Biomaterial Database

Toward a structural understanding of Clostridium difficile toxins A and B. 2012

Rory N Pruitt, and D Borden Lacy

Department of Pathology, Microbiology and Immunology, Vanderbilt University School of Medicine, Nashville TN, USA.

Clostridium difficile is a toxin-producing bacterium that is a frequent cause of hospital-acquired and antibiotic-associated diarrhea. The incidence, severity, and costs associated with C. difficile associated disease are substantial and increasing, making C. difficile a significant public health concern. The two primary toxins, TcdA and TcdB, disrupt host cell function by inactivating small GTPases that regulate the actin cytoskeleton. This review will discuss the role of these two toxins in pathogenesis and the structural and molecular mechanisms by which they intoxicate cells. A focus will be placed on recent publications highlighting mechanistic similarities and differences between TcdA, TcdB, and different TcdB variants.

UI	MeSH Term	Description	Entries
D008954	Models, Biological	Theoretical representations that simulate the behavior or activity of biological processes or diseases. For disease models in living animals, DISEASE MODELS, ANIMAL is available. Biological models include the use of mathematical equations, computers, and other electronic equipment.	Biological Model,Biological Models,Model, Biological,Models, Biologic,Biologic Model,Biologic Models,Model, Biologic
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
D004768	Enterotoxins	Substances that are toxic to the intestinal tract causing vomiting, diarrhea, etc.; most common enterotoxins are produced by bacteria.	Staphylococcal Enterotoxin,Enterotoxin,Staphylococcal Enterotoxins,Enterotoxin, Staphylococcal,Enterotoxins, Staphylococcal
D006801	Humans	Members of the species Homo sapiens.	Homo sapiens,Man (Taxonomy),Human,Man, Modern,Modern Man
D000199	Actins	Filamentous proteins that are the main constituent of the thin filaments of muscle fibers. The filaments (known also as filamentous or F-actin) can be dissociated into their globular subunits; each subunit is composed of a single polypeptide 375 amino acids long. This is known as globular or G-actin. In conjunction with MYOSINS, actin is responsible for the contraction and relaxation of muscle.	F-Actin,G-Actin,Actin,Isoactin,N-Actin,alpha-Actin,alpha-Isoactin,beta-Actin,gamma-Actin,F Actin,G Actin,N Actin,alpha Actin,alpha Isoactin,beta Actin,gamma Actin
D001426	Bacterial Proteins	Proteins found in any species of bacterium.	Bacterial Gene Products,Bacterial Gene Proteins,Gene Products, Bacterial,Bacterial Gene Product,Bacterial Gene Protein,Bacterial Protein,Gene Product, Bacterial,Gene Protein, Bacterial,Gene Proteins, Bacterial,Protein, Bacterial,Proteins, Bacterial
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
D016360	Clostridioides difficile	A common inhabitant of the colon flora in human infants and sometimes in adults. The type species Clostridioides difficile is formerly known as Clostridium difficile. It is a causative agent for CLOSTRIDIOIDES INFECTIONS and is associated with PSEUDOMEMBRANOUS ENTEROCOLITIS in patients receiving antibiotic therapy.	Clostridium difficile
D020559	Monomeric GTP-Binding Proteins	A class of monomeric, low molecular weight (20-25 kDa) GTP-binding proteins that regulate a variety of intracellular processes. The GTP bound form of the protein is active and limited by its inherent GTPase activity, which is controlled by an array of GTPase activators, GDP dissociation inhibitors, and guanine nucleotide exchange factors. This enzyme was formerly listed as EC 3.6.1.47	G-Proteins, Monomeric,GTP-Binding Proteins, Monomeric,Monomeric G-Protein,Monomeric G-Proteins,Small G-Protein,Small G-Proteins,Small GTPase,Small GTPases,ras-Related GTP-Binding Protein,ras-Related GTPase,ras-Related GTPases,ras-Related G-Proteins,ras-Related GTP-Binding Proteins,G Proteins, Monomeric,G-Protein, Monomeric,G-Protein, Small,G-Proteins, Small,G-Proteins, ras-Related,GTP Binding Proteins, Monomeric,GTP-Binding Protein, ras-Related,GTP-Binding Proteins, ras-Related,GTPase, Small,GTPase, ras-Related,GTPases, Small,GTPases, ras-Related,Monomeric G Protein,Monomeric G Proteins,Monomeric GTP Binding Proteins,Protein, ras-Related GTP-Binding,Proteins, ras-Related GTP-Binding,Small G Protein,Small G Proteins,ras Related G Proteins,ras Related GTP Binding Protein,ras Related GTP Binding Proteins,ras Related GTPase,ras Related GTPases
D037521	Virulence Factors	Those components of an organism that determine its capacity to cause disease but are not required for its viability per se. Two classes have been characterized: TOXINS, BIOLOGICAL and surface adhesion molecules that effect the ability of the microorganism to invade and colonize a host. (From Davis et al., Microbiology, 4th ed. p486)	Pathogenicity Factor,Pathogenicity Factors,Virulence Factor,Factor, Pathogenicity,Factor, Virulence,Factors, Pathogenicity,Factors, Virulence