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

Tzviya Zeev-Ben-Mordehai; Marion Weberruss; Michael Lorenz; Juliana Cheleski; Teresa Hellberg; Cathy Whittle; Kamel El Omari; Daven Vasishtan; Kyle C. Dent; Karl Harlos; Kati Franzke; Christoph Hagen; Barbara G. Klupp; Wolfram Antonin; Thomas C. Mettenleiter; Kay Gruenewald

doi:10.1016/j.celrep.2015.11.008

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

Tzviya Zeev-Ben-Mordehai, Marion Weberruss, Michael Lorenz, Juliana Cheleski, Teresa Hellberg, Cathy Whittle, Kamel El Omari, Daven Vasishtan, Kyle C. Dent, Karl Harlos, Kati Franzke, Christoph Hagen, Barbara G. Klupp, Wolfram Antonin, Thomas C. Mettenleiter, Kay Gruenewald

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Research output: Contribution to journal › Article › Academic › peer-review

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.

Original language	English
Pages (from-to)	2645-2652
Number of pages	8
Journal	Cell Reports
Volume	13
Issue number	12
DOIs	https://doi.org/10.1016/j.celrep.2015.11.008
Publication status	Published - 29 Dec 2015
Externally published	Yes

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10.1016/j.celrep.2015.11.008

1-s2.0-S2211124715012954-mainFinal published version, 3.42 MBLicence: CC BY

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Zeev-Ben-Mordehai, T., Weberruss, M., Lorenz, M., Cheleski, J., Hellberg, T., Whittle, C., El Omari, K., Vasishtan, D., Dent, K. C., Harlos, K., Franzke, K., Hagen, C., Klupp, B. G., Antonin, W., Mettenleiter, T. C., & Gruenewald, K. (2015). Crystal Structure of the Herpesvirus Nuclear Egress Complex Provides Insights into Inner Nuclear Membrane Remodeling. Cell Reports, 13(12), 2645-2652. https://doi.org/10.1016/j.celrep.2015.11.008

@article{86d7e168762d4cac8a65d26731bb11cd,

title = "Crystal Structure of the Herpesvirus Nuclear Egress Complex Provides Insights into Inner Nuclear Membrane Remodeling",

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.",

author = "Tzviya Zeev-Ben-Mordehai and Marion Weberruss and Michael Lorenz and Juliana Cheleski and Teresa Hellberg and Cathy Whittle and {El Omari}, Kamel and Daven Vasishtan and Dent, {Kyle C.} and Karl Harlos and Kati Franzke and Christoph Hagen and Klupp, {Barbara G.} and Wolfram Antonin and Mettenleiter, {Thomas C.} and Kay Gruenewald",

year = "2015",

month = dec,

day = "29",

doi = "10.1016/j.celrep.2015.11.008",

language = "English",

volume = "13",

pages = "2645--2652",

journal = "Cell Reports",

issn = "2211-1247",

publisher = "Elsevier Saunders",

number = "12",

}

Zeev-Ben-Mordehai, T, Weberruss, M, Lorenz, M, Cheleski, J, Hellberg, T, Whittle, C, El Omari, K, Vasishtan, D, Dent, KC, Harlos, K, Franzke, K, Hagen, C, Klupp, BG, Antonin, W, Mettenleiter, TC & Gruenewald, K 2015, 'Crystal Structure of the Herpesvirus Nuclear Egress Complex Provides Insights into Inner Nuclear Membrane Remodeling', Cell Reports, vol. 13, no. 12, pp. 2645-2652. https://doi.org/10.1016/j.celrep.2015.11.008

TY - JOUR

T1 - Crystal Structure of the Herpesvirus Nuclear Egress Complex Provides Insights into Inner Nuclear Membrane Remodeling

AU - Zeev-Ben-Mordehai, Tzviya

AU - Weberruss, Marion

AU - Lorenz, Michael

AU - Cheleski, Juliana

AU - Hellberg, Teresa

AU - Whittle, Cathy

AU - El Omari, Kamel

AU - Vasishtan, Daven

AU - Dent, Kyle C.

AU - Harlos, Karl

AU - Franzke, Kati

AU - Hagen, Christoph

AU - Klupp, Barbara G.

AU - Antonin, Wolfram

AU - Mettenleiter, Thomas C.

AU - Gruenewald, Kay

PY - 2015/12/29

Y1 - 2015/12/29

N2 - 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.

AB - 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.

U2 - 10.1016/j.celrep.2015.11.008

DO - 10.1016/j.celrep.2015.11.008

M3 - Article

SN - 2211-1247

VL - 13

SP - 2645

EP - 2652

JO - Cell Reports

JF - Cell Reports

IS - 12

ER -

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

Abstract

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