ArticlePLoS pathogens2010
A family of plasmodesmal proteins with receptor-like properties for plant viral movement proteins.
Article in PLoS pathogens, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 91 papers, 1 of them a synthesis that pooled it.
What it found
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Who cites it
91 citing papers in PubMed, 1 synthesis or guideline pooled it, 198 citations in OpenAlex.
- Primary nitrate responses mediated by calcium signalling and diverse protein phosphorylation.Journal of experimental botany · 2020Pooled it
- Role of Plasmodesmata During Plant-Pathogen Interactions.The plant pathology journal · 2026Review
- Microscopic probing into plasmodesmata (PD) and PD-derived intercellular gateways (PdIGs): Beyond morphology.Protoplasma · 2026Review
- The Interaction Network of NSm and Its Role as a Movement Protein in the Tomato Zonate Spot Virus.Viruses · 2025Article
- Lettuce Big-Vein Associated Virus ORF3 Encodes a Functional 30K Movement Protein.Molecular plant pathology · 2025Article
- Loss-of-Function of Two PD-Associated Proteins Confers Resistance to Rice Stripe Virus.Molecular plant pathology · 2025Article
- An RNase H-Like gene complements resistance to Bean common mosaic necrosis virus in Phaseolus vulgaris.The plant genome · 2025Article
- Viral tropism in plants, reproductive tissues, and seeds.Archives of microbiology · 2025Review
- Studies on the Japanese soil-borne wheat mosaic virus movement protein highlight its ability to bind plant RNA.Virology journal · 2025Article
- A pectin acetyl-transferase facilitates secondary plasmodesmata formation and RNA silencing movement between plant cells.The Plant journal : for cell and molecular biology · 2025Article
- HSP90 interacts with VP37 to facilitate the cell-to-cell movement of broad bean wilt virus 2.mBio · 2025Article
- Silencing of Putative Plasmodesmata-Associated GenesPlants (Basel, Switzerland) · 2025Article
- PDLP5, a plasmodesmata permeability regulator, can traffic between plant cells.NPJ science of plants · 2025Article
- Novel resources to investigate leaf plasmodesmata formation in CThe Plant journal : for cell and molecular biology · 2024Article
- Developing an SNP dataset for efficiently evaluating soybean germplasm resources using the genome sequencing data of 3,661 soybean accessions.BMC genomics · 2024Article
- Predictive Modeling of Proteins Encoded by a Plant Virus Sheds a New Light on Their Structure and Inherent Multifunctionality.Biomolecules · 2024Article
- dsRNA-induced immunity targets plasmodesmata and is suppressed by viral movement proteins.The Plant cell · 2023Article
- Tools and targets: The dual role of plant viruses in CRISPR-Cas genome editing.The plant genome · 2023Review
- Mutations in CmVPS41 controlling resistance to cucumber mosaic virus display specific subcellular localization.Plant physiology · 2023Article
- Manipulation of the Cellular Membrane-Cytoskeleton Network for RNA Virus Replication and Movement in Plants.Viruses · 2023Review
31 more citing papers are in PubMed but not listed here.
Corrections and comments
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Authors and funding
13 authors at 6 institutions in 2 countries.
Funding
Abstract
Plasmodesmata (PD) are essential but poorly understood structures in plant cell walls that provide symplastic continuity and intercellular communication pathways between adjacent cells and thus play fundamental roles in development and pathogenesis. Viruses encode movement proteins (MPs) that modify these tightly regulated pores to facilitate their spread from cell to cell. The most striking of these modifications is observed for groups of viruses whose MPs form tubules that assemble in PDs and through which virions are transported to neighbouring cells. The nature of the molecular interactions between viral MPs and PD components and their role in viral movement has remained essentially unknown. Here, we show that the family of PD-located proteins (PDLPs) promotes the movement of viruses that use tubule-guided movement by interacting redundantly with tubule-forming MPs within PDs. Genetic disruption of this interaction leads to reduced tubule formation, delayed infection and attenuated symptoms. Our results implicate PDLPs as PD proteins with receptor-like properties involved the assembly of viral MPs into tubules to promote viral movement.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.