Biomaterial Database

Pseudomonas aeruginosa ExoS and ExoT. 2004

J T Barbieri, and J Sun

Microbiology and Molecular Genetics, Medical College of Wisconsin, 8701 Watertown Plk. Road, Milwaukee, WI 53226, USA. jtb01@mcw.edu

ExoS and ExoT are bi-functional type-III cytotoxins of Pseudomonas aeruginosa that share 76% primary amino acid homology and contain N-terminal RhoGAP domains and C-terminal ADP-ribosylation domains. The Rho GAP activities of ExoS and ExoT appear to be biochemically and biologically identical, targeting Rho, Rac, and Cdc42. Expression of the RhoGAP domain in mammalian cells results in the disruption of the actin cytoskeleton and interference of phagocytosis. Expression of the ADP-ribosyltransferase domain of ExoS elicits a cytotoxic phenotype in cultured cells, while expression of ExoT appears to interfere with host cell phagocytic activity. Recent studies showed that ExoS and ExoT ADP-ribosylate different substrates. While ExoS has poly-substrate specificity and can ADP-ribosylate numerous host proteins, ExoT ADP-ribosylates a more restricted subset of host proteins including the Crk proteins. Protein modeling predicts that electrostatic interactions contribute to the substrate specificity of the ADP-ribosyltransferase domains of ExoS and ExoT.

UI	MeSH Term	Description	Entries
D008958	Models, Molecular	Models used experimentally or theoretically to study molecular shape, electronic properties, or interactions; includes analogous molecules, computer-generated graphics, and mechanical structures.	Molecular Models,Model, Molecular,Molecular Model
D010587	Phagocytosis	The engulfing and degradation of microorganisms; other cells that are dead, dying, or pathogenic; and foreign particles by phagocytic cells (PHAGOCYTES).	Phagocytoses
D011487	Protein Conformation	The characteristic 3-dimensional shape of a protein, including the secondary, supersecondary (motifs), tertiary (domains) and quaternary structure of the peptide chain. PROTEIN STRUCTURE, QUATERNARY describes the conformation assumed by multimeric proteins (aggregates of more than one polypeptide chain).	Conformation, Protein,Conformations, Protein,Protein Conformations
D011550	Pseudomonas aeruginosa	A species of gram-negative, aerobic, rod-shaped bacteria commonly isolated from clinical specimens (wound, burn, and urinary tract infections). It is also found widely distributed in soil and water. P. aeruginosa is a major agent of nosocomial infection.	Bacillus aeruginosus,Bacillus pyocyaneus,Bacterium aeruginosum,Bacterium pyocyaneum,Micrococcus pyocyaneus,Pseudomonas polycolor,Pseudomonas pyocyanea
D002462	Cell Membrane	The lipid- and protein-containing, selectively permeable membrane that surrounds the cytoplasm in prokaryotic and eukaryotic cells.	Plasma Membrane,Cytoplasmic Membrane,Cell Membranes,Cytoplasmic Membranes,Membrane, Cell,Membrane, Cytoplasmic,Membrane, Plasma,Membranes, Cell,Membranes, Cytoplasmic,Membranes, Plasma,Plasma Membranes
D001427	Bacterial Toxins	Toxic substances formed in or elaborated by bacteria; they are usually proteins with high molecular weight and antigenicity; some are used as antibiotics and some to skin test for the presence of or susceptibility to certain diseases.	Bacterial Toxin,Toxins, Bacterial,Toxin, Bacterial
D019143	Evolution, Molecular	The process of cumulative change at the level of DNA; RNA; and PROTEINS, over successive generations.	Molecular Evolution,Genetic Evolution,Evolution, Genetic
D020690	GTPase-Activating Proteins	Proteins that activate the GTPase of specific GTP-BINDING PROTEINS.	GAP Proteins,GAP Protein,GTPase-Activating Protein,GTPase Activating Protein,GTPase Activating Proteins
D036002	ADP Ribose Transferases	Enzymes that transfer the ADP-RIBOSE group of NAD or NADP to proteins or other small molecules. Transfer of ADP-ribose to water (i.e., hydrolysis) is catalyzed by the NADASES. The mono(ADP-ribose)transferases transfer a single ADP-ribose. POLY(ADP-RIBOSE) POLYMERASES transfer multiple units of ADP-ribose to protein targets, building POLY ADENOSINE DIPHOSPHATE RIBOSE in linear or branched chains.	ADP-Ribosyltransferase,Mono(ADP-Ribose) Transferases,NAD(P)(+)-Arginine ADP-Ribosyltransferase,NAD+ ADP-Ribosyltransferase,ADP Ribose Transferase,ADPRT,ADPRTs,ART Transferase,ART Transferases,ARTase,ARTases,Mono ADP-ribose Transferases,Mono ADPribose Transferase,Mono ADPribose Transferases,Mono(ADP-Ribose) Transferase,Mono(ADP-Ribosyl)transferase,Mono(ADPribosyl)transferase,Mono-ADP-Ribosyltransferase,MonoADPribosyltransferase,NAD ADP-Ribosyltransferase,NAD(+)-L-arginine ADP-D-ribosyltransferase,NAD-Agmatine ADP-Ribosyltransferase,NAD-Arginine ADP-Ribosyltransferase,NADP-ADPRTase,NADP-Arginine ADP-Ribosyltransferase,ADP Ribosyltransferase,ADP-Ribosyltransferase, NAD,ADP-Ribosyltransferase, NAD+,ADP-Ribosyltransferase, NAD-Agmatine,ADP-Ribosyltransferase, NAD-Arginine,ADP-Ribosyltransferase, NADP-Arginine,ADP-ribose Transferases, Mono,ADPribose Transferase, Mono,ADPribose Transferases, Mono,Mono ADP Ribosyltransferase,Mono ADP ribose Transferases,NAD ADP Ribosyltransferase,NAD Agmatine ADP Ribosyltransferase,NAD Arginine ADP Ribosyltransferase,NAD+ ADP Ribosyltransferase,NADP ADPRTase,NADP Arginine ADP Ribosyltransferase,Ribose Transferase, ADP,Ribose Transferases, ADP,Transferase, ADP Ribose,Transferase, ART,Transferase, Mono ADPribose,Transferases, ADP Ribose,Transferases, ART,Transferases, Mono ADP-ribose,Transferases, Mono ADPribose