

9 Recently, we have engineered CCMV-VLPs by incorporating the universal tetanus toxin (

10 ular genetic, and atomic structural data for CCMV are then reviewed, related to each other, and incor

11 and incorporated into an assembly model for CCMV that is discussed with respect to the modular, chem

12 In CCMV, the structures of the A, B, and C subunits are nea

13 used to follow the conformational change in CCMV coat dynamics.

14 esidues longer than the analogous regions in CCMV.

15 Initially, CCMV capsid protein (CP) dimers bind RNA with low cooper

16 namics simulations suggest that viruses like CCMV assemble by the bulk adsorption of CPs onto the RNA

17 The modified CCMV(TT)-VLPs successfully form icosahedral particles T

18 NA viruses, namely, Cowpea chlorotic mottle (CCMV) and Brome mosaic virus (BMV), are modulated by the

19 The wild-type and mutant CCMV virions were used to correlate virion swelling with

20 trol and monitor the in vitro co-assembly of CCMV CP and single-stranded RNA as a function of the str

21 tocol for the efficient in vitro assembly of CCMV VLPs and suggest potential strategies that the viru

22 capsid structure during the self-assembly of CCMV-like particles.

23 ggesting that cotranslational disassembly of CCMV involves presentation of the virion RNA through the

24 uired for the cotranslational disassembly of CCMV.

25 From the native form of CCMV, the structure can be displaced along the direction

26 Interaction of CCMV capsid protein with this RNA-DNA template leads to

27 The substitution of this region of CCMV US6 with the corresponding residues from HCMV US6 g

28 more efficiently by CCMV CP than is RNA1 of CCMV, even though the two RNAs have virtually identical

29 The sequence of CCMV US6 differs from that of HCMV US6 in the region cor

30 ncorporating TT epitope at the C-terminus of CCMV(TT)-VLPs results in the formation of Rod-shaped VLP

31 Unlike that of CCMV, the capsid of CMV does not undergo swelling at pH

32 MV is approximately 12 A larger than that of CCMV.

33 olytic analysis of the three virion types of CCMV assembled individually in planta revealed that, whi

34 his motif during encapsidation, a variant of CCMV RNA3 (C3) precisely lacking the ARM region (C3/Delt

35 as Round-shaped CCMV(TT)-VLPs and Rod-shaped CCMV(TT)-VLPs) as potential B cell immunogens using diff

36 Furthermore, compared to Rod-shaped CCMV(TT)-VLPs, Round-shaped CCMV(TT)-VLPs led to more th

37 oth engineered forms (termed as Round-shaped CCMV(TT)-VLPs and Rod-shaped CCMV(TT)-VLPs) as potential

38 Our results reveal that Round-shaped CCMV(TT)-VLPs are more efficient in draining to secondar

39 Round-shaped CCMV(TT)-VLPs could also polarize the induced T cell res

40 ed to Rod-shaped CCMV(TT)-VLPs, Round-shaped CCMV(TT)-VLPs led to more than 100-fold increased system

41 capsulation results in stable 21-22 nm sized CCMV-like particles, which is characteristic of an icosa

42 len and closed forms of the wild-type and SS-CCMV particles have highly dynamic N-terminal regions, y

43 sociation in high salt (salt-stable CCMV [SS-CCMV]) and retains 70% of wild-type infectivity.

44 Thus, the increase in SS-CCMV particle stability is a result of concentrated teth

45 2.7-A resolution crystal structure of the SS-CCMV capsid shows an addition of 660 new intersubunit in

46 ighly dynamic N-terminal regions, yet the SS-CCMV particles are more resistant to degradation.

47 e chemical stability and viability of the SS-CCMV particles.

48 le to dissociation in high salt (salt-stable CCMV [SS-CCMV]) and retains 70% of wild-type infectivity

49 trategy can be adapted to viruses other than CCMV.

50 -nm-diameter particles despite the fact that CCMV CP prefers to form 28-nm-diameter (T = 3) particles

51 We find that CCMV CP is also capable of packaging polyU RNAs, which-u

52 ratory has identified point mutations in the CCMV coat protein which result in virions with altered s

53 However, nucleotides in the CCMV core required for RNA synthesis are not identical t

54 Remarkably, a single-residue mutant of the CCMV N-terminal arm, K42R, is not susceptible to dissoci

55 This indicates that the CCMV capsid protein is multifunctional, with a distinct

56 ut the electrostatic interactions within the CCMV virion, relatively little is known about these inte

57 on the mutations observed in 3-57, wild-type CCMV clones were modified to determine if the carboxyl t

58 (ii) The wild-type CCMV virions purified from cowpea are highly susceptible

59 Using CCMV-like particles to mimic nanocompartments can provid

60 sembly of the Cowpea chlorotic mottle virus (CCMV) and observed that assembly with viral RNA follows

61 (GFP) and the cowpea chlorotic mottle virus (CCMV) are able to perform catalysis after introduction o

62 otein cage of cowpea chlorotic mottle virus (CCMV) at neutral pH.

63 mal region of cowpea chlorotic mottle virus (CCMV) capsid protein (CP) contains an arginine-rich RNA

64 for example, cowpea chlorotic mottle virus (CCMV) capsid protein (CP) has been shown to package RNA

65 sequence from Cowpea Chlorotic Mottle Virus (CCMV) could also substitute for the BMV subgenomic core

66 ch virions of cowpea chlorotic mottle virus (CCMV) disassemble and allow for translation of the virio

67 Cowpea chlorotic mottle virus (CCMV) forms highly elastic icosahedral protein capsids t

68 Cowpea chlorotic mottle virus (CCMV) has long been studied as a model system for the as

69 Cowpea chlorotic mottle virus (CCMV) is a widely used model for virus replication studi

70 otein (CP) of cowpea chlorotic mottle virus (CCMV) is capable of packaging both purified single-stran

71 eins (CPs) of cowpea chlorotic mottle virus (CCMV) is controlled by the solution pH.

72 Cowpea chlorotic mottle virus (CCMV) is used as a template that undergoes a pH-dependen

73 Cowpea chlorotic mottle virus (CCMV) undergoes a well-studied reversible structural exp

74 oordinates of cowpea chlorotic mottle virus (CCMV) used to generate hypothetical structures in approx

75 acteriophage, cowpea chlorotic mottle virus (CCMV), and cowpea mosaic virus (CPMV).

76 by virions of cowpea chlorotic mottle virus (CCMV), another unenveloped virus similar in size to ADV.

77 specifically cowpea chlorotic mottle virus (CCMV), are T = 3 icosahedral particles.

78 us (CMV), and Cowpea chlorotic mottle virus (CCMV), in infections of a common host, Nicotiana bentham

79 imilarity) to cowpea chlorotic mottle virus (CCMV), the core structures of these two members of the B

80 plant virus, cowpea chlorotic mottle virus (CCMV), we demonstrate the synthesis of virus-like partic

81 the model of cowpea chlorotic mottle virus (CCMV), which BMV closely resembles.

82 enomic RNA of Cowpea chlorotic mottle virus (CCMV), which is pathogenic to plants, is packaged into t

83 us (HBV), and cowpea chlorotic mottle virus (CCMV)-to assess both the range of pathway types the meth

84 hedral virus, cowpea chlorotic mottle virus (CCMV).

85 binding of labeled VP2 virions to ABP, while CCMV virions had no effect.

86 In addition, while CCMV has a cluster of aspartic acid residues at the quas