Multiple functions of a proteinase in closterovirus life cycle Public Deposited

http://ir.library.oregonstate.edu/concern/graduate_thesis_or_dissertations/37720g705

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  • More than half of the recognized genera of positive strand RNA viruses employ polyprotein processing as one of the strategies for their genome expression. Normally, this processing is mediated by virus-encoded proteinases that belong to the trypsin-like or papain-like family. In particular, papain-like, leader proteinases were found in diverse families of human, animal, plant, and fungal positive strand RNA viruses. In addition to autocatalytic processing, these proteinases play a variety of roles in the virus life cycle. In plant potyviruses, a papain-like helper component-proteinase (HC-Pro) was implicated in genome amplification, cell-to-cell movement, long distance transport, and suppression of host defense. The p29 proteinase encoded by a fungal hypovirus CHV1 was found to be dispensable for virus replication, but it was identified as a major determinant of viral pathogenicity. In an animal equine aterivirus (EAV), a papain-like proteinase nspl was demonstrated to possess a putative zinc finger domain, which functions in subgenomic RNA synthesis, although it is not essential for virus replication. The Lab proteinase of the foot and mouse disease virus (FMDV) is involved in inhibition of cellular mRNA translation and in virus spread in infected animals. In general, it appears that functional plasticity of the papain-like leader proteinases played an important role in the evolution of viral diversity. Here, we examined the functions of a papain-like leader proteinase (L-Pro) in the life cycle of the beet yellows closterovirus (BYV). It was found that L-Pro is required for autoproteolytic processing, genome amplification, virus invasiveness and cell-to-cell movement for BYV. The gene swapping experiments involving several closterviruses, a potyvirus, as well as CHV1, FMDV, and EAV revealed complex functional profiles of the papain-like leader proteinases. The possible mechanisms that underlie L-Pro functions are discussed.
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