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The stem region of premembrane protein plays an important role in the virus surface protein rearrangement during dengue maturation

Zhang, Q. and Hunke, C. and Yau, Y. H. and Seow, V. and Lee, S. and Tanner, L. B. and Guan, X. L. and Wenk, M. R. and Fibriansah, G. and Chew, P. L. and Kukkaro, P. and Biukovic, G. and Shi, P. Y. and Shochat, S. G. and Gruber, G. and Lok, S. M.. (2012) The stem region of premembrane protein plays an important role in the virus surface protein rearrangement during dengue maturation. Journal of biological chemistry, Vol. 287, H. 48. pp. 40525-40534.

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Official URL: http://edoc.unibas.ch/dok/A6094429

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Abstract

Newly assembled dengue viruses (DENV) undergo maturation to become infectious particles. The maturation process involves major rearrangement of virus surface premembrane (prM) and envelope (E) proteins. The prM-E complexes on immature viruses are first assembled as trimeric spikes in the neutral pH environment of the endoplasmic reticulum. When the virus is transported to the low pH environment of the exosomes, these spikes rearrange into dimeric structures, which lie parallel to the virus lipid envelope. The proteins involved in driving this process are unknown. Previous cryoelectron microscopy studies of the mature DENV showed that the prM-stem region (residues 111-131) is membrane-associated and may interact with the E proteins. Here we investigated the prM-stem region in modulating the virus maturation process. The binding of the prM-stem region to the E protein was shown to increase significantly at low pH compared with neutral pH in ELISAs and surface plasmon resonance studies. In addition, the affinity of the prM-stem region for the liposome, as measured by fluorescence correlation spectroscopy, was also increased when pH is lowered. These results suggest that the prM-stem region forms a tight association with the virus membrane and attracts the associated E protein in the low pH environment of exosomes. This will lead to the surface protein rearrangement observed during maturation
Faculties and Departments:09 Associated Institutions > Swiss Tropical and Public Health Institute (Swiss TPH) > Department of Medical Parasitology and Infection Biology > Molecular Immunology (Pluschke)
UniBasel Contributors:Guan, Xueli
Item Type:Article, refereed
Article Subtype:Research Article
Bibsysno:Link to catalogue
Publisher:American Society of Biological Chemists
ISSN:0021-9258
Note:Publication type according to Uni Basel Research Database: Journal article
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Last Modified:19 Jul 2013 07:43
Deposited On:19 Jul 2013 07:39

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