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|Title:||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||Authors:||Chua, J.J.E.
Dengue virus type 2
Non-structural 3 protein
Nuclear receptor binding protein
|Issue Date:||2004||Citation:||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. ScholarBank@NUS Repository. https://doi.org/10.1016/j.virusres.2004.01.025||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. © 2004 Elsevier B.V. All rights reserved.||Source Title:||Virus Research||URI:||http://scholarbank.nus.edu.sg/handle/10635/31188||ISSN:||01681702||DOI:||10.1016/j.virusres.2004.01.025|
|Appears in Collections:||Staff Publications|
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