Elucidation of the viral disassembly switch of tobacco mosaic virus

被引:23
作者
Weis, Felix [1 ]
Beckers, Maximilian [1 ,2 ,3 ]
von Der Hocht, Iris [4 ,5 ]
Sachse, Carsten [1 ,4 ,5 ]
机构
[1] EMBL, Struct & Computat Biol Unit, Heidelberg, Germany
[2] EMBL, Fac Biosci, Heidelberg, Germany
[3] Heidelberg Univ, Heidelberg, Germany
[4] Forschungszentrum Julich, Ernst Ruska Ctr Microscopy & Spect Electrons Stru, Julich, Germany
[5] Forschungszentrum Julich, JuStruct Julich Ctr Struct Biol, Julich, Germany
关键词
Caspar carboxylates; cryo-EM; helical reconstruction; tobacco mosaic virus; virus assembly; disassembly; CALCIUM-ION BINDING; BEAM-INDUCED MOTION; CRYO-EM; ELECTRON-MICROSCOPY; PROTEIN; RESOLUTION; PARTICLE; VALIDATION; MODEL; VISUALIZATION;
D O I
10.15252/embr.201948451
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
Stable capsid structures of viruses protect viral RNA while they also require controlled disassembly for releasing the viral genome in the host cell. A detailed understanding of viral disassembly processes and the involved structural switches is still lacking. This process has been extensively studied using tobacco mosaic virus (TMV), and carboxylate interactions are assumed to play a critical part in this process. Here, we present two cryo-EM structures of the helical TMV assembly at 2.0 and 1.9 angstrom resolution in conditions of high Ca2+ concentration at low pH and in water. Based on our atomic models, we identify the conformational details of the disassembly switch mechanism: In high Ca2+/acidic pH environment, the virion is stabilized between neighboring subunits through carboxyl groups E95 and E97 in close proximity to a Ca2+ binding site that is shared between two subunits. Upon increase in pH and lower Ca2+ levels, mutual repulsion of the E95/E97 pair and Ca2+ removal destabilize the network of interactions between adjacent subunits at lower radius and release the switch for viral disassembly.
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页数:9
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