bioRxiv Science⌕ Search

Biology subjects

El Karkouri, K.

Publications and source records attributed to El Karkouri, K..

2 recordsLinked to original sources

Evidence for a central ecological function of predatory Myxococcota in soil ecosystems

Myxococcota is a recently classified phylum including bacteria renowned for their predatory lifestyle. However, ecological functions of these bacteria remain under studied. Here, we examined the ecological position and potential impact of Myxococcota communities across diverse soil habitats using the global geographical collection of 16S microbial communities structured by the Earth Microbiome Project (EMP). First, we found that the abundance of Myxococcota varied greatly from 6.3% to 0.8% across 13 soil habitats. A deeper microbial analysis in two selected habitats showed that Myxococcota was highly abundant (4.9%) ranking 5 in field soil (a grassland planted with switchgrass) than in sand biofilter (an engineered system for water quality production, 1.3% and 11, resp.). Moreover, both Myxococcota and microbial communities displayed a significantly higher -diversity in field soil than in sand biofilter environments, suggesting that diversity of Myxococcota seems to be associated with that of microbial communities in these habitats. Using co-occurrence network analysis, we found that Myxococcota exhibited a high eigenvector centrality (5.1%) and one hub taxon, Polyangiales, in field soil habitat. In contrast, Myxococcota centrality was less pronounced (1.1%) in the sand biofilter, where consistent negative correlations were also detected. Altogether, these results suggest that Myxococcota communities experienced beneficial interactions in field soil environment, whereas they may have faced competitive relationships in sand biofilter habitat. Overall, our findings provide further insights into the status of Myxococcota communities in soil environments, suggesting their fundamental roles in the structure of soil microbial communities.

ecology↗

Periplasmic detoxification of urate hydroperoxide underpins E. coli survival in the inflamed gut

Uric acid, the final product of purine metabolism in humans, accumulates in blood and tissues at relatively high concentrations1 as humans lack the enzyme uricase2,3. Under inflammatory conditions, uric acid can be oxidised to yield reactive intermediates4. In activated neutrophils, myeloperoxidase (MPO) catalyses the oxidation of uric acid by hydrogen peroxide, leading to the formation of urate hydroperoxide (UH)5,6. While recent studies have shown that UH is toxic to bacteria lacking peroxiredoxins7, its precise mechanism of toxicity and the existence of dedicated bacterial defence systems remain unknown. Here, we identify HiuH as a periplasmic enzyme, conserved across E. coli strains, that specifically degrades UH. Our findings reveal that UH selectively induces the expression of hiuH and that HiuH efficiently detoxifies UH both in vitro and in bacterial cells. HiuH cooperates with MsrP, a periplasmic methionine sulfoxide reductase that repairs UH-induced protein-bound methionine oxidation. This combined defence offering both direct detoxification and damage repair, is essential for bacterial survival under UH stress, and confers a competitive fitness advantage in a DSS-induced mouse model of colitis. Although UH is chemically transient, our work shows that it imposes durable biological consequences and a sufficient fitness cost in the in vivo niches occupied by E. coli to favour the evolution of a dedicated detoxification pathway beyond general oxidative-stress responses, defining a key adaptation to periods of gut inflammation.

microbiology↗