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- Publisher Website: 10.1016/j.febslet.2012.02.047
- Scopus: eid_2-s2.0-84859266464
- PMID: 22569259
- WOS: WOS:000302268400015
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Article: The dengue virus M protein localises to the endoplasmic reticulum and forms oligomers
Title | The dengue virus M protein localises to the endoplasmic reticulum and forms oligomers |
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Authors | |
Keywords | Dengue Endoplasmic reticulum Localisation M Protein Oligomerisation PrM |
Issue Date | 2012 |
Citation | FEBS Letters, 2012, v. 586, n. 7, p. 1032-1037 How to Cite? |
Abstract | The dengue virus membrane (M) protein is a key component of the mature virion. Here, we characterised the cellular behaviour of M using a recombinant protein construct to understand its inherent properties. Using confocal microscopy, we showed that M and its intracellular precursor, prM, localised to the endoplasmic reticulum. M protein was also detected on the cell surface and secreted, suggesting that M can enter the secretory pathway. In addition, cross-linking studies showed that M can form dimers and tetramers. These findings suggest that M behaves as a secretory protein analogous to the major envelope protein E. © 2012 Federation of European Biochemical Societies. Published by Elsevier B.V. All rights reserved. |
Persistent Identifier | http://hdl.handle.net/10722/311928 |
ISSN | 2023 Impact Factor: 3.0 2023 SCImago Journal Rankings: 1.208 |
ISI Accession Number ID |
DC Field | Value | Language |
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dc.contributor.author | Wong, Sook San | - |
dc.contributor.author | Haqshenas, Gholamreza | - |
dc.contributor.author | Gowans, Eric J. | - |
dc.contributor.author | MacKenzie, Jason | - |
dc.date.accessioned | 2022-04-06T04:31:47Z | - |
dc.date.available | 2022-04-06T04:31:47Z | - |
dc.date.issued | 2012 | - |
dc.identifier.citation | FEBS Letters, 2012, v. 586, n. 7, p. 1032-1037 | - |
dc.identifier.issn | 0014-5793 | - |
dc.identifier.uri | http://hdl.handle.net/10722/311928 | - |
dc.description.abstract | The dengue virus membrane (M) protein is a key component of the mature virion. Here, we characterised the cellular behaviour of M using a recombinant protein construct to understand its inherent properties. Using confocal microscopy, we showed that M and its intracellular precursor, prM, localised to the endoplasmic reticulum. M protein was also detected on the cell surface and secreted, suggesting that M can enter the secretory pathway. In addition, cross-linking studies showed that M can form dimers and tetramers. These findings suggest that M behaves as a secretory protein analogous to the major envelope protein E. © 2012 Federation of European Biochemical Societies. Published by Elsevier B.V. All rights reserved. | - |
dc.language | eng | - |
dc.relation.ispartof | FEBS Letters | - |
dc.subject | Dengue | - |
dc.subject | Endoplasmic reticulum | - |
dc.subject | Localisation | - |
dc.subject | M Protein | - |
dc.subject | Oligomerisation | - |
dc.subject | PrM | - |
dc.title | The dengue virus M protein localises to the endoplasmic reticulum and forms oligomers | - |
dc.type | Article | - |
dc.description.nature | link_to_subscribed_fulltext | - |
dc.identifier.doi | 10.1016/j.febslet.2012.02.047 | - |
dc.identifier.pmid | 22569259 | - |
dc.identifier.scopus | eid_2-s2.0-84859266464 | - |
dc.identifier.volume | 586 | - |
dc.identifier.issue | 7 | - |
dc.identifier.spage | 1032 | - |
dc.identifier.epage | 1037 | - |
dc.identifier.eissn | 1873-3468 | - |
dc.identifier.isi | WOS:000302268400015 | - |