Development of a hybrid photo-bioreactor and nanoparticle adsorbent system for the removal of CO, and selected organic and metal co-pollutants.

Fossil fuel combustion and many industrial processes generate gaseous emissions that contain a number of toxic organic pollutants and carbon dioxide (CO) which contribute to climate change and atmospheric pollution. There is a need for green and sustainable solutions to remove air pollutants, as opposed to conventional techniques which can be expensive, consume additional energy and generate further waste. We developed a novel integrated bioreactor combined with recyclable iron oxide nano/micro-particle adsorption interfaces, to remove CO and undesired organic air pollutants using natural particles, while generating oxygen.

Localization of the C3-Like ADP-ribosyltransferase from Staphylococcus aureus during bacterial invasion of mammalian cells.

The C3stau2 exoenzyme from Staphylococcus aureus is a C3-like ADP-ribosyltransferase which possesses no specific receptor-binding domain or translocation unit required for entry in target cells where its substrate is located. Here we show that C3stau2 can reach its target after invasion of staphylococci in eukaryotic cells without needing translocation.

Cellular uptake of Clostridium botulinum C2 toxin: membrane translocation of a fusion toxin requires unfolding of its dihydrofolate reductase domain.

The Clostridium botulinum C2 toxin is the prototype of the family of binary actin-ADP-ribosylating toxins. C2 toxin is composed of two separated nonlinked proteins. The enzyme component C2I ADP-ribosylates actin in the cytosol of target cells.

Glucosylation of Ras by Clostridium sordellii lethal toxin: consequences for effector loop conformations observed by NMR spectroscopy.

The lethal toxin (LT) from Clostridium sordellii, which belongs to the family of large clostridial cytotoxins, acts as a monoglucosyltransferase for the Rho subfamily GTPase Rac and also modifies Ras. In the present study we investigated structural changes of H-Ras in its di- and triphosphate form that occur upon glucosylation of the effector domain amino acid threonine-35 by LT. (31)P NMR experiments recorded during the enzymatic glucosylation process, using UDP-glucose as a cosubstrate, show that the modification of the threonine side chain influences the chemical shifts of the phosphate groups of the bound nucleotides.

Rho-specific Bacillus cereus ADP-ribosyltransferase C3cer cloning and characterization.

C3-like ADP-ribosyltransferases represent an expanding family of related exoenzymes, which are produced by Clostridia and various Staphylococcus aureus strains. Here we report on the cloning and biochemical characterization of an ADP-ribosyltransferase from Bacillus cereus strain 2339. The transferase encompasses 219 amino acids; it has a predicted mass of 25.

Interaction of the Rho-ADP-ribosylating C3 exoenzyme with RalA.

RhoA, -B, and -C are ADP-ribosylated and biologically inactivated by Clostridium botulinum C3 exoenzyme and related C3-like transferases. We report that RalA GTPase, which is not ADP-ribosylated by C3, inhibits ADP-ribosylation of RhoA by C3 from C. botulinum (C3bot), Clostridium limosum (C3lim), and Bacillus cereus (C3cer) but not from Staphylococcus aureus (C3stau) in human platelet membranes and rat brain lysate.

Structure-function analysis of the Rho-ADP-ribosylating exoenzyme C3stau2 from Staphylococcus aureus.

Exoenzyme C3stau2 from Staphylococcus aureus is a new member of the family of C3-like ADP-ribosyltransferases that ADP-ribosylates RhoA, -B, and -C. Additionally, it modifies RhoE and Rnd3. Here we report on studies of the structure-function relationship of recombinant C3stau2 by site-directed mutagenesis.

C3stau, a new member of the family of C3-like ADP-ribosyltransferases.

C3-like ADP-ribosyltransferases, which are produced by Clostridium botulinum, Clostridium limosum, Bacillus cereus and Staphylococcus aureus, are exoenzymes lacking a translocation unit. These enzymes specifically inactivate Rho GTPases in host target cells. Recently, a novel C3-like transferase from S.