The N-terminal region of severe acute respiratory syndrome coronavirus protein 6 induces membrane rearrangement and enhances virus replication

Haixia Zhou; Debra Ferraro; Jincun Zhao; Snawar Hussain; Jianqiang Shao; Jonathan Trujillo; Jason Netland; Thomas Gallagher; Stanley Perlman

doi:10.1128/JVI.02570-09

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The N-terminal region of severe acute respiratory syndrome coronavirus protein 6 induces membrane rearrangement and enhances virus replication

Journal article

Open access

Peer reviewed

The N-terminal region of severe acute respiratory syndrome coronavirus protein 6 induces membrane rearrangement and enhances virus replication

Haixia Zhou, Debra Ferraro, Jincun Zhao, Snawar Hussain, Jianqiang Shao, Jonathan Trujillo, Jason Netland, Thomas Gallagher and Stanley Perlman

Journal of virology, Vol.84(7), pp.3542-3551

04/2010

DOI: 10.1128/JVI.02570-09

PMCID: PMC2838104

PMID: 20106914

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Abstract

The severe acute respiratory syndrome coronavirus (SARS-CoV) accessory protein 6 (p6) is a 63-amino-acid multifunctional Golgi-endoplasmic reticulum (ER) membrane-associated protein, with roles in enhancing virus replication and in evading the innate immune response to infection by inhibiting STAT1 (signal transducer and activator of transcription factor 1) translocation to the nucleus. Here, we demonstrate that p6 has an N-terminal region-cytoplasm-C-terminal region-cytoplasm configuration with residues 2 to 37 likely membrane embedded. Expression of p6, or of its N-terminal 41-amino-acid region, in the absence of other viral proteins, induced the formation of membranous structures, some of which were similar to double membrane vesicles involved in virus replication. Consistent with a role in virus replication, p6 partially colocalized with nonstructural protein 3 (nsp3), a marker for virus replication complexes. Further, while the C-terminal region is required for preventing STAT1 translocation to the nucleus, our results also indicated that the N-terminal 18 amino acids were necessary for maximal inhibition. Collectively, these results support the notion that p6 is a two-domain protein, although the function of each is not completely independent of the other.

Cell Membrane - chemistry

STAT1 Transcription Factor - metabolism

Protein Structure, Secondary

Virus Replication

Viral Proteins - chemistry

Humans

Cells, Cultured

Viral Proteins - physiology

SARS Virus - physiology

Active Transport, Cell Nucleus

Protein Transport

Details

Title: Subtitle: The N-terminal region of severe acute respiratory syndrome coronavirus protein 6 induces membrane rearrangement and enhances virus replication
Creators: Haixia Zhou - Department of Microbiology, University of Iowa, 3-712 BSB, Iowa City, IA 52242, USA
Debra Ferraro
Jincun Zhao
Snawar Hussain
Jianqiang Shao
Jonathan Trujillo
Jason Netland
Thomas Gallagher
Stanley Perlman
Resource Type: Journal article
Publication Details: Journal of virology, Vol.84(7), pp.3542-3551
DOI: 10.1128/JVI.02570-09
PMID: 20106914
PMCID: PMC2838104
NLM abbreviation: J Virol
ISSN: 0022-538X
eISSN: 1098-5514
Publisher: United States
Grant note: T32 HL07638 / NHLBI NIH HHS P01 AI060699 / NIAID NIH HHS T32 GM007337 / NIGMS NIH HHS T32 HL007638 / NHLBI NIH HHS
Language: English
Date published: 04/2010
Academic Unit: Microbiology and Immunology; Stead Family Department of Pediatrics; Iowa Neuroscience Institute; Infectious Disease (Pediatrics)
Record Identifier: 9983777471302771

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