BIOMAT Database Logo BIOMAT Database Logo

Induction of autophagy by anthrax lethal toxin. 2009

Yian Kim Tan, and Caroline M Kusuma, and Lena J St John, and Hao A Vu, and Kenneth Alibek, and Aiguo Wu
Molecular and Microbiology Department, College of Sciences, George Mason University, Manassas, VA 22010, USA.

Autophagy is an evolutionary conserved intracellular process whereby cells break down long-lived proteins and organelles. Accumulating evidences suggest increasing physiological significance of autophagy in pathogenesis of infectious diseases. Anthrax lethal toxin (LT) exerts its influence on numerous cells and herein, we report a novel effect of LT-induced autophagy on mammalian cells. Several autophagy biochemical markers including LC3-II conversion, increased punctuate distribution of GFP-LC3 and development of acidic vesicular organelles (AVO) were detected in cells treated with LT. Analysis of individual LT component revealed a moderate increase in LC3-II conversion for protective antigen-treated cells, whereas the LC3-II level in lethal factor-treated cells remained unchanged. In addition, our preliminary findings suggest a protective role of autophagy in LT intoxication as autophagy inhibition resulted in accelerated cell death. This study presents a hitherto undescribed effect of LT-induced autophagy on cells and provides the groundwork for future studies on the implication of autophagy in anthrax pathogenesis.

UI MeSH Term Description Entries
D008869 Microtubule-Associated Proteins High molecular weight proteins found in the MICROTUBULES of the cytoskeletal system. Under certain conditions they are required for TUBULIN assembly into the microtubules and stabilize the assembled microtubules. Ensconsin,Epithelial MAP, 115 kDa,Epithelial Microtubule-Associate Protein, 115 kDa,MAP4,Microtubule Associated Protein,Microtubule Associated Protein 4,Microtubule Associated Protein 7,Microtubule-Associated Protein,Microtubule-Associated Protein 7,E-MAP-115,MAP1 Microtubule-Associated Protein,MAP2 Microtubule-Associated Protein,MAP3 Microtubule-Associated Protein,Microtubule Associated Proteins,Microtubule-Associated Protein 1,Microtubule-Associated Protein 2,Microtubule-Associated Protein 3,7, Microtubule-Associated Protein,Associated Protein, Microtubule,E MAP 115,Epithelial Microtubule Associate Protein, 115 kDa,MAP1 Microtubule Associated Protein,MAP2 Microtubule Associated Protein,MAP3 Microtubule Associated Protein,Microtubule Associated Protein 1,Microtubule Associated Protein 2,Microtubule Associated Protein 3,Microtubule-Associated Protein, MAP1,Microtubule-Associated Protein, MAP2,Microtubule-Associated Protein, MAP3,Protein 7, Microtubule-Associated,Protein, Microtubule Associated,Protein, Microtubule-Associated
D002460 Cell Line Established cell cultures that have the potential to propagate indefinitely. Cell Lines,Line, Cell,Lines, Cell
D003600 Cytosol Intracellular fluid from the cytoplasm after removal of ORGANELLES and other insoluble cytoplasmic components. Cytosols
D000165 Acridine Orange A cationic cytochemical stain specific for cell nuclei, especially DNA. It is used as a supravital stain and in fluorescence cytochemistry. It may cause mutations in microorganisms. Tetramethyl Acridine Diamine,3,6-Bis(dimethylamino)acridine,Acridine Orange Base,Basic Orange 3RN,C.I. 46005,C.I. Basic Orange 14,Euchrysine,N,N,N',N'-Tetramethyl-3,6-Acridinediamine Hydrochloride,Rhoduline Orange,Acridine Diamine, Tetramethyl,Base, Acridine Orange,Diamine, Tetramethyl Acridine,Orange 3RN, Basic,Orange Base, Acridine,Orange, Acridine,Orange, Rhoduline
D000225 Adenine A purine base and a fundamental unit of ADENINE NUCLEOTIDES. Vitamin B 4,4, Vitamin B,B 4, Vitamin
D000818 Animals Unicellular or multicellular, heterotrophic organisms, that have sensation and the power of voluntary movement. Under the older five kingdom paradigm, Animalia was one of the kingdoms. Under the modern three domain model, Animalia represents one of the many groups in the domain EUKARYOTA. Animal,Metazoa,Animalia
D000942 Antigens, Bacterial Substances elaborated by bacteria that have antigenic activity. Bacterial Antigen,Bacterial Antigens,Antigen, Bacterial
D001343 Autophagy The segregation and degradation of various cytoplasmic constituents via engulfment by MULTIVESICULAR BODIES; VACUOLES; or AUTOPHAGOSOMES and their digestion by LYSOSOMES. It plays an important role in BIOLOGICAL METAMORPHOSIS and in the removal of bone by OSTEOCLASTS. Defective autophagy is associated with various diseases, including NEURODEGENERATIVE DISEASES and cancer. Autophagocytosis,ER-Phagy,Lipophagy,Nucleophagy,Reticulophagy,Ribophagy,Autophagy, Cellular,Cellular Autophagy,ER Phagy
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
D014617 Vacuoles Any spaces or cavities within a cell. They may function in digestion, storage, secretion, or excretion. Vacuole

Related Publications

Yian Kim Tan, and Caroline M Kusuma, and Lena J St John, and Hao A Vu, and Kenneth Alibek, and Aiguo Wu
Anthrax lethal toxin and the induction of CD4 T cell immunity.
October 2012, Toxins,
Yian Kim Tan, and Caroline M Kusuma, and Lena J St John, and Hao A Vu, and Kenneth Alibek, and Aiguo Wu
Cisplatin inhibition of anthrax lethal toxin.
August 2006, Antimicrobial agents and chemotherapy,
Yian Kim Tan, and Caroline M Kusuma, and Lena J St John, and Hao A Vu, and Kenneth Alibek, and Aiguo Wu
Anthrax toxin: a tripartite lethal combination.
November 2002, FEBS letters,
Yian Kim Tan, and Caroline M Kusuma, and Lena J St John, and Hao A Vu, and Kenneth Alibek, and Aiguo Wu
Crystallographic studies of the anthrax lethal toxin
August 1999, Journal of applied microbiology,
Yian Kim Tan, and Caroline M Kusuma, and Lena J St John, and Hao A Vu, and Kenneth Alibek, and Aiguo Wu
Novel repression of the glucocorticoid receptor by anthrax lethal toxin.
June 2004, Annals of the New York Academy of Sciences,
Yian Kim Tan, and Caroline M Kusuma, and Lena J St John, and Hao A Vu, and Kenneth Alibek, and Aiguo Wu
Perturbation of mouse retinal vascular morphogenesis by anthrax lethal toxin.
September 2009, PloS one,
Yian Kim Tan, and Caroline M Kusuma, and Lena J St John, and Hao A Vu, and Kenneth Alibek, and Aiguo Wu
Sensitizing anthrax lethal toxin-resistant macrophages to lethal toxin-induced killing by tumor necrosis factor-alpha.
February 2003, The Journal of biological chemistry,
Yian Kim Tan, and Caroline M Kusuma, and Lena J St John, and Hao A Vu, and Kenneth Alibek, and Aiguo Wu
Expression of anthrax lethal factor gene by osmolyte induction.
April 2002, FEMS microbiology letters,
Yian Kim Tan, and Caroline M Kusuma, and Lena J St John, and Hao A Vu, and Kenneth Alibek, and Aiguo Wu
Oxidized ATP protection against anthrax lethal toxin.
July 2006, Infection and immunity,
Yian Kim Tan, and Caroline M Kusuma, and Lena J St John, and Hao A Vu, and Kenneth Alibek, and Aiguo Wu
CA-074Me protection against anthrax lethal toxin.
October 2009, Infection and immunity,
Copied contents to your clipboard!