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Signal peptide cleavage and internal targeting signals direct the hepatitis C virus p7 protein to distinct intracellular membranes

Signal peptide cleavage and internal targeting signals direct the hepatitis C virus p7 protein to distinct intracellular membranes
Signal peptide cleavage and internal targeting signals direct the hepatitis C virus p7 protein to distinct intracellular membranes
The hepatitis C virus (HCV) p7 protein forms an amantadine-sensitive ion channel required for viral replication in chimpanzees, though its precise role in the life cycle of HCV is unknown. In an attempt to gain some insights into p7 function, we examined the intracellular localization of p7 using epitope tags and an anti-p7 peptide antibody, antibody 1055. Immunofluorescence labeling of p7 at its C terminus revealed an endoplasmic reticulum (ER) localization independent of the presence of its signal peptide, whereas labeling the N terminus gave a mitochondrial-type distribution in brightly labeled cells. Both of these patterns could be visualized within individual cells, suggestive of separate pools of p7 where the N and C termini differed in accessibility to antibody. These patterns were disrupted by preventing signal peptide cleavage. Subcellular fractionation revealed that p7 was enriched in a heavy membrane fraction associated with mitochondria as well as normal ER-derived microsomes. The complex regulation of the intracellular distribution of p7 suggests that p7 plays multiple roles in the HCV life cycle either intracellularly or as a virion component.
0022-538X
15525-15536
Griffin, Stephen
49c409b7-ee50-4809-b6b8-d5e192ff7424
Clarke, Dean
b1581e06-6aa4-424f-bef7-28a85dfd7106
McCormick, Christopher
66875e85-4b9c-43ad-b2ae-d21ccb097d4e
Rowlands, David
44d4528a-2f27-4a75-8aea-d87453eb055a
Harris, Mark
065415f3-96a7-443c-91b4-f75a5945f82b
Griffin, Stephen
49c409b7-ee50-4809-b6b8-d5e192ff7424
Clarke, Dean
b1581e06-6aa4-424f-bef7-28a85dfd7106
McCormick, Christopher
66875e85-4b9c-43ad-b2ae-d21ccb097d4e
Rowlands, David
44d4528a-2f27-4a75-8aea-d87453eb055a
Harris, Mark
065415f3-96a7-443c-91b4-f75a5945f82b

Griffin, Stephen, Clarke, Dean, McCormick, Christopher, Rowlands, David and Harris, Mark (2005) Signal peptide cleavage and internal targeting signals direct the hepatitis C virus p7 protein to distinct intracellular membranes. Journal of Virology, 79 (24), 15525-15536. (doi:10.1128/JVI.79.24.15525-15536.2005).

Record type: Article

Abstract

The hepatitis C virus (HCV) p7 protein forms an amantadine-sensitive ion channel required for viral replication in chimpanzees, though its precise role in the life cycle of HCV is unknown. In an attempt to gain some insights into p7 function, we examined the intracellular localization of p7 using epitope tags and an anti-p7 peptide antibody, antibody 1055. Immunofluorescence labeling of p7 at its C terminus revealed an endoplasmic reticulum (ER) localization independent of the presence of its signal peptide, whereas labeling the N terminus gave a mitochondrial-type distribution in brightly labeled cells. Both of these patterns could be visualized within individual cells, suggestive of separate pools of p7 where the N and C termini differed in accessibility to antibody. These patterns were disrupted by preventing signal peptide cleavage. Subcellular fractionation revealed that p7 was enriched in a heavy membrane fraction associated with mitochondria as well as normal ER-derived microsomes. The complex regulation of the intracellular distribution of p7 suggests that p7 plays multiple roles in the HCV life cycle either intracellularly or as a virion component.

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Published date: 2005

Identifiers

Local EPrints ID: 27075
URI: http://eprints.soton.ac.uk/id/eprint/27075
ISSN: 0022-538X
PURE UUID: c0cb553c-f28d-415a-b938-642c6c4ca6ec

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Date deposited: 25 Apr 2006
Last modified: 15 Mar 2024 07:15

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Contributors

Author: Stephen Griffin
Author: Dean Clarke
Author: Christopher McCormick
Author: David Rowlands
Author: Mark Harris

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