Evidence map›Paper›PMID 42806337›Full record

ArticleVirology journal2026

Characterization of the C4 protein encoded by parsley yellow leaf curl virus.

Hasan Zeitooni, Rosa Lozano-Durán, Masoud Shams-Bakhsh

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Article in Virology journal, 2026. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.

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1 · What the graph read from it

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4 · The record

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5 · Who and what money

Authors and funding

3 authors.

Hasan ZeitooniDepartment of Plant Pathology, Faculty of Agriculture, Tarbiat Modares University, Tehran, Iran.
Rosa Lozano-DuránDepartment of Plant Biochemistry, Center for Plant Molecular Biology (ZMBP), Eberhard Karls University, Tübingen, Germany. rosa.lozano-duran@uni-tuebingen.de.
Masoud Shams-BakhshDepartment of Plant Pathology, Faculty of Agriculture, Tarbiat Modares University, Tehran, Iran. shamsbakhsh@modares.ac.ir.

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

backgroundGeminiviruses encode small, rapidly evolving proteins that reprogram host functions to facilitate infection. Among these, C4/AC4 proteins frequently act as determinants of pathogenicity and symptom expression. Parsley yellow leaf curl virus (PYLCV; Pylecuvirus petroselini), a recently described monopartite geminivirus associated with yellowing and leaf curling in parsley, encodes a C4 protein whose biological activities and cellular distribution remain uncharacterized.

methodsHere, we combined comparative sequence analysis, confocal microscopy, site-directed mutagenesis, heterologous expression, and RNA silencing suppression assays to characterize PYLCV C4.

resultsIn silico analysis of the 85-amino-acid C4 protein identified several candidate targeting features, including a predicted N-terminal myristoylation motif, a putative palmitoylation site, nuclear trafficking-related motifs, and a chloroplast transit peptide. Confocal imaging showed that C4-GFP localizes to the plasma membrane and also accumulates in the nucleus and chloroplasts. Substitution of Gly2 within the predicted N-myristoylation motif strongly reduced plasma membrane association and increased the chloroplast-associated signal of C4-GFP, supporting an important role for the Gly2-containing N-terminal region in membrane targeting and suggesting that chloroplast-associated targeting becomes more prominent when Gly2-dependent cell-peripheral association is disrupted. Expression of PYLCV C4 from a potato virus X (PVX; Potexvirus ecspotati)-based vector in Nicotiana benthamiana induced severe developmental alterations, including mosaic, yellowing, leaf curling, stem deformation, and plant death, without affecting PVX RNA accumulation. PYLCV C4 did not behave as a strong suppressor of local or systemic post-transcriptional gene silencing (PTGS) under the conditions tested, although a possible delay in the spread of GFP silencing was observed in N. benthamiana 16c plants.

conclusionsTogether, these findings provide the first experimental characterization of PYLCV C4 and establish a framework for future mechanistic studies addressing how this protein may contribute to host developmental perturbation and PYLCV-plant interactions.

Indexed as

BegomovirusPlant DiseasesViral ProteinsAmino Acid SequenceCell MembraneChloroplastsMicroscopy, ConfocalMutagenesis, Site-DirectedNicotianaViral ProteinsBAM1Developmental alterationsN‑myristoylationPlasma membranePost-transcriptional gene silencingPYLCV

Identifiers

PMID42806337
PMCPMC13617785

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