Structure, Interactions and Dynamics ofPRD1Virus I. Coupling of Subunit Folding and Capsid Assembly

Tůma, Roman; Bamford, Jaana H.K.; Bamford, Dennis H.; Russell, Malcolm P.; Thomas, George J.

doi:10.1006/jmbi.1996.0149

Cited by 42 publications

(41 citation statements)

References 51 publications

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“…Analysis of CIV showed not only the organization of the major capsid proteins in the capsomers, but also recognized some minor capsid proteins between the outer protein capsid and an inner membrane surrounding the nucleocapsid core. Similar stabilizing proteins were identified in the dsDNA bacteriophage PRD1 (10,11).…”

supporting

confidence: 59%

“…1B). Therefore, the amino-terminal 24 amino acids of Vp54 are apparently ordered in the virus because of their association with a minor capsid protein (10). The Vp54 double jelly-roll structure is similar to the structure of the capsid protein P3 in the lipid enveloped bacteriophage PRD1, with approximately 59% of the Vp54 C α atoms being superimposable onto the structure of P3 (27,28).…”

Section: Resultsmentioning

confidence: 91%

“…1B) following the peripheries of the MCP capsomers. They have some similarity to the long glue proteins between capsomers of the PRD1 bacteriophage (10,11) and adenovirus (29,30) (Fig. S2A).…”

Section: Resultsmentioning

confidence: 98%

“…After setting the density corresponding to all of the 1,680 trimeric capsomers in the virus to zero, a series of densities remain that has the same positional periodicity as the capsomers. These densities are presumably minor capsid proteins as occur in viruses CIV (9) and PRD1 (10,11). However, the minor capsid proteins lack icosahedral symmetry.…”

Section: Resultsmentioning

confidence: 99%

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Three-dimensional structure and function of the Paramecium bursaria chlorella virus capsid

Zhang

Xiang

Dunigan

et al. 2011

Proc. Natl. Acad. Sci. U.S.A.

126

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A cryoelectron microscopy 8.5 Å resolution map of the 1,900 Å diameter, icosahedral, internally enveloped Paramecium bursaria chlorella virus was used to interpret structures of the virus at initial stages of cell infection. A fivefold averaged map demonstrated that two minor capsid proteins involved in stabilizing the capsid are missing in the vicinity of the unique vertex. Reconstruction of the virus in the presence of host chlorella cell walls established that the spike at the unique vertex initiates binding to the cell wall, which results in the enveloped nucleocapsid moving closer to the cell. This process is concurrent with the release of the internal viral membrane that was linked to the capsid by many copies of a viral membrane protein in the mature infectous virus. Simultaneously, part of the trisymmetrons around the unique vertex disassemble, probably in part because two minor capsid proteins are absent, causing Paramecium bursaria chlorella virus and the cellular contents to merge, possibly as a result of enzyme(s) within the spike assembly. This may be one of only a few recordings of successive stages of a virus while infecting a eukaryotic host in pseudoatomic detail in three dimensions.3D structure | cell entry | conformation changes | minor proteins | PBCV-1

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supporting

confidence: 59%

Section: Resultsmentioning

confidence: 91%

Section: Resultsmentioning

confidence: 98%

Section: Resultsmentioning

confidence: 99%

See 2 more Smart Citations

Three-dimensional structure and function of the Paramecium bursaria chlorella virus capsid

Zhang

Xiang

Dunigan

et al. 2011

Proc. Natl. Acad. Sci. U.S.A.

126

View full text Add to dashboard Cite

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“…The early assembly product is devoid of the viral genome as empty, thick-shelled, rounded particles with a circular inner membrane were observed in thin sections of STIV-infected cells. These empty particles likely represent an intermediate stage as is observed for PRD1 and Bam35 (1,12,31,54). However, creating a prohead does not appear to be a universally conserved feature of the PRD1-adenovirus lineage since other members such as PM2 appear to assemble their membrane around the viral DNA genome (1).…”

Section: Discussionmentioning

confidence: 94%

Particle Assembly and Ultrastructural Features Associated with Replication of the Lytic Archaeal Virus Sulfolobus Turreted Icosahedral Virus

Brumfield

Ortmann

Ruigrok

et al. 2009

J Virol

128

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Little is known about the replication cycle of archaeal viruses. We have investigated the ultrastructural changes of Sulfolobus solfataricus P2 associated with infection by Sulfolobus turreted icosahedral virus (STIV). A time course of a near synchronous STIV infection was analyzed using both scanning and transmission electron microscopy. Assembly of STIV particles, including particles lacking DNA, was observed within cells, and fully assembled STIV particles were visible by 30 h postinfection (hpi). STIV was determined to be a lytic virus, causing cell disruption beginning at 30 hpi. Prior to cell lysis, virus infection resulted in the formation of pyramid-like projections from the cell surface. These projections, which have not been documented in any other host-virus system, appeared to be caused by the protrusion of the cell membrane beyond the bordering S-layer. These structures are thought to be sites at which progeny virus particles are released from infected cells. Based on these observations of lysis, a plaque assay was developed for STIV. From these studies we propose an overall assembly model for STIV.

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UV resonance Raman spectroscopy of DNA and protein constituents of viruses: Assignments and cross sections for excitations at 257, 244, 238, and 229 nm

Wen

Thomas

1998

Biopolymers

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Ultraviolet resonance Raman (UVRR) spectra of H2O and D2O solutions of the nucleoside (dA, dG, dC, dT) and aromatic amino acid (Phe, Trp, Tyr) constituents of DNA viruses have been obtained with laser excitation wavelengths of 257, 244, 238, and 229 nm. Using the 981 cm−1 marker of Na2SO4 as an internal standard, Raman frequencies and scattering cross sections were evaluated for all prominent UVRR bands at each excitation wavelength. The results show that UVRR cross sections of both the nucleosides and amino acids are strongly dependent on excitation wavelength and constitute sensitive and selective probes of the residues. The results provide a library of UVRR marker bands for structural analysis of DNA viruses and other nucleoprotein assemblies. © 1998 John Wiley & Sons, Inc. Biopoly 45: 247–256, 1998

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Structure, Interactions and Dynamics ofPRD1Virus I. Coupling of Subunit Folding and Capsid Assembly

Cited by 42 publications

References 51 publications

Three-dimensional structure and function of the Paramecium bursaria chlorella virus capsid

Three-dimensional structure and function of the Paramecium bursaria chlorella virus capsid

Particle Assembly and Ultrastructural Features Associated with Replication of the Lytic Archaeal Virus Sulfolobus Turreted Icosahedral Virus

UV resonance Raman spectroscopy of DNA and protein constituents of viruses: Assignments and cross sections for excitations at 257, 244, 238, and 229 nm

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