Capsid shells of viruses are key in understanding how the virus interacts with the host and delivers its genetic material. In this recent paper, the authors discover that the protein capsid for the norovirus, which causes acute enteritis and roughly 200,000 deaths each year, changes its conformation over its lifecycle and while under thermal stress. They find that the shell domain remains relatively constant while the protruding domains are highly flexible with independent P domain dimers which improves antibody invasion. A mutation at L412Q in the gene ORF2 disrupts the dimers but keeps the virus as a whole stable under thermal stress, preventing denaturation.
-Alexis Williams
Snowden JS, Hurdiss DL, Adeyemi OO, Ranson NA, Herod MR, Stonehouse NJ (2020) Dynamics in the murine norovirus capsid revealed by high-resolution cryo-EM. PLoS Biol 18(3):e3000649.
https://doi.org/10.1371/journal.pbio.3000649
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