Anthrax toxin: the long and winding road that leads to the kill.
The past five years have led to a tremendous increase in our molecular understanding of the mode of action of the anthrax toxin, one of the two main virulence factors produced by Bacillus anthracis. The structures of each of the three components of the toxin--lethal factor (LF), edema factor (EF) and protective antigen (PA)--have been solved not only in their monomeric forms but, depending on the subunit, in a heptameric form, bound to their substrate, co-factor or receptor. The endocytic route followed by the toxin has also been unraveled and the enzymatic mechanisms of EF and LF elucidated.
Abrami
Laurence
L
Department of Microbiology and Molecular Medicine, University of Geneva, 1 rue Michel Servet, 1211 Geneva 4, Switzerland.
Reig
Nuria
N
van der Goot
F Gisou
FG
D000881:Anthrax / Q000378:metabolism* / Q000382:microbiology; D000942:Antigens, Bacterial / Q000737:chemistry / Q000502:physiology*; D001408:Bacillus anthracis / Q000737:chemistry / Q000378:metabolism*; D001427:Bacterial Toxins / Q000737:chemistry; D006801:Humans; D008565:Membrane Proteins / Q000378:metabolism; D008840:Microfilament Proteins; D008958:Models, Molecular; D009363:Neoplasm Proteins; D011956:Receptors, Cell Surface / Q000378:metabolism; D018000:Receptors, Peptide
C473287:ANTXR1 protein, human; C447150:ANTXR2 protein, human; D000942:Antigens, Bacterial; D001427:Bacterial Toxins; D008565:Membrane Proteins; D008840:Microfilament Proteins; D009363:Neoplasm Proteins; D011956:Receptors, Cell Surface; D018000:Receptors, Peptide; C030325:anthrax toxin