Talk:Anthrax toxin

Copyright assertation

I am a doctoral student and after a year and a half of researching the topic and after several drafts (which were used as term papers for my college courses), I wrote this article. I have a ton of figures for it, but the quality of some of them need to be improved. I've been swamped with my classes, work and my family, so it might a few months before I finish fixing the images and wikifying the article (I also recently noticed that many of my links to my references disappered when I was copying from my word perfect document, so I need to fix that too). Also I haven't had the time to figure out how to post new images. I'll try to update the article asap. I hold the copyright of the original posting of this article (yes, I posted a lot in one day... because I wrote it first in a word processor) and release it under the GFDL by posting it to wikipedia. If anyone has questions as to whether this is truly my original work, please contact me and I can discuss it with you. I once again verify that this is my original work and none of it has been plagiarize from any other source. --Nate 19:16, 10 November 2006 (UTC)

References

I began trying to reformat the references, but now I realize I'm not sure exactly where the references go. I reformatted the first 6 and just replaced the number in parentheses with a < ref > tag. I couldn't find reference #7 anywhere in the text. Without reading all the articles referenced, I don't think I can justify continuing to reformat. However, this is an excellent article and very well written. Good luck with your PhD work! Ramin Herati (Sedmic) 16:10, 17 December 2006 (UTC)

I too got lost in amongst the references after wikifying the first two sections. As a minor aside, I've worked in the bacterial toxin field in the past, and I have never heard the system of anthrax virulence factors referred to as a singular 'anthrax toxin'. The two A components of a binary toxin sharing a single B component is unique (i think)... but I've never heard anyone refer to Anthrax toxin. Possibly rename the page to Anthrax virulence factors (a bit wordy) or maybe Anthrax toxins.

Good work though. Bassophile 14:28, 15 January 2007 (UTC)

The correct name of the toxin is 'anthrax toxin.' Don't confuse the fact that 3 proteins are involved. Lethal toxin is a mixture of LF and PA. Anthrax toxin is a mixture of EF, LF and PA. None of these proteins on their own are toxic to cells. bakrantz

Additional Information

Some information on the genetics involved, and in particular the properties of the avirulent stern strain (lacks the pOX2 plasmid that codes for the poly-D-glutamic acid capsule) would be useful. Thats what I came to this page looking for and it wasn't present. I have too much to do right now to figure out a good way to add it but heres a quote and the source:

"Virulence

5. Prototypical virulent strains of B. anthracis synthesise three anthrax toxins and a poly-D-glutamic acid capsule, known to be involved in virulence. The structural genes for the toxin proteins are located on plasmid pXO1 and an operon encoding biosynthetic enzymes for the capsule are found on plasmid pXO2. The capsule confers anti-phagocytic properties on the bacteria and facilitates dissemination from the site of exposure. The three toxin proteins PA (protective antigen), LF (lethal factor) and EF (edema factor) are encoded by non-contiguous genes pagA, lef and cya respectively and regulated by a global regulator (AtxA), all of which are located on pXO1. The PA, is responsible for binding and toxin entry into cells, whereupon it is cleaved and forms a toxin complex with EF or LF. The PA-LF or PA-EF complex enters cells by endocytosis. The change in pH in the endosome results in conformational change in the complex, pore formation in the cell membrane and delivery of LF or EF into the cell cytosol (Heninger et al 2006).

6. In vivo studies, using toxigenic or capsular mutants have demonstrated that the capsule is essential for bacterial dissemination from the site of exposure and virulence in the murine model for inhalation anthrax (Drysdale et al 2005) and that the toxin proteins are not required for lethality but do effect the course of infection (Heninger et al 2006). Taken together these studies indicate that when present, the capsule is the prevailing virulence factor."

ADVISORY COMMITTEE ON DANGEROUS PATHOGENS CATEGORISATION OF STERNE STRAIN OF BACILLUS ANTHRACIS ACDP/87/P9 http://www.hse.gov.uk/aboutus/meetings/committees/acdp/021007/acdp87p9.pdf

Repapetilto (talk) 01:22, 19 February 2009 (UTC)

Human genetic variation altering anthrax toxin sensitivity

Could you insert this? http://www.pnas.org/content/early/2012/01/30/1121006109 --Biggerj1 (talk) 14:42, 2 March 2012 (UTC)

EF is an adenylate cyclase or activates a cellular adenylate cycles?

In a pubmed article, it is stated "EF, a calmodulin- and Ca2+-dependent adenylate cyclase, is responsible for the edema seen in the disease.", while this article seems to state that EF stimulates a cellular adenylate cyclase. I tend to believe the PubMed version, but am not confident enough to change the article. Need a biochemists opinion here. — Preceding unsigned comment added by 50.149.238.168 (talk) 17:11, 28 September 2013 (UTC)

EF is an adenylate cyclase. ATP is converted to cAMP by EF directly. This wiki should be checked over for that error because it does not stimulate the activity, since it is the activity. — Preceding unsigned comment added by 134.192.6.40 (talk) 19:50, 17 October 2014 (UTC)

Complete rewrite needed

This article seems to mostly come from a (badly written) thesis introduction or review draft, even still including the references to figures etc. It needs drastic trimming of superfluous information, and significant rewrite, removing poor grammar and spelling. I will try and get this done asap when I have time. 131.251.254.154 (talk) 13:10, 27 October 2015 (UTC)

Assessment comment

The comment(s) below were originally left at Talk:Anthrax toxin/Comments, and are posted here for posterity. Following several discussions in past years, these subpages are now deprecated. The comments may be irrelevant or outdated; if so, please feel free to remove this section.

I've been doing a review of Protective-Antigen related work, and this article suggests that the pore maintains contact with the cellular receptor after insertion. There is evidence suggesting otherwise using immunoprecipitation assays which show receptor release associated with a pH drop (Fig. 2 in Rainey, et all PNAS (2005) Vol. 102, No.37), indicating that the idea of a cellular receptor 'supporting' the pore for insertion may be inaccurate, since pore insertion is observed in lipid bilayers in the absence of cellular receptors. I'm genuinely curious about what role(s) the ATR may play besides localizing PA83 to the membrane for removal of the 20 kDa fragment prior to oligomerization, so any more info or insight you have would be great. Thanks! AshleyP

Last edited at 23:41, 8 April 2008 (UTC). Substituted at 07:59, 29 April 2016 (UTC)