February 6, 2021Open Access

The cryo-EM structure of vesivirus 2117 highlights functional variations in entry pathways for viruses in different clades of the Vesivirus genus

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Population

Capsid of Vesivirus 2117

Design

Cryogenic electron microscopy structural study

Authors

HSHazel SutherlandUniversity of Liverpool MCMichaela J. ConleyMRC University of Glasgow Centre for Virus Research EEEdward EmmottUniversity of Liverpool

Discussion

Member takes

Implication

Cryo-EM structure of Vesivirus 2117 informs bioprocess monitoring; leaves open questions on cross-species transmission and antigen design.

Structured PICO

Population

Vesivirus 2117 virus-like particles (VLPs) produced by heterologous baculovirus expression of the VP1 gene in insect cells (Hi5 cells)

Intervention

Cryogenic electron microscopy (cryo-EM) and three-dimensional image reconstruction

Outcome

Capsid structure of vesivirus 2117

The cryo-EM structure of vesivirus 2117 reveals structural differences in the major capsid protein compared to feline calicivirus, suggesting distinct mechanisms for receptor engagement and viral entry among Vesivirus clades.

Cite This Study

Sutherland et al. (2021) studied this question.

synapsesocial.com/papers/6a7098155d37378ac1ddb698 https://doi.org/10.1101/2021.02.05.429895

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Implication

Cryo-EM structure of Vesivirus 2117 informs bioprocess monitoring; leaves open questions on cross-species transmission and antigen design.

The cryo-EM structure of vesivirus 2117 highlights functional variations in entry pathways for viruses in different clades of the Vesivirus genus

Discussion

Member takes

Implication

Structured PICO

Cite This Study

The cryo-EM structure of vesivirus 2117 highlights functional variations in entry pathways for viruses in different clades of the Vesivirus genus

Discussion

Member takes

Implication

Structured PICO

Cite This Study

Also Consider

Also Consider