Journal
MOLECULAR PLANT PATHOLOGY
Volume 19, Issue 6, Pages 1504-1510Publisher
WILEY
DOI: 10.1111/mpp.12640
Keywords
host adaptation; host factor; P1 proteases; poly-protein processing; Potyviridae; RNA silencing suppression
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Funding
- China Scholarship Council
- Spanish Government [BIO2013-49053-R, BIO2016-80572-R, Plant KBBE PCIN-2013-056]
- FEDER program
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The Potyviridae family is a major group of plant viruses that includes c. 200 species, most of which have narrow host ranges. The potyvirid P1 leader proteinase self-cleaves from the remainder of the viral polyprotein and shows large sequence variability linked to host adaptation. P1 proteins can be classified as Type A or Type B on the basis, amongst other things, of their dependence 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 showed that the N-terminal domain is relevant for host factor interaction and suggested that the C-terminal domain is also involved. In the 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, strongly increasing local infection in a non-permissive host. Altogether, our results shed new insights into the adaptation and evolution of potyvirids.
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