3 years ago

Truncation of a P1 leader proteinase facilitates potyvirus replication in a non-permissive host

Bernardo Rodamilans, Carmen Simón-Mateo, Ioannis E. Tzanetakis, Hongying Shan, Fabio Pasin, Juan Antonio García
The Potyviridae family is a major group of plant viruses that includes ca. 200 species, most of which have narrow host ranges. The potyvirid P1 leader proteinase self-cleaves from the remainder of viral polyprotein and shows large sequence variability linked to host adaptation. P1 proteins can be classified as Type A or Type B based, among other things, on their dependency or not on a host factor to develop their protease activity. In this work, we studied Type A proteases from the Potyviridae family characterizing their host factor requirements. Our in vitro cleavage analyses of potyvirid P1 proteases show that the N-terminal domain is relevant for host factor interaction and suggest that the C-terminal domain is also involved. In absence of plant factors, the N-terminal end of Plum pox virus P1 antagonizes protease self-processing. We performed extended deletion mutagenesis analysis to define the N-terminal antagonistic domain of P1. In viral infections, removal of the P1 protease antagonistic domain led to a gain-of-function phenotype, deeply increasing local infection in a non-permissive host. Altogether, our results shed new insights into adaptation and evolution of potyvirids. This article is protected by copyright. All rights reserved.

Publisher URL: http://onlinelibrary.wiley.com/resolve/doi

DOI: 10.1111/mpp.12640

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