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(Referência obtida automaticamente do Web of Science, por meio da informação sobre o financiamento pela FAPESP e o número do processo correspondente, incluída na publicação pelos autores.)

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

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Autor(es):
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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]
Número total de Autores: 16
Afiliação do(s) autor(es):
[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
Número total de Afiliações: 3
Tipo de documento: Artigo Científico
Fonte: CELL REPORTS; v. 13, n. 12, p. 2645-2652, DEC 29 2015.
Citações Web of Science: 16
Resumo

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)

Processo FAPESP: 13/24972-1 - Tomografia crio-eletrônica para visualizar a organização molecular
Beneficiário:Juliana Cheleski Wiggers
Linha de fomento: Bolsas no Exterior - Estágio de Pesquisa - Pós-Doutorado