Acta Med. 2002, 45: 3-5
https://doi.org/10.14712/18059694.2019.49
Anthrax Toxin Characterization
References
1. R, Batra S. Anthrax toxin. Crit Rev Microbiol 2001; 27:167–200.
<https://doi.org/10.1080/20014091096738>
2. F, Mock M. Toxins of Bacillus anthracis. Toxicon 2001; 39:1747–55.
<https://doi.org/10.1016/S0041-0101(01)00161-1>
3. F, Weber-Levy M, Mock M, Sirard JC. Protective antigen-mediated antibody response against a heterologous protein produced in vivo by Bacillus anthracis. Infect Immun 2000; 68:5731–4.
<https://doi.org/10.1128/IAI.68.10.5731-5734.2000>
4. H, Agrawal D, Kushner N, Touzjian N, Essex M, Lu Y. Delivery of exogenous protein antigens to major histocompatibility complex class I pathway in cytosol. J Infect Dis 2002; 185:244–51.
<https://doi.org/10.1086/338448>
5. DC, Rennie RP. The ecology of anthrax spores: tough but not invincible. Can Vet J 1995; 36:295–301.
6. CL, Shen Y, Rice PA, Bohm A, Tang WJ. Crystallization and preliminary X-ray study of the edema factor exotoxin adenylyl cyclase domain from Bacillus anthracis in the presence of its activator, calmodulin. Acta Crystallogr D Biol Crystallogr 2001; 57:1881–4.
<https://doi.org/10.1107/S0907444901014937>
7. NS, Webb CP, Leppla SH et al. Proteolytic inactivation of MAP-kinase- kinase by anthrax lethal factor. Science 1998;280:734–7. Comment in: Science 280: 1673–4 and Science 1998; 280:676.
<https://doi.org/10.1126/science.280.5364.734>
8. NS, Vande Woude GF. Anthrax lethal factor causes proteolytic inactivation of mitogen-activated protein kinase kinase. J Appl Microbiol 1999; 87:289–93.
<https://doi.org/10.1046/j.1365-2672.1999.00892.x>
9. C, Weber-Levy M, Mock M, Cabiaux V. Translocation of Bacillus anthracis lethal and oedema factors across endosome membranes. Cell Microbiol 2000; 2:259–64.
<https://doi.org/10.1046/j.1462-5822.2000.00057.x>
10. P. Lethal toxin actions and their consequences. J Appl Microbiol 1999; 87:285–7.
<https://doi.org/10.1046/j.1365-2672.1999.00891.x>
11. E, Okstad OA, Caugant DA et al. Bacillus anthracis, Bacillus cereus, and Bacillus thuringiensis – one species on the basis of genetic evidence. Appl Environ Microbiol 2000; 66:2627–30.
<https://doi.org/10.1128/AEM.66.6.2627-2630.2000>
12. P, Ahuja N, Bhatnagar R. Purification of anthrax edema factor from Escherichia coli and identification of residues required for binding to anthrax protective antigen. Infect Immun 2001; 69:6532–6.
<https://doi.org/10.1128/IAI.69.10.6532-6536.2001>
<PubMed>
13. M, Fouet A. Anthrax. Annu Rev Microbiol 2001; 55:647–71.
<https://doi.org/10.1146/annurev.micro.55.1.647>
14. S, Collier RJ, Finkelstein A. PA63 channel of anthrax toxin: an extended beta-barrel. Biochemistry 2002; 41:1445–50.
<https://doi.org/10.1021/bi0119518>
15. AD, Wong TY, Schwarzenbacher R et al. Crystal structure of the anthrax lethal factor. Nature 2001; 414:229–33.
<https://doi.org/10.1038/n35101998>
16. JC, Guidi-Rontani C, Fouet A, Mock M. Characterization of a plasmid region involved in Bacillus anthracis toxin production and pathogenesis. Int J Med Microbiol 2000; 290:313–16.
<https://doi.org/10.1016/S1438-4221(00)80030-2>
17. S, Little S, Friedlander A, Fritz D, Fellows P. The role of antibodies to Bacillus anthracis and anthrax toxin components in inhibiting the early stages of infection by anthrax spores. Microbiology 2001; 147:1677–85.
<https://doi.org/10.1099/00221287-147-6-1677>
18. J, Milne JC, Collier RJ. Effect of anthrax toxin’s lethal factor on ion channels formed by the protective antigen. J Biol Chem 1995; 270:18626–30.
<https://doi.org/10.1074/jbc.270.31.18626>
