Abstract
Plants are constantly challenged by diverse pathogens and respond through multilayered immune mechanisms described by the classical "zig-zag" model. Apoplast nanoparticles (ANs), extracellular vesicle (EV)-like entities, are dynamically remodeled during plant-pathogen interactions. Although EVs are known to carry immune-regulatory cargos, the specificity and coordination of ANs protein responses to distinct pathogens remain largely unresolved. Here, we show that the glycosylation profiles of ANs and their N-glycoproteins undergo distinct remodeling upon infection with Pseudomonas syringae and Botrytis cinerea, as revealed by lectin microarray and mass spectrometry analyses. We identify SPILR, an ANs protein that modulates bacterial morphology and motility by reducing polygalacturonase activity and inhibiting the bacterial flagellar P-ring protein, FlgI. Additionally, the ESM1 protein enhances Arabidopsis resistance to B. cinerea through modulation of lipase activity and lipid metabolism. Disruption of N-glycosylation sites on ANs proteins compromises their antimicrobial function and alters host resistance to both bacterial and fungal pathogens. Together, our findings uncover N-glycosylation as a critical determinant of ANs-mediated extracellular immunity, highlighting glycosylation as an integrative mechanism linking vesicle biology, pathogen specificity, and immune signaling. This work establishes a framework for glycoengineering-based strategies to enhance crop resistance and advance nano-agricultural applications.
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Claims 5
Claim · model-written summary
Glycosylation profiles of apoplast nanoparticles and their N-glycoproteins in Arabidopsis undergo distinct remodeling upon infection with Pseudomonas syringae and Botrytis cinerea.
- Taxon
- Arabidopsis
Arabidopsist0 - Treatment
- infection with Pseudomonas syringae and Botrytis cinereae1
- Interactor
- Pseudomonas syringae
Pseudomonas syringaee1pathogen - Second interactor
- Botrytis cinerea
Botrytis cinereae1pathogen - Outcome
- glycosylation profiles of ANs and their N-glycoproteinse1
- Direction
- distinct remodelinge1
Organisms pictured · Representative pictures of the matched species, not figures from the paper.
Verbatim
e1“the glycosylation profiles of ANs and their N-glycoproteins undergo distinct remodeling upon infection with Pseudomonas syringae and Botrytis cinerea”
t0“Arabidopsis”
Claim · model-written summary
The apoplast nanoparticle protein SPILR modulates bacterial morphology and motility by reducing polygalacturonase activity and inhibiting the bacterial flagellar P-ring protein FlgI.
- Taxon
- ArabidopsisArabidopsist0
- Gene
- SPILRe1
- Outcome
- bacterial morphology and motilitye1
- Qualifier
- reducing polygalacturonase activity and inhibiting the bacterial flagellar P-ring protein, FlgIe1
Organisms pictured · Representative pictures of the matched species, not figures from the paper.
Verbatim
e1“SPILR, an ANs protein that modulates bacterial morphology and motility by reducing polygalacturonase activity and inhibiting the bacterial flagellar P-ring protein, FlgI”
t0“Arabidopsis”
Claim · model-written summary
The ESM1 protein enhances Arabidopsis resistance to Botrytis cinerea through modulation of lipase activity and lipid metabolism.
- Taxon
- ArabidopsisArabidopsise1
- Interactor
- B. cinereaBotrytis cinereae1pathogen
- Gene
- ESM1e1
- Outcome
- resistance to B. cinereae1
- Qualifier
- modulation of lipase activity and lipid metabolisme1
Organisms pictured · Representative pictures of the matched species, not figures from the paper.
Verbatim
e1“the ESM1 protein enhances Arabidopsis resistance to B. cinerea through modulation of lipase activity and lipid metabolism”
Claim · model-written summary
Disruption of N-glycosylation sites on apoplast nanoparticle proteins compromises their antimicrobial function.
- Taxon
- ArabidopsisArabidopsist0
- Treatment
- Disruption of N-glycosylation sites on ANs proteinse1
- Outcome
- antimicrobial functione1
- Direction
- compromisese1
Not reportedComparator
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”
t0“Arabidopsis”
Claim · model-written summary
Disruption of N-glycosylation sites on apoplast nanoparticle proteins alters host resistance to both bacterial and fungal pathogens.
- Taxon
- ArabidopsisArabidopsist0
- Treatment
- Disruption of N-glycosylation sites on ANs proteinse1
- Outcome
- host resistance to both bacterial and fungal pathogense1
- Direction
- alterse1
Not reportedComparator
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”
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