The dengue virus M protein localises to the endoplasmic reticulum and forms oligomers
dc.contributor.author | Wong, S. | |
dc.contributor.author | Haqshenas, G. | |
dc.contributor.author | Gowans, E. | |
dc.contributor.author | MacKenzie, J. | |
dc.date.issued | 2012 | |
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. | |
dc.description.statementofresponsibility | Sook-San Wonga, Gholamreza Haqshenas, Eric J. Gowans, Jason Mackenzie | |
dc.identifier.citation | FEBS Letters, 2012; 586(7):1032-1037 | |
dc.identifier.doi | 10.1016/j.febslet.2012.02.047 | |
dc.identifier.issn | 0014-5793 | |
dc.identifier.issn | 1873-3468 | |
dc.identifier.orcid | Gowans, E. [0000-0002-4274-8311] | |
dc.identifier.uri | http://hdl.handle.net/2440/76007 | |
dc.language.iso | en | |
dc.publisher | Elsevier Science BV | |
dc.rights | Crown Copyright © 2012 Published by Elsevier B.V. on behalf of Federation of European Biochemical society. All rights reserved. | |
dc.source.uri | https://doi.org/10.1016/j.febslet.2012.02.047 | |
dc.subject | Dengue | |
dc.subject | PrM | |
dc.subject | M Protein | |
dc.subject | Localisation | |
dc.subject | Endoplasmic reticulum | |
dc.subject | Oligomerisation | |
dc.title | The dengue virus M protein localises to the endoplasmic reticulum and forms oligomers | |
dc.type | Journal article | |
pubs.publication-status | Published |