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  The non-structural 3 (NS3) protein of dengue virus type 2 interacts with human nuclear receptor binding protein and is associated with alterations in membrane structure.

Chua, J. J. E., Ng, M. M. L., & Chow, V. T. K. (2004). The non-structural 3 (NS3) protein of dengue virus type 2 interacts with human nuclear receptor binding protein and is associated with alterations in membrane structure. Virus Research, 102(2), 151-163. doi:10.1016/j.virusres.2004.01.025.

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Item Permalink: http://hdl.handle.net/11858/00-001M-0000-0018-0AE4-1 Version Permalink: http://hdl.handle.net/11858/00-001M-0000-0027-C5B8-4
Genre: Journal Article

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1952174.pdf (Publisher version), 516KB
 
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 Creators:
Chua, J. J. E.1, Author              
Ng, M. M. L., Author
Chow , V. T. K., Author
Affiliations:
1Research Group of Protein Trafficking in Synaptic Development and Function, MPI for Biophysical Chemistry, Max Planck Society, ou_1933287              

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Free keywords: Dengue virus type 2; Non-structural 3 protein; Nuclear receptor binding protein; Protein-protein interactions; Membrane alterations; Dengue pathogenesis
 Abstract: Flaviviral infections produce a distinct array of virus-induced intracellular membrane alterations that are associated with the flaviviral replication machinery. Currently, it is still unknown which flaviviral protein(s) is/are responsible for this induction. Using yeast two-hybrid and co-immunoprecipitation analyses, we demonstrated that the NS3 protein of dengue virus type 2 interacted specifically with nuclear receptor binding protein (NRBP), a host cellular protein that influences trafficking between the endoplasmic reticulum (ER) and Golgi, and that interacts with Rac3, a member of the Rho-GTPase family. Co-expression of NS3 and NRBP in baby hamster kidney cells exhibited significant subcellular co-localization, and revealed the redistribution of NRBP from the cytoplasm to the perinuclear region. Furthermore, a set of membrane structures affiliated with the rough ER at the perinuclear region was induced in cells transfected with NS3. These structures are reminiscent of the virus-induced convoluted membranes previously observed in flavivirus-infected cells. This interaction between dengue viral and host cell proteins as well as the formation of the NS3-induced membrane structures suggest that NS3 may subvert the role of NRBP in ER-Golgi trafficking.

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Language(s): eng - English
 Dates: 2004-06-15
 Publication Status: Published in print
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 Rev. Method: Peer
 Identifiers: DOI: 10.1016/j.virusres.2004.01.025
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Title: Virus Research
Source Genre: Journal
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Pages: - Volume / Issue: 102 (2) Sequence Number: - Start / End Page: 151 - 163 Identifier: -