期刊
JOURNAL OF VIROLOGY
卷 87, 期 13, 页码 7585-7592出版社
AMER SOC MICROBIOLOGY
DOI: 10.1128/JVI.00757-13
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资金
- Duke-NUS block [R913-200-039-263]
- NMRC [R-913-300-021-213]
- NRF fellowship [R-913-301-015-281]
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 degrees C, where viruses change their surface from smooth to rough. Here we present the cryo-electron microscopy structures of dengue virus at 37 degrees 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.
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