Structure of the Herpes Simplex Virus Capsid Molecular Composition of the Pentons and the Triplexes

Newcomb, William W.; Trus, Benes L.; Booy, Frank P.; Steven, Alasdair C.; Wall, Joseph S.; Brown, Jay C.

doi:10.1006/jmbi.1993.1406

Cited by 242 publications

(301 citation statements)

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“…The role of VP26 remains somewhat mysterious. It does not confer additional stability [45] and it is dispensable, although its absence somehow decreases infectious virion production [46]. Another consequence of HSV1 procapsid maturation is weakening of the interaction between the inner (scaffold) shell and the MCP.…”

Section: Capsid Maturation Of Herpes Simplex Virusmentioning

confidence: 99%

Virus maturation: dynamics and mechanism of a stabilizing structural transition that leads to infectivity

Steven

Heymann

Cheng

et al. 2005

Current Opinion in Structural Biology

160

143

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For many viruses, the final stage of assembly involves structural transitions that convert an innocuous precursor particle into an infectious agent. This process -maturation -is controlled by proteases that trigger large-scale conformational changes. In this context, protease inhibitor antiviral drugs act by blocking maturation. Recent work has succeeded in determining the folds of representative examples of the five major proteins -major capsid protein, scaffolding protein, portal, protease and accessory protein -that are typically involved in capsid assembly. These data provide a framework for detailed mechanistic investigations and elucidation of mutations that affect assembly in various ways. The nature of the conformational change has been elucidated: it entails rigid-body rotations and translations of the arrayed subunits that transfer the interactions between them to different molecular surfaces, accompanied by refolding and redeployment of local motifs. Moreover, it has been possible to visualize maturation at the submolecular level in movies based on time-resolved cryo-electron microscopy.

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Section: Capsid Maturation Of Herpes Simplex Virusmentioning

confidence: 99%

Virus maturation: dynamics and mechanism of a stabilizing structural transition that leads to infectivity

Steven

Heymann

Cheng

et al. 2005

Current Opinion in Structural Biology

160

143

View full text Add to dashboard Cite

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“…Studies using recombinant baculoviruses have shown that VP26 is not required for assembly of recognizable capsids (Tatman et aI., 1994;Thomsen et al, I994) and it can be removed from intact capsids without affecting their overall integrity (Newcomb & Brown, 1991;Newcomb et al, 1993). It is not yet known whether VP26 is essential for virus growth and its role in the capsid has not been established.…”

Section: Behaviour Of Vp26mentioning

confidence: 99%

Multiple Interactions Control the Intracellular Localization of the Herpes Simplex Virus Type 1 Capsid Proteins

Rixon

Addison

McGregor

et al. 1996

Journal of General Virology

106

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“…Limitations on the amount of UL37 protein which can be incorporated could result from interaction of this polypeptide with a component of the capsid. The stoichiometry of the proteins present in the capsid is essentially invariant (Newcomb et al, 1993) and this in turn could impose limits on the abundance of tegument components which interact with the capsid. However, the UL37 protein is present in equal abundance in vUL37IEP virions and L-particles and thus, while the UL37 protein could interact with the capsid, any such interaction cannot be the primary determinant which regulates the abundance of this protein in virus particles.…”

mentioning

confidence: 99%

The abundance of the herpes simplex virus type 1 UL37 tegument protein in virus particles is closely controlled.

McLauchlan¹

1997

Journal of General Virology

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The tegument region of herpes simplex virus type 1 virus particles contains approximately 15 virusencoded polypeptide species. One of the less abundant species is a 120 kDa protein specified by gene UL37. The abundance of the UL37 protein in infected cells was increased about 20-fold by replacing the native promoter for gene UL37 with the strong immediate early promoter of human cytomegalovirus. This rise in abundance did not induce any detectable increase in the amount of UL37 protein incorporated into virus particles. These data contrast with those previously obtained for a second tegument protein VP22 whose level of incorporation was elevated by increasing its abundance in infected cells. Thus, for the UL37 protein, a mechanism exists to control its abundance in the tegument. Moreover, data obtained with light particles which lack the viral capsid suggest that this controlled incorporation is not directed by interaction with the capsid structure.

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Structure of the Herpes Simplex Virus Capsid Molecular Composition of the Pentons and the Triplexes

Cited by 242 publications

References 0 publications

Virus maturation: dynamics and mechanism of a stabilizing structural transition that leads to infectivity

Virus maturation: dynamics and mechanism of a stabilizing structural transition that leads to infectivity

Multiple Interactions Control the Intracellular Localization of the Herpes Simplex Virus Type 1 Capsid Proteins

The abundance of the herpes simplex virus type 1 UL37 tegument protein in virus particles is closely controlled.

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