viruses Review Expanding Repertoire of Plant Positive-Strand RNA Virus Proteases Krin S. Mann † and Hélène Sanfaçon ,* Summerland Research and Development Centre, Agriculture and Agri-Food Canada, Summerland, BC V0H 1Z0, Canada;
[email protected] * Correspondence:
[email protected]; Tel.: +1-250-494-6393 † Current Address: University of British Columbia Okanagan, Kelowna, BC V1V 1V7, Canada. Received: 21 December 2018; Accepted: 12 January 2019; Published: 15 January 2019 Abstract: Many plant viruses express their proteins through a polyprotein strategy, requiring the acquisition of protease domains to regulate the release of functional mature proteins and/or intermediate polyproteins. Positive-strand RNA viruses constitute the vast majority of plant viruses and they are diverse in their genomic organization and protein expression strategies. Until recently, proteases encoded by positive-strand RNA viruses were described as belonging to two categories: (1) chymotrypsin-like cysteine and serine proteases and (2) papain-like cysteine protease. However, the functional characterization of plant virus cysteine and serine proteases has highlighted their diversity in terms of biological activities, cleavage site specificities, regulatory mechanisms, and three-dimensional structures. The recent discovery of a plant picorna-like virus glutamic protease with possible structural similarities with fungal and bacterial glutamic proteases also revealed new unexpected sources of protease domains. We discuss the variety of plant positive-strand RNA virus protease domains. We also highlight possible evolution scenarios of these viral proteases, including evidence for the exchange of protease domains amongst unrelated viruses. Keywords: proteolytic processing; viral proteases; protease specificity; protease structure; virus evolution 1. Introduction Eukaryotic RNA viruses have a long evolution history, which is driven by their necessary adaptation to their hosts [1].