Rhinovirus 3C Protease Can Localize in the Nucleus and Alter Active and Passive Nucleocytoplasmic Transport

Reena Ghildyal, Benjamin Jordan, Dongsheng Li, Hayat Dagher, Phillip G Bardin, James E Gern, David A Jans

Research output: Contribution to journalArticle

39 Citations (Scopus)

Abstract

The degradation of nuclear pore components and disruption of nucleocytoplasmic trafficking during rhinovirus infection have been attributed to viral 2A protease. Here we show for the first time that rhinovirus 3C protease may also have a role. Specifically, we show that 3C and its precursor, 3CD, can target green fluorescent protein to the nucleus of living cells, leading to degradation of nuclear pore components, and that incubation with recombinant 3C disrupts active and passive nucleocytoplasmic transport in a semi-intact cell nuclear transport system dependent on 3C protease activity. 3C may thus contribute to host cell shutoff in infected cells by localizing in the nucleus and facilitating nuclear pore breakdown.

Original languageEnglish
Pages (from-to)7349-7352
Number of pages4
JournalJournal of Virology
Volume83
Issue number14
DOIs
Publication statusPublished - Jul 2009
Externally publishedYes

Fingerprint

nucleocytoplasmic transport
Nuclear Pore
Enterovirus
Cell Nucleus Active Transport
nuclear membrane
proteinases
Rhinovirus
cells
Green Fluorescent Proteins
Cell Nucleus
degradation
Peptide Hydrolases
green fluorescent protein
Infection
3C proteases
infection

Cite this

Ghildyal, Reena ; Jordan, Benjamin ; Li, Dongsheng ; Dagher, Hayat ; Bardin, Phillip G ; Gern, James E ; Jans, David A. / Rhinovirus 3C Protease Can Localize in the Nucleus and Alter Active and Passive Nucleocytoplasmic Transport. In: Journal of Virology. 2009 ; Vol. 83, No. 14. pp. 7349-7352.
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abstract = "The degradation of nuclear pore components and disruption of nucleocytoplasmic trafficking during rhinovirus infection have been attributed to viral 2A protease. Here we show for the first time that rhinovirus 3C protease may also have a role. Specifically, we show that 3C and its precursor, 3CD, can target green fluorescent protein to the nucleus of living cells, leading to degradation of nuclear pore components, and that incubation with recombinant 3C disrupts active and passive nucleocytoplasmic transport in a semi-intact cell nuclear transport system dependent on 3C protease activity. 3C may thus contribute to host cell shutoff in infected cells by localizing in the nucleus and facilitating nuclear pore breakdown.",
keywords = "Active Transport, Cell Nucleus, Animals, COS Cells, Cell Line, Cell Nucleus, Cercopithecus aethiops, Cysteine Endopeptidases, Cytoplasm, Humans, Picornaviridae Infections, Protein Transport, Rhinovirus, Viral Proteins, Journal Article, Research Support, Non-U.S. Gov't",
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Rhinovirus 3C Protease Can Localize in the Nucleus and Alter Active and Passive Nucleocytoplasmic Transport. / Ghildyal, Reena; Jordan, Benjamin; Li, Dongsheng; Dagher, Hayat; Bardin, Phillip G; Gern, James E; Jans, David A.

In: Journal of Virology, Vol. 83, No. 14, 07.2009, p. 7349-7352.

Research output: Contribution to journalArticle

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T1 - Rhinovirus 3C Protease Can Localize in the Nucleus and Alter Active and Passive Nucleocytoplasmic Transport

AU - Ghildyal, Reena

AU - Jordan, Benjamin

AU - Li, Dongsheng

AU - Dagher, Hayat

AU - Bardin, Phillip G

AU - Gern, James E

AU - Jans, David A

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AB - The degradation of nuclear pore components and disruption of nucleocytoplasmic trafficking during rhinovirus infection have been attributed to viral 2A protease. Here we show for the first time that rhinovirus 3C protease may also have a role. Specifically, we show that 3C and its precursor, 3CD, can target green fluorescent protein to the nucleus of living cells, leading to degradation of nuclear pore components, and that incubation with recombinant 3C disrupts active and passive nucleocytoplasmic transport in a semi-intact cell nuclear transport system dependent on 3C protease activity. 3C may thus contribute to host cell shutoff in infected cells by localizing in the nucleus and facilitating nuclear pore breakdown.

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KW - Animals

KW - COS Cells

KW - Cell Line

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KW - Picornaviridae Infections

KW - Protein Transport

KW - Rhinovirus

KW - Viral Proteins

KW - Journal Article

KW - Research Support, Non-U.S. Gov't

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