Literature DB >> 11577702

Toxins as weapons of mass destruction. A comparison and contrast with biological-warfare and chemical-warfare agents.

J M Madsen1.   

Abstract

Toxins are toxic chemical compounds synthesized in nature by living organisms. Classifiable by molecular weight, source, preferred targets in the body, and mechanism of action, they include the most potent poisons on the planet, although considerations of production, weaponization, delivery, environmental stability, and host factors place practical limits on their use as WMD. The two most important toxin threats on the battlefield or in bioterrorism are probably botulinum toxin (a series of seven serotypes, of which botulinum toxin A is the most toxic for humans) and SEB, an incapacitating toxin. Ricin and the trichothecene mycotoxins, including T-2 mycotoxin, are of lesser concern but are still potential threats. Botulinum toxin is a neurotoxin, ricin and trichothecene mycotoxins are membrane-damaging proteins, and SEB is a superantigen capable of massive nonspecific activation of the immune system. The clinical intoxications resulting from exposure to and absorption (usually by inhalation) of these agents reflect their underlying pathophysiology. Because of the hybrid nature of toxins, they have sometimes been considered CW agents and sometimes BW agents. The current trend seems to be to emphasize their similarities to living organisms and their differences from CW agents, but examination of all three groups relative to a number of factors reveals both similarities and differences between toxins and each of the other two categories of non-nuclear unconventional WMD. The perspective that groups toxins with BW agents is logical and very useful for research and development and for administrative and treaty applications, but for medical education and casualty assessment, there are real advantages in clinician use of assessment techniques that emphasize the physicochemical behavior of these nonliving, nonreplicating, intransmissible chemical poisons.

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Year:  2001        PMID: 11577702

Source DB:  PubMed          Journal:  Clin Lab Med        ISSN: 0272-2712            Impact factor:   1.935


  40 in total

1.  Protein engineering: security implications. The increasing ability to manipulate protein toxins for hostile purposes has prompted calls for regulation.

Authors:  Jonathan B Tucker; Craig Hooper
Journal:  EMBO Rep       Date:  2006-07       Impact factor: 8.807

2.  Superactivation of the botulinum neurotoxin serotype A light chain metalloprotease: a new wrinkle in botulinum neurotoxin.

Authors:  Laura A McAllister; Mark S Hixon; Jack P Kennedy; Tobin J Dickerson; Kim D Janda
Journal:  J Am Chem Soc       Date:  2006-04-05       Impact factor: 15.419

3.  In vitro and in vivo evaluation of staphylococcal superantigen peptide antagonists.

Authors:  Govindarajan Rajagopalan; Moon M Sen; Chella S David
Journal:  Infect Immun       Date:  2004-11       Impact factor: 3.441

4.  Acute systemic immune activation following conjunctival exposure to staphylococcal enterotoxin B.

Authors:  Govindarajan Rajagopalan; Michele K Smart; Robin Patel; Chella S David
Journal:  Infect Immun       Date:  2006-10       Impact factor: 3.441

5.  Role of CD44 and its v7 isoform in staphylococcal enterotoxin B-induced toxic shock: CD44 deficiency on hepatic mononuclear cells leads to reduced activation-induced apoptosis that results in increased liver damage.

Authors:  Robert J McKallip; Michael Fisher; Ursula Gunthert; Andras K Szakal; Prakash S Nagarkatti; Mitzi Nagarkatti
Journal:  Infect Immun       Date:  2005-01       Impact factor: 3.441

6.  Early gene expression changes induced by the bacterial superantigen staphylococcal enterotoxin B and its modulation by a proteasome inhibitor.

Authors:  Govindarajan Rajagopalan; Ashenafi Y Tilahun; Yan W Asmann; Chella S David
Journal:  Physiol Genomics       Date:  2009-03-31       Impact factor: 3.107

7.  Natural indoles, indole-3-carbinol and 3,3'-diindolymethane, inhibit T cell activation by staphylococcal enterotoxin B through epigenetic regulation involving HDAC expression.

Authors:  Philip B Busbee; Mitzi Nagarkatti; Prakash S Nagarkatti
Journal:  Toxicol Appl Pharmacol       Date:  2013-11-05       Impact factor: 4.219

Review 8.  Potent Neutralization of Staphylococcal Enterotoxin B In Vivo by Antibodies that Block Binding to the T-Cell Receptor.

Authors:  Gang Chen; Hatice Karauzum; Hua Long; Danielle Carranza; Frederick W Holtsberg; Katie A Howell; Laura Abaandou; Bojie Zhang; Nick Jarvik; Wei Ye; Grant C Liao; Michael L Gross; Daisy W Leung; Gaya K Amarasinghe; M Javad Aman; Sachdev S Sidhu
Journal:  J Mol Biol       Date:  2019-03-27       Impact factor: 5.469

9.  Rapamycin protects mice from staphylococcal enterotoxin B-induced toxic shock and blocks cytokine release in vitro and in vivo.

Authors:  Teresa Krakauer; Marilyn Buckley; Haleem J Issaq; Stephen D Fox
Journal:  Antimicrob Agents Chemother       Date:  2010-01-19       Impact factor: 5.191

10.  Proinflammatory mediators of toxic shock and their correlation to lethality.

Authors:  Teresa Krakauer; Marilyn J Buckley; Diana Fisher
Journal:  Mediators Inflamm       Date:  2010-06-16       Impact factor: 4.711

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