Comparative label-free proteomics of the neonatal meningitis-causing K1 IHE3034 and RS218 morphotypes.

The proteome of two newborn meningitis K1 (NMEC) morphotypes was examined via a label-free proteomics approach. Besides shared NMEC virulence factors, the two strains have different evolutionary strategies-strain IHE3034 tends to perform anaerobic respiration continuously, while strain RS218 maintains its filamentous morphotype due to active SOS response.

Colony phase variation switch modulates antimicrobial tolerance and biofilm formation in .

Carbapenem-resistant causes one of the most difficult-to-treat nosocomial infections. Polycationic drugs like polymyxin B or colistin and tetracycline drugs such as doxycycline or minocycline are commonly used to treat infections caused by carbapenem-resistant . Here, we show that a subpopulation of cells associated with the opaque/translucent colony phase variation by AB5075 displays differential tolerance to subinhibitory concentrations of colistin and tetracycline.

Csu pili dependent biofilm formation and virulence of Acinetobacter baumannii.

Acinetobacter baumannii has emerged as one of the most common extensive drug-resistant nosocomial bacterial pathogens. Not only can the bacteria survive in hospital settings for long periods, but they are also able to resist adverse conditions. However, underlying regulatory mechanisms that allow A.

Metabolic and Morphotypic Trade-Offs within the Eco-Evolutionary Dynamics of Escherichia coli.

Escherichia coli arbitrarily encompasses facultative anaerobic, rod-shaped bacteria with defined respiratory and fermentative types of metabolism. The species diversification has been further advanced by atypical strains whose features deviate from the essential species-specific morphological and metabolic cutoff. The morphological cutoff is exemplified by bacterial filamentation.

Protein-lipid interaction at low pH induces oligomerization of the MakA cytotoxin from .

The α-pore-forming toxins (α-PFTs) from pathogenic bacteria damage host cell membranes by pore formation. We demonstrate a remarkable, hitherto unknown mechanism by an α-PFT protein from . As part of the MakA/B/E tripartite toxin, MakA is involved in membrane pore formation similar to other α-PFTs.