The herpes simplex virus procapsid: structure, conformational changes upon maturation, and roles of the triplex proteins VP19c and VP23 in assembly

Trus, Benes L.; Booy, Frank P.; Newcomb, William W.; Brown, Jay C.; Homa, Fred L.; Thomsen, Darrell R.; Steven, Alasdair C.

doi:10.1016/s0022-2836(96)80018-0

Cited by 215 publications

(215 citation statements)

References 47 publications

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“…Studies of ϕ29 can help pinpoint the capsid structural changes that accompany DNA packaging and that, thus far, have only been inferred by comparison of procapsids and mature particles in other viral systems. These include the ssDNA bacteriophage ϕX174 (Ilag et al, 1995;Dokland et al, 1997); the dsDNA bacteriophages P22 (Prasad et al, 1993), λ (Dokland and Murialdo, 1993), and HK97 (Conway et al, 1995); and also the mammalian herpes simplex virus (Trus et al, 1996;Zhou et al, 1998).…”

Section: Introductionmentioning

confidence: 99%

Assembly of a Tailed Bacterial Virus and Its Genome Release Studied in Three Dimensions

Tao¹,

Olson²,

Wang³

et al. 2014

Selected Papers of Michael G Rossmann With Commentaries

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SummaryWe present the first three-dimensional reconstruction of a prolate, tailed phage, and its empty prohead precursor by cryo-electron microscopy. The head-tail connector, the central component of the DNA packaging machine, is visualized for the first time in situ within the Bacillus subtilis dsDNA phage ϕ29. The connector, with 12-or 13-fold symmetry, appears to fit loosely into a pentameric vertex of the head, a symmetry mismatch that may be required to rotate the connector to package DNA. The prolate head of ϕ29 has 10 hexameric units in its cylindrical equatorial region, and 11 pentameric and 20 hexameric units comprise icosahedral end-caps with T=3 quasisymmetry. Reconstruction of an emptied phage particle shows that the connector and neck/tail assembly undergo significant conformational changes upon ejection of DNA.

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Section: Introductionmentioning

confidence: 99%

Assembly of a Tailed Bacterial Virus and Its Genome Release Studied in Three Dimensions

Tao¹,

Olson²,

Wang³

et al. 2014

Selected Papers of Michael G Rossmann With Commentaries

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“…[7][8][9] Proteins residing in the underlying tegument are responsible for initiating gene expression from the viral genome, 10,11 shutting off host cell protein synthesis, 12,13 and assist in virion maturation and egress. [14][15][16][17][18] The virion proteins VP5, VP19c, VP23, and VP26 [19][20][21][22] form the icosadeltahedral capsid that encases the double-stranded DNA genome. The 152 kb viral genome encodes 84 genes (Figure 1b), and consists of a unique long (U L ) and a unique short (U S ) segment (Figure 1b) each flanked by repeat sequences (ab, b 0 a 0 , a 0 c 0 ca) [23][24][25][26][27] that can invert relative to one another.…”

Section: Introductionmentioning

confidence: 99%

HSV trafficking and development of gene therapy vectors with applications in the nervous system

et al. 2005

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Herpes simplex virus type 1 (HSV-1) is a neurotropic doublestranded DNA virus that causes cold sores, keratitis, and rarely encephalitis in humans. Nonpathogenic HSV-1 gene transfer vectors have been generated by elimination of viral functions necessary for replication. The life cycle of the native virus includes replication in epithelial cells at the site of initial inoculation followed by retrograde axonal transport to the nuclei of sensory neurons innervating the area of cutaneous primary infection. In this review, we summarize the current understanding of the molecular basis for HSV cell entry, nuclear transport of the genome, virion egress following replication, and retrograde and anterograde axonal transport in neurons. We discuss how each of these properties has been exploited or modified to allow the generation of gene transfer vectors with particular utility for neurological applications. Recent advances in engineering virus entry have provided proof of principle that vector targeting is possible. Furthermore, significant and potentially therapeutic modifications to the pathological responses to various noxious insults have been demonstrated in models of peripheral nerve disease. These applications exploit the natural axonal transport mechanism of HSV, allowing transgene expression in the cell nucleus within the inaccessible trigeminal ganglion or dorsal root ganglion, following the noninvasive procedure of subcutaneous vector inoculation. These findings demonstrate the importance of understanding basic virology in the design of vector systems and the powerful approach of exploiting favorable properties of the parent virus in the generation of gene transfer vectors. Gene Therapy (2005) 12, 891-901.

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“…Self-associated pAP and pPR constitute the protein scaffold of a sphere with the MCP on its surface. Several additional viral proteins participate in assembling this fragile procapsid (about 124 nm in diameter [29]) by binding to the MCP and/or the portal [30][31][32][33][34][35]. The ratio of pPR and pAP in the procapsid is 1 : 10 4 .…”

Section: Introductionmentioning

confidence: 99%

“…1a, b), which leads to the release of the scaffold from the MCP and the portal. This causes conformational changes and the labile, spherical procapsid matures to the stable, icosahedral capsid [31,33,40]. Consequently, this cleavage site is called maturational site (M-site) [41].…”

Section: Introductionmentioning

confidence: 99%

Assemblins as maturational proteases in herpesviruses

Zühlsdorf

Hinrichs

2017

Journal of General Virology

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During assembly of herpesvirus capsids, a protein scaffold self-assembles to ring-like structures forming the scaffold of the spherical procapsids. Proteolytic activity of the herpesvirus maturational protease causes structural changes that result in angularization of the capsids. In those mature icosahedral capsids, the packaging of viral DNA into the capsids can take place. The strictly regulated protease is called assemblin. It is inactive in its monomeric state and activated by dimerization. The structures of the dimeric forms of several assemblins from all herpesvirus subfamilies have been elucidated in the last two decades. They revealed a unique serine-protease fold with a catalytic triad consisting of a serine and two histidines. Inhibitors that disturb dimerization by binding to the dimerization area were found recently. Additionally, the structure of the monomeric form of assemblin from pseudorabies virus and some monomer-like structures of Kaposi's sarcoma-associated herpesvirus assemblin were solved. These findings are the proof-of-principle for the development of new anti-herpesvirus drugs. Therefore, the most important information on this fascinating and unique class of proteases is summarized here.

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The herpes simplex virus procapsid: structure, conformational changes upon maturation, and roles of the triplex proteins VP19c and VP23 in assembly

Cited by 215 publications

References 47 publications

Assembly of a Tailed Bacterial Virus and Its Genome Release Studied in Three Dimensions

Assembly of a Tailed Bacterial Virus and Its Genome Release Studied in Three Dimensions

HSV trafficking and development of gene therapy vectors with applications in the nervous system

Assemblins as maturational proteases in herpesviruses

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