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4 recordsLinked to original sources
PubMed2026

Characterization of yam virus X isolates from Dioscorea trifida in Brazil.

OBJECTIVE: Yam virus X (YVX; Potexvirus ecsdioscoreae) is a positive-sense, flexuous RNA virus belonging to the family Alphaflexiviridae. It has been first reported from Guadeloupe, a French archipelago located in the Caribbean Sea. In this study, we investigated the virome in yam (Dioscorea spp.) plant material collected in the state of Bahia (Brazil) by high-throughput sequencing (HTS) on Illumina platform. The objective of the investigation was to explore the occurrence of YVX in yam from South America, and to study its genetic diversity compared to the only one YVX genome sequence available in the GenBank public database. RESULTS: An initial investigation by HTS of bulked RNA extracts (n=23, combined into 4 pools) revealed occurrence of YVX only in samples collected in the region of Valença. Subsequent screening by RT-PCR of the individual samples composing the pool uncovered infection with YVX only in Discorea trifida. Total RNA extracts from three infected plants were individually sequenced, resulting in the assembly of three complete genome sequences of YVX, showing ~84% nucleotide identity to the reference sequence from Guadeloupe. Our results contribute to expanding the pool of sequences available for YVX, supporting detection purposes and stimulating additional investigations for future studies on YVX diversity and evolution.

Brazil↗
PubMed2026

A conserved COBL3-like protein promotes PDLP5-dependent callose accumulation to confer broad-spectrum plasmodesmata-mediated antiviral defense.

Plasmodesmata (PDs) play vital roles in plant growth and defense by controlling the symplastic transport of important molecules. Here we report that a conserved COBRA-like protein, COBL3, positively regulates callose accumulation and is required for PD-mediated antiviral defense (PMAD) against divergent plant RNA viruses in wheat (Triticum aestivum) and tobacco (Nicotiana benthamiana). The wheat COBL3 protein, TaCOBL3, interacts with the 17K movement protein (MP) of barley yellow dwarf virus-GAV (BYDV-GAV). TaCOBL3 is associated with the plasma membrane and co-localizes with 17K MP at PDs. Genetic analysis with overexpression and knockout lines revealed that TaCOBL3 positively regulates wheat defense against BYDV-GAV by modulating callose accumulation at PDs. Interestingly, TaCOBL3 interacts with the wheat homolog of PDLP5, a conserved key regulator of PD permeability in higher plants. Silencing TaPDLP5 attenuates the elevated BYDV-GAV defense conferred by overexpression of TaCOBL3 in wheat. Furthermore, transient expression of TaCOBL3 promotes callose accumulation and lowers PD permeability in tobacco cells, and these effects are largely compromised when tobacco PDLP5 is silenced. Notably, BYDV 17K MP weakens the interaction between TaCOBL3 and TaPDLP5 and inhibits their callose-binding activities. Finally, silencing of tobacco NbCOBL3 reduces callose content and attenuates host defense against two tobraviruses, one potexvirus, and one hordeivirus. Overall, our study reveals a previously unknown role of COBRA-like proteins in PMAD and provides insight into how a plant viral MP sabotages PMAD by perturbing the COBL3-PDLP5 interaction to facilitate virus spread through PDs. The conserved COBL3 gene may be a valuable target for engineering of broad-spectrum antiviral resistance in crop plants.

COBRA-like protein↗
PubMed2026

Multivalent Display of Antimicrobial Peptides on Plant Virus Scaffolds Enhances Killing of Drug-Resistant Bacteria.

Multidrug-resistant (MDR) bacteria pose a significant challenge to global health. Antimicrobial peptides (AMPs) have emerged as promising candidates against MDR bacteria due to their rapid and broad-spectrum activity; however, their clinical translation is hindered by compromised activity, toxicity, and poor stability under in vivo conditions. Here, we report the development of RPG (rod-based peptide grids), a plant virus-based antimicrobial platform that harnesses the structural scaffold of high-aspect-ratio Potato virus X (PVX) for the multivalent and modular display of AMPs. Our data show that RPG enhances the efficacy of AMPs by more than 9700-fold, maintaining activity under in vivo salt conditions. RPG eradicates MDR pathogens within 10-30 min, surpassing the efficacy of last-resort antibiotics (vancomycin, tigecycline, and cefiderocol), while exhibiting low measurable cytotoxicity to mammalian cells at high therapeutic doses. Due to structural complexity, RPG demonstrates stability in serum and resistance to proteases. Multivalent display of peptide variants enabled enhanced broad-spectrum killing at low doses. This work establishes plant virus-AMP conjugates as a safe, potent, broad-spectrum antimicrobial platform, offering a versatile strategy for addressing antibiotic resistance.

Antimicrobial Peptides↗
PubMed2025

Live-cell RNA imaging with the inactivated endonuclease Csy4 enables new insights into plant virus transport through plasmodesmata.

Plant-infecting viruses spread through their hosts by transporting their infectious genomes through intercellular nano-channels called plasmodesmata. This process is mediated by virus-encoded movement proteins. Whilst the sub-cellular localisations of movement proteins have been intensively studied, live-cell RNA imaging systems have so far not been able to detect viral genomes inside the plasmodesmata. Here, we describe a highly sensitive RNA live-cell reporter based on an enzymatically inactive form of the small bacterial endonuclease Csy4, which binds to its cognate stem-loop with picomolar affinity. This system allows imaging of plant viral RNA genomes inside plasmodesmata and shows that potato virus X RNA remains accessible within the channels and is therefore not fully encapsidated during movement. We also combine Csy4-based RNA-imaging with interspecies movement complementation to show that an unrelated movement protein from tobacco mosaic virus can recruit potato virus X replication complexes adjacent to plasmodesmata. Therefore, recruitment of potato virus X replicase is mediated non-specifically, likely by indirect coupling of movement proteins and viral replicase via the viral RNA or co-compartmentalisation, potentially contributing to transport specificity. Lastly, we show that a 'self-tracking' virus can express the Csy4-based reporter during the progress of infection. However, expression of the RNA-binding protein in cis interferes with viral movement by an unidentified mechanism when cognate stem-loops are present in the viral RNA.

Plasmodesmata↗