Identification, characterization, and genome sequencing of Brevibacterium sediminis MG-1 isolate with growth-promoting properties.

In recent years, plant growth-promoting rhizobacteria (PGPR) have received increased attention due to their prospective use as biofertilizers for the enhancement of crop growth and yields. However, there is a growing need to identify new PGPR isolates with additional beneficial properties. In this paper, we describe the identification of a new strain of a non-sporulating Gram-positive bacterium isolated from the rhizosphere of potato plants, classified as Brevibacterium sediminis MG-1 based on whole-genome sequencing. The bacteria are aerobic; they grow in a pH range of 6.0-10.0 (optimum 6.0), and a temperature range of 20-37 °C (optimum 30 °C). At 96 h of cultivation, strain MG-1 synthesizes 28.65 µg/ml of indole-3-acetic acid (IAA) when 500 µg/ml of l-tryptophan is added. It is a producer of catechol-type siderophores and ACC deaminase (213 ± 12.34 ng/ml) and shows halotolerance. Treatment of pea, rye, and wheat seeds with a suspension of MG-1 strain cells resulted in the stimulation of stem and root biomass accumulation by 12-26% and 6-25% (P < 0.05), respectively. Treatment of seeds with bacteria in the presence of high salt concentration reduced the negative effects of salt stress on plant growth by 18-50%. The hypothetical gene lin, encoding the bacteriocin Linocin-M18, RIPP-like proteins, and polyketide synthase type III (T3PKS) loci, gene clusters responsible for iron acquisition and metabolism of siderophores, as well as gene clusters responsible for auxin biosynthesis, were identified in the B. sediminis MG-1 genome. Thus, the rhizosphere-associated strain B. sediminis MG-1 has growth-stimulating properties and can be useful for the treatment of plants grown on soils with high salinity. Supplementary Information: The online version contains supplementary material available at 10.1007/s13205-022-03392-z.

Bacterial enzymes effectively digest Alzheimer's ß-amyloid peptide.

Aggregated ß-amyloid peptides play key roles in the development of Alzheimer's disease, and recent evidence suggests that microbial particles, among others, can facilitate their polymerization. Bacterial enzymes, however, have been proved to be beneficial in degrading pathological fibrillar structures in clinical settings, such as strepto-kinases in resolving blood-clots. The purpose of this study was to investigate the ability of bacterial substances to effectively hydrolyze ß-amyloid peptides. Degrading products of several proteinases from Bacillus pumilus were evaluated using MALDI-TOF mass-spectrometry, and their toxicity was assessed in vitro using cell-culture assays and morphological studies. These enzymes have proved to be non-toxic and were demonstrated to cleave through the functional domains of ß-amyloid peptide. By yielding inactive fragments, proteinases of Bacillus pumilus may be used as candidate anti-amyloid agents.