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Konig, A.

Publications and source records attributed to Konig, A..

3 recordsLinked to original sources

Model substrate particles uncover dynamics of microbial communities associated with particulate organic matter decomposition in soil

Soil organic matter is the largest terrestrial reservoir of organic carbon. Its particulate fraction, particulate organic matter (POM), serves as a resource and surface for microbial colonization. Degradation of complex biopolymers like cellulose and chitin requires extracellular enzymes produced by phylogenetically diverse microbes. Despite their importance for carbon cycling, the structure and spatio-temporal dynamics of POM-associated microbial communities in soil and how specific substrates influence them remain poorly understood. This study investigated whether microbial communities associated with POM change in composition and richness over time and whether chitin and cellulose select for distinct fungal and bacterial taxa. We incubated self-manufactured, millimetre-sized model substrate particles containing chitin or cellulose in soil under laboratory and field conditions. We assessed particle-associated communities at multiple time points over a 50-day-long incubation in the lab and after 47 days in the field. Our results show that community structure and temporal dynamics of particle-associated microbial communities were substrate-specific. While microbial biomass increased on both particle types, chitin-associated microbial communities exhibited stronger temporal changes. Communities on chitin and cellulose particles were enriched in specific bacterial and fungal genera compared to communities in the surrounding soil. We demonstrate that microbial communities associated with model chitin particles underwent notable temporal changes, including decreased microbial richness and shifts in community composition over the incubation period. This study shows the potential of model particles to advance our understanding of particle- and substrate-associated microbial communities in soil.

microbiology↗

Glycation of alpha-synuclein enhances aggregation and neuroinflammatory responses

The risk of developing Parkinsons disease (PD) is elevated in people with type 2 diabetes, but the precise molecular pathways underlying this connection are still unclear. One hypothesis is that glycation, a non-enzymatic family of reactions between glycating agents, such as reducing sugars or reactive dicarbonyls, and specific amino acids, such as lysines and arginines, may alter proteostasis and trigger pathological alterations. Glycation of alpha-synuclein (aSyn), a central player in PD pathology, causes profound changes in the aggregation process of aSyn. Methylglyoxal (MGO), a strong glycating agent, induces the formation of pathological inclusions enriched in phosphorylated aSyn on serine 129 (pS129). In addition, we found that neuroinflammatory responses are enhanced by MGO-mediated aSyn glycation. Using novel polyclonal antibodies developed towards specific MGO-glycated aSyn residues, we confirmed the occurrence of glycated aSyn both in vitro as well as in animal and in human brain tissue. In total, our findings shed light into the interplay between glycation, PD, and type 2 diabetes, potentially paving the way for the development of novel therapeutic strategies targeting these intertwined conditions.

neuroscience↗

Alpha-synuclein oligomers activate nuclear factor of activated T-cells (NFAT) modulating apoptosis and synaptic homeostasis

Soluble oligomeric forms of alpha-synuclein (aSyn-O) are believed to be one of the main toxic species in Parkinsons disease (PD) leading to degeneration. aSyn-O can induce Ca2+ influx, over activating downstream pathways leading to PD phenotype. Calcineurin (CN), a phosphatase regulated by Ca2+ levels, activates NFAT transcription factors that are involved in the regulation of neuronal plasticity, growth and survival. Here, we investigate NFATs role in neuronal degeneration induced by aSyn-O. aSyn-O are toxic to neurons leading to cell death, loss of neuron ramification and reduction of synaptic proteins which are reversed by CN inhibition with ciclosporin-A or VIVIT, a NFAT specific inhibitor. aSyn-O induce NFAT nuclear translocation and transactivation. We found that aSyn-O modulates the gene involved in the maintenance of synapses, synapsin 1 (Syn 1). Syn1 mRNA and protein and synaptic puncta are drastically reduced in cells treated with aSyn-O which are reversed by NFAT inhibition. For the first time a direct role of NFAT in aSyn-O-induced toxicity and Syn1 gene regulation was demonstrated, enlarging our understanding of the pathways underpinnings synucleinopathies.

neuroscience↗