Key result
The capsid precursor protein of human astrovirus VA1 is cleaved intracellularly to yield mature infectious particles formed by VP33 and VP38, independent of trypsin and caspases.
Why the study?
Human astrovirus VA1 has been linked to neurological disease in immunocompromised individuals, and its recent cell culture propagation enabled investigation into its biology.
Does not yet inform astrovirus management; leaves open whether intracellular cleavage occurs across clinical strains.
Human astrovirus VA1 has been associated with neurological disease in immunocompromised patients. Its recent propagation in cell culture has facilitated the study of its biology. In this work, we show that despite the ability of this virus to grow in the absence of trypsin, a marked feature of human classical astroviruses, the capsid precursor protein of astrovirus VA1 is cleaved intracellularly to yield the mature infectious particles, formed by two polypeptides, VP33 that constitutes the core domain of the virus particle, and VP38 that forms the spike of the virus. These studies provide a platform to advance our knowledge on astrovirus VA1 cell entry and replication.
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Aguilera-Flores et al. (2022) studied Human astrovirus VA1 infection. In vitro astrovirus VA1 infection and proteolytic processing analysis was evaluated on Proteolytic processing of VA1 capsid precursor protein. The capsid precursor protein of human astrovirus VA1 is cleaved intracellularly to yield mature infectious particles formed by VP33 and VP38, independent of trypsin and caspases.
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