Structural Changes in Dengue Virus When Exposed to a Temperature of 37°C

被引:150
作者
Fibriansah, Guntur [1 ,2 ]
Ng, Thiam-Seng [1 ,2 ]
Kostyuchenko, Victor A. [1 ,2 ]
Lee, Jaime [1 ,2 ]
Lee, Sumarlin [1 ,2 ]
Wang, Jiaqi [1 ,2 ]
Lok, Shee-Mei [1 ,2 ]
机构
[1] Duke NUS Grad Med Sch, Program Emerging Infect Dis, Singapore, Singapore
[2] Natl Univ Singapore, Ctr BioImaging Sci, Singapore 117548, Singapore
关键词
ENVELOPE GLYCOPROTEIN; DOMAIN-III; ANTIBODY; PROTEIN; NEUTRALIZATION; BINDING; VISUALIZATION; RECOGNITION; MICROSCOPY; RESOLUTION;
D O I
10.1128/JVI.00757-13
中图分类号
Q93 [微生物学];
学科分类号
071005 ; 100705 ;
摘要
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.
引用
收藏
页码:7585 / 7592
页数:8
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