Rhizobacteria play a crucial role in plant health by providing natural antagonism against soil-borne fungi. The use of rhizobacteria has been viewed as an alternative to the use of chemicals that could be useful for the integrated management of plant diseases and also increase yield in an environmentally friendly manner. However, there is limited understanding of the specific mechanisms by which rhizobacteria inhibit these pathogens and the diversity of rhizobacterial species involved. This study aims to isolate, identify, and characterize rhizobacteria with antagonistic activities against soil-borne fungi. Laboratory tests were carried out on isolated rhizobacteria to evaluate their inhibitory activity against Rhizoctonia solani, Pythium aphanidermatum and Macrophomina phaseolina. The selected bacteria were identified using the Vitek 2 compact system and 16S rRNA genes. Experiments were carried out to evaluate the plant growth promotion and biocontrol ability of these selected isolates. Out of 324 rhizobacteria isolates obtained from various plant species, twelve were chosen due to their strong (>50 %) wide-ranging antifungal activity against three significant phytopathogenic fungi species. According to the identification results, they belong to the following species: Aeribacillus pallidus ECC4, Alloiococcus otitis BRE6, Aneurinibacillus thermoaerophilus ECL1, A. thermoaerophilus SDV1, Bacillus halotolerans DMC8, B. megaterium SKE2, B. megaterium TNK1, B. subtilis NAS1, Enterobacter cloacae complex BZD3, Leclercia adecarboxylata DKS3, Paenibacillus polymyxa TRS4, and Staphylococcus lentus BZD2. Eleven isolates produced protease, six isolates produced chitinase, and seven isolates were highly effective in producing hydrogen cyanide. Ten isolates could fix nitrogen, while all isolates could produce potassium, indole-3-acetic acid, siderophore, and ammonia. These findings enhance our understanding of rhizobacterial biodiversity and their potential as biocontrol agents in sustainable agriculture.© 2024 The Authors.

Escherichia coli is unable to grow on polymeric and oligomeric chitin, but grows on chitin disaccharide (GlcNAc-GlcNAc; N,N'-diacetylchitobiose) and chitin trisaccharide (GlcNAc-GlcNAc-GlcNAc; N,N',N''-triacetylchitotriose) via expression of the chb operon (chbBCARFG). The phosphotransferase system (PTS) transporter ChbBCA facilitates transport of both saccharides across the inner membrane and their concomitant phosphorylation at the non-reducing end, intracellularly yielding GlcNAc 6-phosphate-GlcNAc (GlcNAc6P-GlcNAc) and GlcNAc6P-GlcNAc-GlcNAc, respectively. We revisited the intracellular catabolism of the PTS products, thereby correcting the reported functions of the 6-phospho-glycosidase ChbF, the monodeacetylase ChbG, and the transcriptional regulator ChbR. Intracellular accumulation of glucosamine 6P-GlcNAc (GlcN6P-GlcNAc) and GlcN6P-GlcNAc-GlcNAc in a chbF mutant unraveled a role for ChbG as a monodeacetylase that removes the N-acetyl group at the non-reducing end. Consequently, GlcN6P- but not GlcNAc6P-containing saccharides likely function as coactivators of ChbR. Furthermore, ChbF removed the GlcN6P from the non-reducing terminus of the former saccharides, thereby degrading the inducers of the chb operon and facilitating growth on the saccharides. Consequently, ChbF was unable to hydrolyze GlcNAc6P-residues from the non-reducing end, contrary to previous assumptions but in agreement with structural modeling data and with the unusual catalytic mechanism of the family 4 of glycosidases, to which ChbF belongs. We also refuted the assumption that ChiA is a bifunctional endochitinase/lysozyme ChiA, and show that it is unable to degrade peptidoglycans but acts as a bona fide chitinase in vitro and in vivo, enabling growth of E. coli on chitin oligosaccharides when ectopically expressed. Overall, this study revises our understanding of the chitin, chitin oligosaccharide, and chitin disaccharide metabolism of E. coli.
© 2021 The Author(s). Published by S. Karger AG, Basel.