Haemophilus Protein F Orthologs of Pathogens Infecting the Airways: Exploiting Host Laminin at Heparin-Binding Sites for Maximal Adherence to Epithelial Cells.

Haemophilus influenzae protein F (PF) is an important virulence factor interacting with laminin, an extracellular matrix protein ubiquitously expressed in the respiratory tract. Here we defined PF orthologs in Pseudomonas aeruginosa, Moraxella catarrhalis, and Staphylococcus aureus, bacteria that occasionally colonize and infect the human airways. Despite low sequence homology (48.

Response of Vibrio cholerae to the Catecholamine Hormones Epinephrine and Norepinephrine.

Unlabelled: In Escherichia coli or Salmonella enterica, the stress-associated mammalian hormones epinephrine (E) and norepinephrine (NE) trigger a signaling cascade by interacting with the QseC sensor protein. Here we show that Vibrio cholerae, the causative agent of cholera, exhibits a specific response to E and NE. These catecholates (0.

Serine 26 in the PomB subunit of the flagellar motor is essential for hypermotility of Vibrio cholerae.

Vibrio cholerae is motile by means of its single polar flagellum which is driven by the sodium-motive force. In the motor driving rotation of the flagellar filament, a stator complex consisting of subunits PomA and PomB converts the electrochemical sodium ion gradient into torque. Charged or polar residues within the membrane part of PomB could act as ligands for Na+, or stabilize a hydrogen bond network by interacting with water within the putative channel between PomA and PomB.

Central role of the Na(+)-translocating NADH:quinone oxidoreductase (Na(+)-NQR) in sodium bioenergetics of Vibrio cholerae.

Vibrio cholerae is a Gram-negative bacterium that lives in brackish or sea water environments. Strains of V. cholerae carrying the pathogenicity islands infect the human gut and cause the fatal disease cholera.

Roles of the sodium-translocating NADH:quinone oxidoreductase (Na+-NQR) on vibrio cholerae metabolism, motility and osmotic stress resistance.

The Na+ translocating NADH:quinone oxidoreductase (Na+-NQR) is a unique respiratory enzyme catalyzing the electron transfer from NADH to quinone coupled with the translocation of sodium ions across the membrane. Typically, Vibrio spp., including Vibrio cholerae, have this enzyme but lack the proton-pumping NADH:ubiquinone oxidoreductase (Complex I).

The function of the Na+-driven flagellum of Vibrio cholerae is determined by osmolality and pH.

Vibrio cholerae is motile by its polar flagellum, which is driven by a Na(+)-conducting motor. The stators of the motor, composed of four PomA and two PomB subunits, provide access for Na(+) to the torque-generating unit of the motor. To characterize the Na(+) pathway formed by the PomAB complex, we studied the influence of chloride salts (chaotropic, Na(+), and K(+)) and pH on the motility of V.

Extracytoplasmic function σ factors of the widely distributed group ECF41 contain a fused regulatory domain.

Bacteria need signal transducing systems to respond to environmental changes. Next to one- and two-component systems, alternative σ factors of the extra-cytoplasmic function (ECF) protein family represent the third fundamental mechanism of bacterial signal transduction. A comprehensive classification of these proteins identified more than 40 phylogenetically distinct groups, most of which are not experimentally investigated.