Claim · model-written summary
Disruption of N-glycosylation sites on apoplast nanoparticle proteins alters host resistance to both bacterial and fungal pathogens.
- Taxon
- Arabidopsis
Arabidopsist0 - Treatment
- Disruption of N-glycosylation sites on ANs proteinse1
- Outcome
- host resistance to both bacterial and fungal pathogense1
- Direction
- alterse1
Not reportedMaterialGeneCompoundOrgan / stageInteractorInteractor roleSecond interactorSecond interactor roleComparatorSettingValueQualifier
Organisms pictured · Representative pictures of the matched species, not figures from the paper.
Verbatim
e1“Disruption of N-glycosylation sites on ANs proteins compromises their antimicrobial function and alters host resistance to both bacterial and fungal pathogens”
t0“Arabidopsis”
Title
Guanting Niu; Hao Lu; Tunyu Jian; et al. Journal of Integrative Plant Biology 2026. doi:10.1111/jipb.70142
Other claims from this paper (4)
- Observation Glycosylation profiles of apoplast nanoparticles and their N-glycoproteins in Arabidopsis undergo distinct remodeling upon infection with Pseudomonas syringae and Botrytis cinerea.
- Mechanism The apoplast nanoparticle protein SPILR modulates bacterial morphology and motility by reducing polygalacturonase activity and inhibiting the bacterial flagellar P-ring protein FlgI.
- Mechanism The ESM1 protein enhances Arabidopsis resistance to Botrytis cinerea through modulation of lipase activity and lipid metabolism.
- Intervention effect Disruption of N-glycosylation sites on apoplast nanoparticle proteins compromises their antimicrobial function.