ArticlePLoS pathogens2014
GAPDH--a recruits a plant virus movement protein to cortical virus replication complexes to facilitate viral cell-to-cell movement.
Article in PLoS pathogens, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 33 papers.
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33 citing papers in PubMed, 66 citations in OpenAlex.
- Deciphering cassava brown streak virus infection in cassava through VPg mediated host protein interactions.Archives of virology · 2026Article
- Genome-wide identification of GAPDH gene family and functional analysis of CaGAPC2-mediated autophagy during BWYV infection in pepper.BMC genomics · 2026Article
- NbHDR, A Host Protein Involved in the MEP Pathway, Interacts With Bamboo Mosaic Virus Replicase and Enhances Viral Accumulation.Molecular plant pathology · 2025Article
- Beyond glycolysis: multifunctional roles of glyceraldehyde-3-phosphate dehydrogenases in plants.Horticulture research · 2025Article
- Live-cell imaging of a plant virus replicase during infection using a genetically encoded, antibody-based probe.Plant physiology · 2025Article
- Identification and expression profiling ofFrontiers in plant science · 2024Article
- Fine Structure of Plasmodesmata-Associated Membrane Bodies Formed by Viral Movement Protein.Plants (Basel, Switzerland) · 2023Article
- Comparative RNA-seq analysis of resistant and susceptible banana genotypes reveals molecular mechanisms in response to banana bunchy top virus (BBTV) infection.Scientific reports · 2023Article
- Review
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- The Crucial Role of Chloroplast-Related Proteins in Viral Genome Replication and Host Defense against Positive-Sense Single-Stranded RNA Viruses.The plant pathology journal · 2023Review
- Identification and Functional Analyses of Host Proteins Interacting with the P3a Protein of Brassica Yellows Virus.Biology · 2023Article
- Palmitoylation of γb protein directs a dynamic switch between Barley stripe mosaic virus replication and movement.The EMBO journal · 2022Article
- NSvc4 Encoded by Rice Stripe Virus Targets Host Chloroplasts to Suppress Chloroplast-Mediated Defense.Viruses · 2021Article
- Genome-Wide Identification of GDSL-Type Esterase/Lipase Gene Family inInternational journal of molecular sciences · 2021Article
- The chloroplast ribosomal protein large subunit 1 interacts with viral polymerase and promotes virus infection.Plant physiology · 2021Article
- Nuclear moonlighting of cytosolic glyceraldehyde-3-phosphate dehydrogenase regulates Arabidopsis response to heat stress.Nature communications · 2020Article
- The Barley stripe mosaic virus γb protein promotes viral cell-to-cell movement by enhancing ATPase-mediated assembly of ribonucleoprotein movement complexes.PLoS pathogens · 2020Article
- Deciphering the Binding of Salicylic Acid toInternational journal of molecular sciences · 2020Article
- First evidence showing that Pepper vein yellows virus P4 protein is a movement protein.BMC microbiology · 2020Article
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Authors and funding
8 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The formation of virus movement protein (MP)-containing punctate structures on the cortical endoplasmic reticulum is required for efficient intercellular movement of Red clover necrotic mosaic virus (RCNMV), a bipartite positive-strand RNA plant virus. We found that these cortical punctate structures constitute a viral replication complex (VRC) in addition to the previously reported aggregate structures that formed adjacent to the nucleus. We identified host proteins that interacted with RCNMV MP in virus-infected Nicotiana benthamiana leaves using a tandem affinity purification method followed by mass spectrometry. One of these host proteins was glyceraldehyde 3-phosphate dehydrogenase-A (NbGAPDH-A), which is a component of the Calvin-Benson cycle in chloroplasts. Virus-induced gene silencing of NbGAPDH-A reduced RCNMV multiplication in the inoculated leaves, but not in the single cells, thereby suggesting that GAPDH-A plays a positive role in cell-to-cell movement of RCNMV. The fusion protein of NbGAPDH-A and green fluorescent protein localized exclusively to the chloroplasts. In the presence of RCNMV RNA1, however, the protein localized to the cortical VRC as well as the chloroplasts. Bimolecular fluorescence complementation assay and GST pulldown assay confirmed in vivo and in vitro interactions, respectively, between the MP and NbGAPDH-A. Furthermore, gene silencing of NbGAPDH-A inhibited MP localization to the cortical VRC. We discuss the possible roles of NbGAPDH-A in the RCNMV movement process.
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