Biology subjects

Moerschbacher, B. M.

Publications and source records attributed to Moerschbacher, B. M..

5 recordsLinked to original sources

bioRxiv2026

Chitin oligomers induce atypical NLRP3 inflammasome activation and innate immune training

Chitin is a highly abundant poly- N-acetyl-glucosamine (GlcNAc) and linked to immune recognition of fungal infections and asthma in humans. Ubiquitous in fungi and insects, in mammals and plants chitin represents a microbe-associated molecular pattern (MAMP) and whereas highly polymeric chitin is insoluble and immunologically inert, soluble chitin oligomers of 6 to 15 GlcNAc activate immediate pro-inflammatory cytokine release via TLR2 in human immune cells. However, TLR2 ligands do not the most typical activators of the NLRP3 inflammasome pathway or innate immune training, a phenomenon of long-term immunological remodeling. Here we show that especially 16-20 GlcNAc long chitin oligomers activate NLRP3-dependent IL-1{beta} and IL-18 release in human myeloid immune cells in an atypical, phagocytosis-dependent manner. Moreover, phagocytosis and methyl transferase activity were essential for innate immune training, by which the same chito-oligomer-training enhanced TNF release in primary murine and human immune cells. Collectively, this suggests that oligomer length impacts on the immune features of chitin which can be customized using glycan assembly.

immunology↗

bioRxiv2026

Immunoengineered Chitosanase-Produced Chitosan Oligomers for Elevating Plant Resistance to Viral Infection

Chitooligomers can act as plant biostimulants or biopesticides, but todays chitosan-based agro-biologics often lack sufficient efficacy. This is due to a lack of scalable production processes for structurally well-controlled chitosans combined with a limited understanding of structure-function relationships. Chitosans differ in their degree of polymerization (DP), fraction and pattern of acetylation (FA and PA). While the influence of DP and FA on antimicrobial and phytostimulatory properties is at least partially known, this is not yet the case for PA. PA can be partially controlled by using enzymatic rather than acid hydrolysis for oligomer production. We have used recombinant chitinases and chitosanases to hydrolyse a well-characterised chitosan polymer, and purified oligomers with different DP. We have structurally characterised the products and tested their abilities to protect tobacco from viral disease. Chitinase products were dominated by GlcNAc units at their reducing and non-reducing ends, with GlcN units dominating their centers, and v.v. for chitosanase products. While the chitinase-derived hydrolysates were inactive, the chitosanase-derived oligomers possessed elicitor and priming activities and protected plants from disease, and their activity increased with increasing DP. Clearly, the Bacillus chitosanase used is well-suited to set up a scalable production process for chitosan oligomers with promising agro-biologic properties. Graphical Abstract O_FIG O_LINKSMALLFIG WIDTH=200 HEIGHT=95 SRC="FIGDIR/small/731087v1_ufig1.gif" ALT="Figure 1"> View larger version (56K): org.highwire.dtl.DTLVardef@b50b59org.highwire.dtl.DTLVardef@1fc35c3org.highwire.dtl.DTLVardef@12db91aorg.highwire.dtl.DTLVardef@d3732f_HPS_FORMAT_FIGEXP M_FIG C_FIG

plant biology↗

bioRxiv2025

Domain gain or loss in fungal chitinases drives ecological specialization toward antagonism or immune suppression

The evolutionary origins of fungal effector proteins remain poorly understood, particularly how structural changes reprogram antimicrobial enzymes into host-adapted immune suppressors. Here, we show that domain modularity drives ecological specialization in chitinase effectors of the beneficial root endophyte Serendipita indica. The GH18 chitinase SiCHIT, which carries a C-terminal carbohydrate-binding module (CBM5), is expressed during fungal competition and antagonizes the fungal pathogen Bipolaris sorokiniana in the rhizosphere, thereby protecting plant roots. Deletion of the CBM5 abolishes this antifungal activity, while fusion of CBM5 to the CBM5-lacking paralog SiCHIT2 restores pathogen inhibition. In contrast, SiCHIT2 is induced during root colonization and suppresses chitin-triggered reactive oxygen species production, promoting immune evasion and host compatibility. These results identify CBM5 as a modular determinant of effector function, switching chitinase activity between microbial antagonism and host immune suppression. Our findings support an evolutionary scenario in which effector function in planta arises through domain loss and transcriptional divergence from an antimicrobial precursor, consistent with transitions along the saprotrophy-to-symbiosis continuum. Significance StatementEffector proteins play key roles in shaping fungal interactions with both plant hosts and microbial competitors, yet how these functions evolve remains unclear. Here, we show that structural domain modularity enables ecological specialization of two paralogous chitinases arising from gene duplication in the root endophyte Serendipita indica. Through domain deletion and fusion, we demonstrate that a carbohydrate-binding module (CBM5) determines whether a chitinase functions in microbial antagonism or immune evasion. Our findings provide mechanistic evidence for effector diversification via domain loss and transcriptional divergence, supporting an evolutionary trajectory from antimicrobial activity to host adaptation. This work advances our understanding of how modular architecture drives effector evolution and niche specialization in symbiotic fungi. HighlightsO_LIGain or loss of a CBM5 binding domain drives effector specialization between fungal antagonism and immune suppression C_LIO_LICBM5 acts as a modular determinant enabling antifungal activity in the GH18 chitinase SiCHIT C_LIO_LIThe CBM5-lacking paralog SiCHIT2 suppresses host immunity and promotes root colonization C_LIO_LIFunctional divergence following gene duplication illustrates evolutionary repurposing of an antimicrobial enzyme into an immune-suppressive effector C_LI

plant biology↗

bioRxiv2019

Protein-surfactant-polysaccharide nanoparticles increase the catalytic activity of an engineered β-lactamase maltose-activated switch enzyme

We present polysaccharide-based nanoparticles able to associate and increase the catalytic activity of the maltose-binding MBP317-347 switch enzyme. Fluorescence quenching and molecular docking studies along with the partial resistance to increasing pH and ionic strength indicate that the increase in enzymatic activity is due to a specific interaction between the maltose binding pocket on MBP317-347 and alginate exposed on the surface of the nanoparticles. Finally, we show that the hybrid self co-assembled particles increase the half-life of MBP317-347 over six-fold at 37{degrees}C, thus reflecting their potential use as a macromolecular drug delivery system.

biochemistry↗

bioRxiv2017

Chitosan perception in Arabidopsis requires the chitin receptor AtCERK1 suggesting an improved model for receptor structure and function

Chitin, a linear polymer of N-acetyl-D-glucosamine, and chitosans, fully or partially deacetylated derivatives of chitin, are known to elicit defense reactions in higher plants. We compared the ability of chitin and chitosan oligomers and polymers (chitin oligomers with degree of polymerization 3 to 8; chitosan oligomers with degree of acetylation 0% to 35% and degree of polymerization 3 to 15; chitosan polymers with degree of acetylation 1% to 60% and degree of polymerization ~1300) to elicit an oxidative burst indicative of induced defense reactions in A. thaliana seedlings. Fully deacetylated chitosans were not able to trigger a response; elicitor activity increased with increasing degree of acetylation of chitosan polymers. Partially acetylated chitosan oligomers required a minimum degree of polymerization of 6 and at least four N-acetyl groups to trigger a response. Invariably, elicitation of an oxidative burst required the presence of the chitin receptor AtCERK1. Our results as well as previously published studies on chitin and chitosan perception in plants are best explained by a new general model of LysM-containing receptor complexes where two partners form a long, but off-set chitin-binding groove and are, thus, dimerized by one chitin or chitosan molecule, sharing a central GlcNAc unit with which both LysM domains interact. To verify this model and to distinguish it from earlier models, we assayed elicitor and inhibitor activities of selected partially acetylated chitosan oligomers with fully defined structures. In contrast to the initial \"continuous groove\", the original \"sandwich\", or the current \"sliding mode\" models for the chitin/chitosan receptor, the here proposed \"slipped sandwich\" model - which builds on these earlier models and represents a consensus combination of these - is in agreement with all experimental observations.

biochemistry↗