ArticleNature communications2026
Domain gain or loss in a fungal chitinase enables specialization towards antagonism or immune suppression.
Article in Nature communications, 2026. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 4 papers.
What it found
Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.
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.
The trial behind it
Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.
Who cites it
4 citing papers in PubMed.
- Endophyte function in climate-stressed crops: integrating molecular regulation, metabolic trade-offs, and ecological constraints.Plant signaling & behavior · 2026Review
- The role of fungal chitinases in the tripartite interactions among insects, plants and entomopathogenic fungi.Pest management science · 2026Review
- Plant-associated fungi co-opt ancient antimicrobials for host manipulation.Science advances · 2026Article
- Microbial chitinases in the plant holobiont: ecological roles and structural determinants.FEMS microbiology reviews · 2026Review
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
6 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Effector proteins orchestrate interactions that determine host compatibility and microbial competition. Among these are microbial chitinases, widespread enzymes involved in nutrient acquisition, fungal cell-wall remodelling, and antagonism, yet how their functions diversify across ecological roles remains unclear. Here, we show that modular domain variation within a conserved GH18 chitinase family enables specialization between microbial antagonism and host immune suppression in the beneficial root endophyte Serendipita indica. The chitinase SiCHIT, bearing a C-terminal CBM5 domain, is induced during fungal confrontation and inhibits growth of the phytopathogen Bipolaris sorokiniana, thereby protecting host roots. Deleting CBM5 abolishes this antagonistic activity, whereas grafting CBM5 onto its paralog SiCHIT2, which lacks this domain, confers antifungal function. In contrast, SiCHIT2 is induced during root colonization and suppresses chitin-triggered immunity, promoting host compatibility. These results show how domain loss and regulatory divergence can reprogram antimicrobial enzymes into immune-suppressive effectors in beneficial plant-associated fungi.
Indexed as
Identifiers
What OpenQuestion holds
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.