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(Reference retrieved automatically from Web of Science through information on FAPESP grant and its corresponding number as mentioned in the publication by the authors.)

Crystal Structure of the Herpesvirus Nuclear Egress Complex Provides Insights into Inner Nuclear Membrane Remodeling

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Author(s):
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Zeev-Ben-Mordehai, Tzviya [1] ; Weberruss, Marion [2] ; Lorenz, Michael [2] ; Cheleski, Juliana [1] ; Hellberg, Teresa [3] ; Whittle, Cathy [1] ; El Omari, Kamel [1] ; Vasishtan, Daven [1] ; Dent, Kyle C. [1] ; Harlos, Karl [1] ; Franzke, Kati [3] ; Hagen, Christoph [1] ; Klupp, Barbara G. [3] ; Antonin, Wolfram [2] ; Mettenleiter, Thomas C. [3] ; Gruenewald, Kay [1]
Total Authors: 16
Affiliation:
[1] Univ Oxford, Div Struct Biol, Wellcome Trust Ctr Human Genet, Oxford OX3 7BN - England
[2] Max Planck Gesell, Friedrich Miescher Lab, D-72076 Tubingen - Germany
[3] Fed Res Inst Anim Hlth, Friedrich Loeffler Inst, Inst Mol Virol & Cell Biol, D-17493 Greifswald - Germany
Total Affiliations: 3
Document type: Journal article
Source: CELL REPORTS; v. 13, n. 12, p. 2645-2652, DEC 29 2015.
Web of Science Citations: 16
Abstract

Although nucleo-cytoplasmic transport is typically mediated through nuclear pore complexes, herpesvirus capsids exit the nucleus via a unique vesicular pathway. Together, the conserved herpesvirus proteins pUL31 and pUL34 form the heterodimeric nuclear egress complex (NEC), which, in turn, mediates the formation of tight-fitting membrane vesicles around capsids at the inner nuclear membrane. Here, we present the crystal structure of the pseudorabies virus NEC. The structure revealed that a zinc finger motif in pUL31 and an extensive interaction network between the two proteins stabilize the complex. Comprehensive mutational analyses, characterized both in situ and in vitro, indicated that the interaction network is not redundant but rather complementary. Fitting of the NEC crystal structure into the recently determined cryoEM-derived hexagonal lattice, formed in situ by pUL31 and pUL34, provided details on the molecular basis of NEC coat formation and inner nuclear membrane remodeling. (AU)

FAPESP's process: 13/24972-1 - Cryo-electron tomography to visualize macromolecular organization
Grantee:Juliana Cheleski Wiggers
Support Opportunities: Scholarships abroad - Research Internship - Post-doctor