Key result
Mengovirus 14S subviral protein particles purified from infected cells and cell-free translation systems contained pure proteins and could form structures cosedimenting with mature mengovirus.
The study demonstrates the successful purification of mengovirus 14S capsid precursor particles that retain the ability to assemble into structures resembling mature virus.
Offers no clinical guidance; extends in vitro models of picornavirus assembly.
Mengovirus 14S subviral protein particles generated in infected L cells and in a cell-free translation system primed with mengovirus RNA were purified by sucrose gradient centrifugation and immunoaffinity chromatography. The preparations from both sources contained essentially pure proteins epsilon, alpha, and gamma, as was demonstrated in terms of virus-specific proteins (by autoradiography) and total protein content (by silver staining of sodium dodecyl sulfate-polyacrylamide electrophoresis gels). These purified proteins sedimented as discrete particles at the 14S position when recentrifuged in sucrose gradients. Although their assembly properties have not yet been studied in detail, preliminary results indicate that during incubation with virion RNA the 14S particles purified from infected cells can form a structure cosedimenting with mature mengovirus.
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Boege et al. (1986) studied Mengovirus infection (in vitro). Purification of mengovirus 14S capsid precursor particles was evaluated on Purification and assembly properties of 14S particles. Mengovirus 14S subviral protein particles purified from infected cells and cell-free translation systems contained pure proteins and could form structures cosedimenting with mature mengovirus.
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