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TitleCryo-EM Reveals Architectural Diversity in Active Rotavirus Particles.
Journal, issue, pagesComput Struct Biotechnol J, Vol. 17, Page 1178-1183, Year 2019
Publish dateJul 31, 2019
AuthorsMary Hauser / William J Dearnaley / A Cameron Varano / Michael Casasanta / Sarah M McDonald / Deborah F Kelly /
PubMed AbstractRotavirus is a well-studied RNA virus that causes severe gastroenteritis in children. During viral entry, the outer layer of the virion is shed, creating a double-layered particle (DLP) that is ...Rotavirus is a well-studied RNA virus that causes severe gastroenteritis in children. During viral entry, the outer layer of the virion is shed, creating a double-layered particle (DLP) that is competent to perform viral transcription (i.e., mRNA synthesis) and launch infection. While inactive forms of rotavirus DLPs have been structurally characterized in detail, information about the transcriptionally-active DLP remains limited. Here, we used cryo-Electron Microscopy (cryo-EM) and 3D image reconstructions to compare the structures of internal protein components in transcriptionally-active versus inactive DLPs. Our findings showed that transcriptionally-active DLPs gained internal order as mRNA synthesis unfolded, while inactive DLPs remained dynamically disordered. Regions of viral protein/RNA constituents were analyzed across two different axes of symmetry to provide a more comprehensive view of moving components. Taken together, our results bring forth a new view of active DLPs, which may enable future pharmacological strategies aimed at obliterating rotavirus transcription as a therapeutic approach.
External linksComput Struct Biotechnol J / PubMed:31467657 / PubMed Central
MethodsEM (single particle)
Resolution10.0 - 12.0 Å
Structure data

EMDB-20592:
Rotavirus, transcriptionally inactive
Method: EM (single particle) / Resolution: 10.0 Å

EMDB-20593:
Rotavirus, transcriptionally active
Method: EM (single particle) / Resolution: 12.0 Å

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