Cover caption: The cover image is based on the Research Article Root nodules of red alder (Alnus rubra) and Sitka alder (Alnus viridis ssp. sinuata) are inhabited by taxonomically diverse cultivable microbial endophytes by Robyn Dove et al., https://doi.org/10.1002/mbo3.1422.

Image credit to Felisha Pooler.

This paper explores the application of a novel DNA sequence type, specifically conserved signature genes encoding conserved signature proteins (CSPs), for bacterial identification. Although our focus is on the identification of Escherichia coli, the same principle can be extended to identify other taxa using their respective CSPs.

This study uses turbidimetric bioassays to detect antimicrobial activity in asymptomatic bacteriuria (ABU) isolates against uropathogenic E. coli (UPEC). The cell-free supernatant (CFS) from eight ABU isolates showed promising results. Notably, E. coli PUTS 58 and SK-106-1 demonstrated enhanced activity in artificial urine medium. The findings suggest a potential use of ABU bacteriocin-producers as prophylactics and therapeutics amidst rising antibiotic resistance.

Plants that host nitrogen-fixing symbionts in their root nodules play a significant role in both ecology and economy. However, the secondary members of these root nodule microbiomes have not been thoroughly studied. Our field survey conducted on Mount St. Helens revealed that both red Alder and Sitka Alder host a diverse range of cultivable microorganisms in their root nodules.

This study investigates the biogeographical patterns of bacterial communities in the gastrointestinal tract of Ampullaceana balthica snails compared with those in sediment and water. The findings indicate that substrate type significantly influences bacterial community composition, with distinct patterns observed in snail gastrointestinal tract communities. The research highlights the role of local water bacterial communities in colonizing the gastrointestinal tract, contributing to our understanding of host-associated bacterial biogeography.

The protein AgtB has a specific affinity for 5-aminovalerate. In contrast, both PA0602 and PA4985 show a strong preference for GABA, with secondary affinities for 5-aminovalerate and ethylenediamine. Despite these findings, there is no evidence to suggest that these solute-binding proteins—PA0602, PA4985, and AgtB—have any role in activating the AgtS and AruS sensor histidine kinases.

This study marks the first assessment of the prevalence, resistome, and genomic characteristics of multidrug-resistant (MDR) Stenotrophomonas maltophilia in residential aged care facilities. MDR S. maltophilia were found in all sampled facilities, with colistin non-wild type and trimethoprim-sulfamethoxazole resistant isolates recovered. Many isolates also exhibited high tolerance to triclosan and benzalkonium chloride. Notably, our findings indicate the continued emergence of S. maltophilia, with lineages not previously identified in Australia observed in this study. This underscores the urgent need for comprehensive surveillance and effective control measures.

In this study, we successfully cultivated the cable bacteria strain Electronema aureum GS on a newly developed synthetic sediment, marking the first instance of such cultivation on synthetic rather than natural sediment. The combination of this synthetic sediment and a specially designed sediment bioreactor enables reproducible cultivation of cable bacteria. This advancement paves the way for future investigations into the potential application of cable bacteria in bioprocess engineering.

G-1, a selective agonist of the G protein-coupled estrogen receptor (GPER), mitigates the pathogenesis mediated by alpha-hemolysin, a toxin produced by Staphylococcus aureus. It achieves this by reducing the surface display of the toxin's receptor, ADAM10. Our study, conducted on macrophage-like differentiated THP-1 cells, reveals that treatment with G-1 leads to a decrease in ATP release, a reduction in the activity of the caspase-1 enzyme, and a decrease in cell death following exposure to alpha-hemolysin.