A pUL25 dimer interfaces the pseudorabies virus capsid and tegument

Yun Tao Liu; Jiansen Jiang; Kevin Patrick Bohannon; Xinghong Dai; G. W. Gant Luxton; Wong Hoi Hui; Guo Qiang Bi; Gregory Allan Smith; Z. Hong Zhou

doi:10.1099/jgv.0.000903

A pUL25 dimer interfaces the pseudorabies virus capsid and tegument

Yun Tao Liu, Jiansen Jiang, Kevin Patrick Bohannon, Xinghong Dai, G. W. Gant Luxton, Wong Hoi Hui, Guo Qiang Bi, Gregory Allan Smith, Z. Hong Zhou

Genetics, Cell Biology and Development (CBS)

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

23 Scopus citations

Abstract

Inside the virions of α-herpesviruses, tegument protein pUL25 anchors the tegument to capsid vertices through direct interactions with tegument proteins pUL17 and pUL36. In addition to promoting virion assembly, both pUL25 and pUL36 are critical for intracellular microtubule-dependent capsid transport. Despite these essential roles during infection, the stoichiometry and precise organization of pUL25 and pUL36 on the capsid surface remain controversial due to the insufficient resolution of existing reconstructions from cryo-electron microscopy (cryoEM). Here, we report a threedimensional (3D) icosahedral reconstruction of pseudorabies virus (PRV), a varicellovirus of the α-herpesvirinae subfamily, obtained by electron-counting cryoEM at 4.9 Å resolution. Our reconstruction resolves a dimer of pUL25 forming a capsidassociated tegument complex with pUL36 and pUL17 through a coiled coil helix bundle, thus correcting previous misinterpretations. A comparison between reconstructions of PRV and the γ-herpesvirus Kaposi’s sarcoma-associated herpesvirus (KSHV) reinforces their similar architectures and establishes important subfamily differences in the capsid-tegument interface.

Original language	English (US)
Article number	000903
Pages (from-to)	2837-2849
Number of pages	13
Journal	Journal of General Virology
Volume	98
Issue number	11
DOIs	https://doi.org/10.1099/jgv.0.000903
State	Published - Nov 2017

Bibliographical note

Funding Information:
This research was supported in part by grants from the US National Institutes of Health (R01 AI056346 to G. A. S.), the NSFC (313290002 to Z. H. Z.) and the CAS (XDB02050000 to G. Q. B.). We acknowledge the use of instruments at the Electron Imaging Center for Nanoma-chines supported by UCLA and by instrumentation grants from NIH (1S10RR23057) and NSF (DBI-1338135). The cryoEM density map has been deposited in the EM Data Bank under the accession codes EMD-8760.

Publisher Copyright:
© 2017 The Authors.

Keywords

CryoEM
PUL17
PUL25 dimer
PUL36 (VP1/2)
Pseudorabies virus
Tegument proteins

UN SDGs

This output contributes to the following UN Sustainable Development Goals (SDGs)

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10.1099/jgv.0.000903

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title = "A pUL25 dimer interfaces the pseudorabies virus capsid and tegument",

abstract = "Inside the virions of α-herpesviruses, tegument protein pUL25 anchors the tegument to capsid vertices through direct interactions with tegument proteins pUL17 and pUL36. In addition to promoting virion assembly, both pUL25 and pUL36 are critical for intracellular microtubule-dependent capsid transport. Despite these essential roles during infection, the stoichiometry and precise organization of pUL25 and pUL36 on the capsid surface remain controversial due to the insufficient resolution of existing reconstructions from cryo-electron microscopy (cryoEM). Here, we report a threedimensional (3D) icosahedral reconstruction of pseudorabies virus (PRV), a varicellovirus of the α-herpesvirinae subfamily, obtained by electron-counting cryoEM at 4.9 {\AA} resolution. Our reconstruction resolves a dimer of pUL25 forming a capsidassociated tegument complex with pUL36 and pUL17 through a coiled coil helix bundle, thus correcting previous misinterpretations. A comparison between reconstructions of PRV and the γ-herpesvirus Kaposi{\textquoteright}s sarcoma-associated herpesvirus (KSHV) reinforces their similar architectures and establishes important subfamily differences in the capsid-tegument interface.",

keywords = "CryoEM, PUL17, PUL25 dimer, PUL36 (VP1/2), Pseudorabies virus, Tegument proteins",

author = "Liu, {Yun Tao} and Jiansen Jiang and Bohannon, {Kevin Patrick} and Xinghong Dai and {Gant Luxton}, {G. W.} and Hui, {Wong Hoi} and Bi, {Guo Qiang} and Smith, {Gregory Allan} and Zhou, {Z. Hong}",

note = "Funding Information: This research was supported in part by grants from the US National Institutes of Health (R01 AI056346 to G. A. S.), the NSFC (313290002 to Z. H. Z.) and the CAS (XDB02050000 to G. Q. B.). We acknowledge the use of instruments at the Electron Imaging Center for Nanoma-chines supported by UCLA and by instrumentation grants from NIH (1S10RR23057) and NSF (DBI-1338135). The cryoEM density map has been deposited in the EM Data Bank under the accession codes EMD-8760. Publisher Copyright: {\textcopyright} 2017 The Authors.",

year = "2017",

month = nov,

doi = "10.1099/jgv.0.000903",

language = "English (US)",

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T1 - A pUL25 dimer interfaces the pseudorabies virus capsid and tegument

AU - Liu, Yun Tao

AU - Jiang, Jiansen

AU - Bohannon, Kevin Patrick

AU - Dai, Xinghong

AU - Gant Luxton, G. W.

AU - Hui, Wong Hoi

AU - Bi, Guo Qiang

AU - Smith, Gregory Allan

AU - Zhou, Z. Hong

N1 - Funding Information: This research was supported in part by grants from the US National Institutes of Health (R01 AI056346 to G. A. S.), the NSFC (313290002 to Z. H. Z.) and the CAS (XDB02050000 to G. Q. B.). We acknowledge the use of instruments at the Electron Imaging Center for Nanoma-chines supported by UCLA and by instrumentation grants from NIH (1S10RR23057) and NSF (DBI-1338135). The cryoEM density map has been deposited in the EM Data Bank under the accession codes EMD-8760. Publisher Copyright: © 2017 The Authors.

PY - 2017/11

Y1 - 2017/11

N2 - Inside the virions of α-herpesviruses, tegument protein pUL25 anchors the tegument to capsid vertices through direct interactions with tegument proteins pUL17 and pUL36. In addition to promoting virion assembly, both pUL25 and pUL36 are critical for intracellular microtubule-dependent capsid transport. Despite these essential roles during infection, the stoichiometry and precise organization of pUL25 and pUL36 on the capsid surface remain controversial due to the insufficient resolution of existing reconstructions from cryo-electron microscopy (cryoEM). Here, we report a threedimensional (3D) icosahedral reconstruction of pseudorabies virus (PRV), a varicellovirus of the α-herpesvirinae subfamily, obtained by electron-counting cryoEM at 4.9 Å resolution. Our reconstruction resolves a dimer of pUL25 forming a capsidassociated tegument complex with pUL36 and pUL17 through a coiled coil helix bundle, thus correcting previous misinterpretations. A comparison between reconstructions of PRV and the γ-herpesvirus Kaposi’s sarcoma-associated herpesvirus (KSHV) reinforces their similar architectures and establishes important subfamily differences in the capsid-tegument interface.

AB - Inside the virions of α-herpesviruses, tegument protein pUL25 anchors the tegument to capsid vertices through direct interactions with tegument proteins pUL17 and pUL36. In addition to promoting virion assembly, both pUL25 and pUL36 are critical for intracellular microtubule-dependent capsid transport. Despite these essential roles during infection, the stoichiometry and precise organization of pUL25 and pUL36 on the capsid surface remain controversial due to the insufficient resolution of existing reconstructions from cryo-electron microscopy (cryoEM). Here, we report a threedimensional (3D) icosahedral reconstruction of pseudorabies virus (PRV), a varicellovirus of the α-herpesvirinae subfamily, obtained by electron-counting cryoEM at 4.9 Å resolution. Our reconstruction resolves a dimer of pUL25 forming a capsidassociated tegument complex with pUL36 and pUL17 through a coiled coil helix bundle, thus correcting previous misinterpretations. A comparison between reconstructions of PRV and the γ-herpesvirus Kaposi’s sarcoma-associated herpesvirus (KSHV) reinforces their similar architectures and establishes important subfamily differences in the capsid-tegument interface.

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KW - PUL36 (VP1/2)

KW - Pseudorabies virus

KW - Tegument proteins

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A pUL25 dimer interfaces the pseudorabies virus capsid and tegument

Abstract

Bibliographical note

Keywords

UN SDGs

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