Claim · model-written summary
NbGAPDH-A was identified as a host protein interacting with the RCNMV movement protein in infected Nicotiana benthamiana leaves.
- Taxon
- Nicotiana benthamiana
Nicotiana benthamianae0 - Organ / stage
- leavese0
- Interactor
- RCNMVRed clover necrotic mosaic viruse0pathogen
- Gene
- NbGAPDH-Ae1
- Outcome
- host proteins that interacted with RCNMV MPe0
Not reportedMaterialCompoundSecond interactorSecond interactor roleTreatmentComparatorSettingDirectionValueQualifier
Organisms pictured · Representative pictures of the matched species, not figures from the paper.
Verbatim
e0“We identified host proteins that interacted with RCNMV MP in virus-infected Nicotiana benthamiana leaves”
e1“glyceraldehyde 3-phosphate dehydrogenase-A (NbGAPDH-A)”
Title
Masanori Kaido; Kazutomo Abe; Akira Mine; et al. PLoS Pathogens 2014. doi:10.1371/journal.ppat.1004505
Other claims from this paper (8)
- Observation Cortical punctate structures containing the movement protein constitute a viral replication complex of RCNMV, in addition to aggregate structures adjacent to the nucleus.
- Intervention effect Virus-induced gene silencing of NbGAPDH-A reduced RCNMV multiplication in inoculated leaves.
- Intervention effect Silencing of NbGAPDH-A did not reduce RCNMV multiplication in single cells.
- Mechanism The authors suggest that GAPDH-A plays a positive role in cell-to-cell movement of RCNMV.
- Observation The NbGAPDH-A-GFP fusion protein localized exclusively to chloroplasts.
- Observation In the presence of RCNMV RNA1, the NbGAPDH-A fusion protein localized to the cortical VRC as well as the chloroplasts.
- Observation Bimolecular fluorescence complementation and GST pulldown assays confirmed in vivo and in vitro interactions, respectively, between the RCNMV movement protein and NbGAPDH-A.
- Intervention effect Gene silencing of NbGAPDH-A inhibited localization of the movement protein to the cortical VRC.