E. coli’s internal bomb – the toxin-antitoxin system – could be triggered to make bacteria turn on themselves, offering a new target for antimicrobial approaches in drug design.
Horizontal gene transfer plagues the control of multi-drug resistant infections, but how exactly are genes transferred and can we stop them? In a recent Cell paper, Rubio-Cosials and colleagues detail the biochemical events leading up to the transfer of transposons carrying antibiotic resistance genes.
This study, recently published in Future Microbiology, aimed to study the effects of encoded heat-shock protein 90 homolog (htpG) on the selected virulence factors responsible for pathogenesis and biofilm formation of P. aeruginosa.
This research, published in Future Microbiology, screens host proteins for those that interact with EspF via flow cytometry and high-throughput screening to try and shed light on how EspF affects host cells to induce colitis and even colorectal carcinogenesis.
Scientists have unveiled the molecular architecture of two key proteins required for bacillus cell wall elongation. Inhibiting their interaction could provide a new mode of action for antibiotics against highly resistant bacteria.
Researchers have demonstrated that individual E. coli cells can sense the mechanical environment via voltage-induced calcium fluxes, a mechanism similar to that seen in vertebrate’s sensory neurons.
Researchers from the Washington University School of Medicine examined the role of yersiniabactin (Ybt) in copper import in bacteria. Their findings indicate that bacteria are able to utilize Ybt to obtain copper as a source of nutrition.
Researchers have discovered that cell division sites in mycobacteria are correlated with inherited wave-like morphological landmarks on the cell surface.
In this exclusive piece the authors discuss the choice of peptide antigen, delivery system/adjuvant and delivery route as key factors in the development of an effective human vaccine against group A Streptococcus.
In this original research article, the authors determine the structural contributions of a compound set containing inhibitors of bacterial enzyme FabI.
