Beyond structures of highly symmetric purified viral capsids by cryo-EM (original) (raw)
Current Opinion in Structural Biology
Cryogenic transmission electron microscopy (cryo-EM) is widely used to determine high-resolution structures of symmetric virus capsids. The method holds promise for extending studies beyond purified capsids and their symmetric protein shells. The non-symmetric genome component has been addressed in dsRNA cypoviruses and ssRNA bacteriophages Qβ and MS2. The structure of human herpes simplex virus type 1 capsids has been determined within intact virions to resolve capsid-tegument interactions. Electron tomography under cryogenic conditions (cryo-ET), has allowed resolving an early membrane fusion intermediate of Rift Valley fever virus. Antibody-affinity based sample grids allow capturing of virions directly from cell cultures or even clinical samples. These and other emerging methods will support studies to address viral entry, assembly and neutralization processes at increasingly high resolutions and native conditions. Highlights • Single-particle averaging has evolved to determine high resolution structures of large icosahedral viruses and viral genomes. • Sub-tomogram averaging continues to produce high resolution structures of viral surface proteins and nucleocapsids. • Tomography of viruses has provided insights into dynamic viral entry processes. Annotated References * [14] This paper on Kaposi's sarcoma-associated herpesvirus reports many technological advances that were required to reconstruct the capsid of this large virus to 4.2-Å resolution. This structure allowed identifying structural motifs that stabilize the capsid and that that could be targeted by antivirals.
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