by Guntur Fibriansah, Thiam-Seng Ng, Victor A. Kostyuchenko, Jaime Lee, Sumarlin Lee, Jiaqi Wang, Shee-Mei Lok
J Virol. 2013 Jul;87(13):7585-92. doi: 10.1128/JVI.00757-13. Epub 2013 May 1.
Previous binding studies of antibodies that recognized a partially or fully hidden epitope suggest that insect cell-derived dengue virus undergoes structural changes at an elevated temperature.
This was confirmed by our cryo-electron microscopy images of dengue virus incubated at 37°C, where viruses change their surface from smooth to rough. Here we present the cryo-electron microscopy structures of dengue virus at 37°C. Image analysis showed four classes of particles. The three-dimensional (3D) map of one of these classes, representing half of the imaged virus population, shows that the E protein shell has expanded and there is a hole at the 3-fold vertices. Fitting E protein structures into the map suggests that all of the interdimeric and some intradimeric E protein interactions are weakened. The accessibility of some previously found cryptic epitopes on this class of particles is discussed.
Read online: Pubmed.
Learn more about Shee-Mei Lok’s research.