The Dynamic Life of Virus Capsids.

Viruses
Michael B ShermanThomas J Smith

Abstract

Protein-shelled viruses have been thought as "tin cans" that merely carry the genomic cargo from cell to cell. However, through the years, it has become clear that viruses such as rhinoviruses and caliciviruses are active and dynamic structures waiting for the right environmental cues to deliver their genomic payload to the host cell. In the case of human rhinoviruses, the capsid has empty cavities that decrease the energy required to cause conformational changes, resulting in the capsids "breathing", waiting for the moment when the receptor binds for it to release its genome. Most strikingly, the buried N-termini of VP1 and VP4 are transiently exposed during this process. A more recent example of a "living" protein capsid is mouse norovirus (MNV). This family of viruses have a large protruding (P) domain that is loosely attached to the shell via a single-polypeptide tether. Small molecules found in the gut, such as bile salts, cause the P domains to rotate and collapse onto the shell surface. Concomitantly, bile alters the conformation of the P domain itself from one that binds antibodies to one that recognizes receptors. In this way, MNV appears to use capsid flexibility to present one face to the immune system and a complete...Continue Reading

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Citations

Jan 27, 2021·Viruses·Stephanie L GummersheimerPranav Danthi
Apr 22, 2021·Proceedings of the National Academy of Sciences of the United States of America·Lauriane LecoqAnja Böckmann
Jun 3, 2021·Viruses·Victoria R TengeMary K Estes

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Methods Mentioned

BETA
gel filtration
ELISA
isothermal titration calorimetry

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