New Insights into Rotavirus Entry Machinery: Stabilization of Rotavirus Spike Conformation Is Independent of Trypsin Cleavage

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Rotavirus is responsible for more than 400,000 annual infant deaths worldwide. Its viral particle bears 60 protuberant spikes that constitute the machinery responsible for virus binding to and entry into the host cell. For efficient infection, the protein molecules that build the spike must be cleaved. Despite the importance of this activation step, the nature of the changes induced in the spike structure is unknown. According to the current hypothesis, the uncleaved spike is very flexible, and activation stabilizes the spike in an entry-competent conformation. Here we used distinct electron microscopy techniques to determine the structure of the uncleaved particle in two model rotavirus strains. Our results provide a complete structure of the uncleaved spike and demonstrate that cleaved and uncleaved spikes have similar conformations, indicating that proteolytic processing is not involved in stabilization of the spike. We suggest that spike processing is important for infection since it is necessary to allow the spike domain movements involved in rotavirus entry.

Vyšlo v časopise: New Insights into Rotavirus Entry Machinery: Stabilization of Rotavirus Spike Conformation Is Independent of Trypsin Cleavage. PLoS Pathog 10(5): e32767. doi:10.1371/journal.ppat.1004157
Kategorie: Research Article
prolekare.web.journal.doi_sk: https://doi.org/10.1371/journal.ppat.1004157

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