Calicivirus assembly and stability are mediated by the N-terminal domain of the capsid protein with the involvement of the viral genome.

ABSTRACT: Caliciviruses are important human and animal pathogens that cause varying clinical signs including gastroenteritis, respiratory illness, and hepatitis. Despite the availability of numerous calicivirus structures, relatively little is known about the mechanisms of capsid assembly and stability, or about genome packaging. Here we present the atomic structure of the RHDV virion and several related non-infectious virus-like particles, determined using cryo-EM at 2.5-3.3 Å resolution. The inherent molecular switch, responsible for the conformational flexibility of the capsid protein VP1, is located in its N-terminal arm (NTA). The NTA establishes an extensive network of interactions on the inner capsid surface that stabilizes the hexamers and pentamers. For this structural polymorphism, we show

SUBMITTER: Novoa G 

PROVIDER: S-EPMC12707631 | biostudies-literature | 2025 Dec

REPOSITORIES: biostudies-literature