title: Switching on RNA silencing suppressor activity by restoring argonaute binding to a viral protein.
abstract: We found that Sweet potato feathery mottle virus (SPFMV) P1, a close homologue of Sweet potato mild mottle virus P1, did not have any silencing suppressor activity. Remodeling the Argonaute (AGO) binding domain of SPFMV P1 by the introduction of two additional WG/GW motifs converted it to a silencing suppressor with AGO binding capacity. To our knowledge, this is the first instance of the transformation of a viral protein of unknown function to a functional silencing suppressor.
authors.affiliation: Department of Dermatology and Allergology, University of Szeged, Szeged, Hungary.
authors.forename: Edit Z
authors.initials: EZ
authors.lastname: Szabó
authors.forename: Máté
authors.initials: M
authors.lastname: Manczinger
authors.forename: Anikó
authors.initials: A
authors.lastname: Göblös
authors.forename: Lajos
authors.initials: L
authors.lastname: Kemény
authors.forename: Lóránt
authors.initials: L
authors.lastname: Lakatos
mesh_terms: D060565:Argonaute Proteins / Q000235:genetics / Q000378:metabolism*; D020868:Gene Silencing; D027723:Ipomoea batatas / Q000235:genetics / Q000378:metabolism / Q000821:virology*; D010940:Plant Proteins / Q000235:genetics / Q000378:metabolism*; D010942:Plant Viruses / Q000235:genetics / Q000378:metabolism*; D011485:Protein Binding; D017434:Protein Structure, Tertiary; D014764:Viral Proteins / Q000235:genetics / Q000378:metabolism*
chemical_list: D060565:Argonaute Proteins; C113489:P1 protein, Sweet potato feathery mottle virus; D010940:Plant Proteins; D014764:Viral Proteins