pH reduction as a trigger for dissociation of herpes simplex virus type 1 scaffolds

Journal of Virology

Volumn 76, Issue 15, 2002, Pages 7407-7417

  McClelland, David A ^a   Aitken, James D ^a   Bhella, David ^a   McNab, David ^a   Mitchell, Joyce ^a   Kelly, Sharon M ^a   Price, Nicholas C ^a   Rixon, Frazer J ^a  

^a INSTITUTE OF VIROLOGY   (United Kingdom)

Author keywords

[No Author keywords available]

Indexed keywords

PROTEIN PRECURSOR; PROTEIN VP22A; REAGENT; UNCLASSIFIED DRUG; VIRUS DNA; VIRUS PROTEIN;

ANIMAL CELL; ARTICLE; CIRCULAR DICHROISM; DISSOCIATION; DNA PACKAGING; ELECTRON MICROSCOPY; FLUORESCENCE SPECTROSCOPY; HERPES SIMPLEX VIRUS 1; NONHUMAN; PH; PRIORITY JOURNAL; PROTEIN ASSEMBLY; PROTEIN SECONDARY STRUCTURE; PROTEIN TERTIARY STRUCTURE; SEDIMENTATION; VIRION; VIRUS CAPSID; VIRUS GENOME;

ANIMALS; BACULOVIRIDAE; CAPSID; CELLS, CULTURED; CENTRIFUGATION, DENSITY GRADIENT; CIRCULAR DICHROISM; ELECTROPHORESIS, POLYACRYLAMIDE GEL; HYDROGEN-ION CONCENTRATION; MICROSCOPY, ELECTRON; PROTEIN PRECURSORS; SIMPLEXVIRUS; SPECTROMETRY, FLUORESCENCE; SPODOPTERA; VIRAL PROTEINS; VIRION; VIRUS ASSEMBLY;

EID: 0036310602     PISSN: 0022538X     EISSN: None     Source Type: Journal    
DOI: 10.1128/JVI.76.15.7407-7417.2002     Document Type: Article

References (69)

1. Molten globule intermediates and protein folding
2. Study of herpes simplex virus maturation during a synchronous wave of assembly
3. Viral RNA modulates the acid sensitivity of foot-and-mouth disease virus capsids
4. ATP depletion blocks herpes simplex virus DNA packaging and capsid maturation
5. Molecular interactions between the HSV-1 capsid proteins as measured by the yeast two-hybrid system
6. Second site mutations in the N-terminus of the major capsid protein (VP5) overcome a block at the maturation cleavage site of the capsid scaffold proteins of herpes simplex virus type 1
7. The size and symmetry of B capsids of herpes simplex virus type 1 are determined by the gene products of the UL26 open reading frame
8. Identification of the herpes simplex virus-1 protease cleavage sites by direct sequence analysis of autoproteolytic cleavage products
9. Scaffolding proteins and their role in viral assembly
10. DNA packaging by the doublestranded DNA bacteriophages
11. Exposure of tryptophanyl residues in proteins. Quantitative determination by fluorescence quenching studies
12. Evidence for the role of His-142 of protein 1C in the acid-induced disassembly of foot-and-mouth disease virus capsids
13. Conformational transformations in the protein lattice of phage P22 procapsids
14. The protease of herpes simplex virus type 1 is essential for functional capsid formation and viral growth
15. Compartmentalization of spermine and spermidine in the herpes simplex virion
16. Proteins specified by herpes simplex virus. VIII. Characterization and composition of multiple capsid forms of subtypes 1 and 2
17. The structural and metabolic involvement of polyamines with herpes simplex virus
18. The atomic structure of the bluetongue virus core
19. Unpacking the incoming influenza virus
20. Identification of a minimal hydrophobic domain in the herpes simplex virus type 1 scaffolding protein which is required for interaction with the major capsid protein
21. The 25 amino acid residues at the carboxy terminus of the herpes simplex virus type 1 UL26.5 protein are required for the formation of the capsid shell around the scaffold
22. The procapsid-to-capsid transition in double stranded DNA bacteriophages
23. The herpes simplex virus triplex protein VP23, exists as a molten globule
24. Maturation dynamics of a viral capsid: Visualization of transitional intermediate states
25. Structural polymorphism of the major capsid protein of rotavirus
26. The herpes simplex virus 1 gene encoding a protease also contains within its coding domain the gene encoding the more abundant substrate
27. The promoter, transcriptional unit, and coding sequences of herpes simplex virus 1 family 35 proteins are contained within and in frame with the UL26 open reading frame
28. Physical mapping of herpes simplex virus-induced polypeptides
29. Atomic structure of the major capsid protein of rotavirus: Implications for the architecture of the virion
30. The C-terminal 25 amino acids of the protease and its substrate ICP35 of herpes simplex virus type 1 are involved in the formation of sealed capsids
31. Structure of the herpes simplex virus capsid: Effects of extraction with guanidine hydrochloride and partial reconstitution of extracted capsids
32. Assembly of the herpes simplex virus capsid: Characterization of intermediates observed during cell-free capsid formation
33. Assembly of the herpes simplex virus procapsid from purified components and identification of small complexes containing the major capsid and scaffolding proteins
34. Cell-free assembly of the herpes simplex virus capsid
35. The UL6 gene product forms the portal for entry of DNA into the herpes simplex virus capsid
36. Structure of the herpes simplex virus capsid: Molecular composition of the pentons and the triplexes
37. Isolation of herpes simplex virus procapsids from cells infected with a protease-deficient mutant virus
38. Self-association of herpes simplex virus type 1 ICP35 is via coiled-coil interactions and promotes stable interaction with the major capsid protein
39. The herpes simplex virus gene UL26 proteinase in the presence of the UL26.5 gene product promotes the formation of scaffold-like structures
40. Identification and characterization of a herpes simplex virus gene product required for encapsidation of virus DNA
41. Efficient herpes simplex virus type 1 (HSV-1) capsid formation directed by the varicella-zoster virus scaffolding protein requires the carboxy-terminal sequences from the HSV-1 homologue
42. Regions of the herpes simplex virus scaffolding protein that are important for intermolecular self-interaction
43. Processing of the herpes simplex virus assembly protein ICP35 near its carboxy terminal end requires the product of the whole of the UL26 reading frame
44. Molten globule and protein-folding
45. Evidence for a molten globule state as a general intermediate in protein folding
46. Packaging competent capsids of a herpes simplex virus temperature-sensitive mutant have properties similar to those of in vitro-assembled procapsids
47. Roles of triplex and scaffolding proteins in herpes simplex virus type 1 capsid formation suggested by structures of recombinant particles
48. Study of the molten globule intermediate state in protein folding by a hydrophobic fluorescent-probe
49. Characterization of intranuclear capsids made by ts morphogenic mutants of HSV-1
50. The bacteriophage φ29 portal motor can package DNA against a large internal force
51. A self consistent method for the analysis of protein secondary structure from circular dichroism
52. Herpesvirus capsid assembly and envelopment
53. Assembly of herpes simplex virus type 1 capsids using a panel of recombinant baculoviruses
54. Assembly of the herpes simplex virus capsid: Requirement for the carboxylterminal twenty-five amino acids of the proteins encoded by the UL26 and UL26.5 genes
55. Assembly of herpes simplex virus (HSV) intermediate capsids in insect cells infected with recombinant baculoviruses expressing HSV capsid proteins
56. Identification of additional coat-scaffolding interactions in a bacteriophage P22 mutant defective in maturation
57. Three-dimensional structure of scaffolding-containing phage P22 procapsids by electron cryo-microscopy
58. The herpes simplex virus procapsid: Structure, conformational changes upon maturation, and roles of the triplex proteins VP19c and VP23 in assembly
59. Herpes simplex virus capsids assembled in insect cells infected with recombinant baculoviruses: Structural authenticity and localization of VP26
60. Distinct monoclonal antibodies separately label the hexons or the pentons of herpes simplex virus capsid
61. Mechanisms of virus assembly probed by Raman spectroscopy: The icosahedral bacteriophage P22
62. Human cytomegalovirus capsid assembly protein precursor (pUL80.5) interacts with itself and with the major capsid protein (pUL86) through two different domains
63. Aromatic and cystine side-chain CD in proteins
64. Visualization of the maturation transition in bacteriophage P22 by electron cryomicroscopy
65. Solubilization of matrix protein M1/M from virions occurs at different pH for orthomyxo- and paramyxoviruses
66. Seeing the herpesvirus capsid at 8.5 Å
67. Assembly of VP26 in herpes simplex virus-1 inferred from structures of wild-type and recombinant capsids
68. Protein subunit structures in the herpes simplex virus A-capsid determined from 400 kV spot-scan electron cryomicroscopy
69. Identification of disulfide linked protein complexes in the nucleocapsids of herpes simplex virus type 2