Please use this identifier to cite or link to this item:
Title: Understanding Dengue Virus Capsid Protein Interaction with Key Biological Targets
Authors: Faustino, André F.
Martins, Ivo C.
Carvalho, Filomena A.
Castanho, Miguel A. R. B.
Maurer-Stroh, Sebastian
Santos, Nuno C.
Keywords: Computational biology and bioinformatics
Viral infection
Issue Date: 2015
Source: Faustino, A. F., Martins, I. C., Carvalho, F. A., Castanho, M. A. R. B., Maurer-Stroh, S., & Santos, N. C. (2015). Understanding Dengue Virus Capsid Protein Interaction with Key Biological Targets. Scientific Reports, 5, 10592-.
Series/Report no.: Scientific Reports
Abstract: Dengue virus (DENV) causes over 500,000 hospitalizations and 20,000 deaths worldwide every year. Dengue epidemics now reach temperate regions due to globalization of trade and travel and climate changes. Currently, there are no successful therapeutic or preventive approaches. We previously developed a peptide drug lead, pep14-23, that inhibits the biologically relevant interaction of DENV capsid (C) protein with lipid droplets (LDs). Surprisingly, pep14-23 also inhibits DENV C interaction with very low-density lipoproteins (VLDL). We thus investigated the similarity between the proposed DENV C molecular targets in LDs and VLDL, respectively, the proteins perilipin 3 (PLIN3) and apolipoprotein E (APOE). APOE N-terminal and PLIN3 C-terminal regions are remarkably similar, namely APOE α-helix 4 (APOEα4) and PLIN3 α-helix 5 (PLIN3α5) sequences, which are also highly superimposable structurally. Interestingly, APOE α-helical N-terminal sequence and structure superimposes with DENV C α-helices α1 and α2. Moreover, the DENV C hydrophobic cleft can accommodate the structurally analogous APOEα4 and PLIN3α5 helical regions. Mirroring DENV C-LDs interaction (previously shown experimentally to require PLIN3), we experimentally demonstrated that DENV C-VLDL interaction requires APOE. Thus, the results fit well with previous data and suggest future drug development strategies targeting the above mentioned α-helical structures.
ISSN: 2045-2322
DOI: 10.1038/srep10592
Schools: School of Biological Sciences 
Rights: This work is licensed under a Creative Commons Attribution 4.0 International License. The images or other third party material in this article are included in the article’s Creative Commons license, unless indicated otherwise in the credit line; if the material is not included under the Creative Commons license, users will need to obtain permission from the license holder to reproduce the material. To view a copy of this license, visit
Fulltext Permission: open
Fulltext Availability: With Fulltext
Appears in Collections:SBS Journal Articles

Files in This Item:
File Description SizeFormat 
Understanding Dengue Virus Capsid Protein Interaction with Key Biological Targets.pdf2.07 MBAdobe PDFThumbnail

Citations 20

Updated on Jun 16, 2024

Web of ScienceTM
Citations 20

Updated on Oct 28, 2023

Page view(s)

Updated on Jun 20, 2024

Download(s) 50

Updated on Jun 20, 2024

Google ScholarTM




Items in DR-NTU are protected by copyright, with all rights reserved, unless otherwise indicated.