Skip to main content Accessibility help
×
Hostname: page-component-cd9895bd7-p9bg8 Total loading time: 0 Render date: 2024-12-22T18:51:55.605Z Has data issue: false hasContentIssue false

1 - Toxins and the interaction between bacterium and host

Published online by Cambridge University Press:  15 September 2009

Alistair J Lax
Affiliation:
Department of Microbiology, Dental Institute, King's College London
Alistair J. Lax
Affiliation:
King's College London
Get access

Summary

The concept of a bacterial protein toxin was born in the 1880s as Friedrich Loeffler in Berlin, and Émile Roux and Alexandre Yersin in Paris, puzzled over the disease diphtheria. The bacteria were localised in the throats of patients and experimental animals, yet the disease caused systemic damage throughout the body. They reasoned that the bacteria must be producing a poison that could escape from the bacteria to cause widespread damage to the host. So the toxin concept was established right at the start of Medical Microbiology (Roux and Yersin, 1888), only a decade after Robert Koch had established the first definite link between a bacterium and disease with his seminal work on anthrax. However, it was only from the mid-twentieth century onwards that the action of any toxin was understood at the molecular level. Since then progress has been rapid, not only in our appreciation of the mode of action of historically known toxins but also in the discovery of new toxins with novel means of attacking cells.

CLASSES OF BACTERIAL PROTEIN TOXINS

The first toxin to be understood at the molecular level was one from Clostridium perfringens, a bacterium notorious for causing wound infections such as gas gangrene. This toxin is a phospholipase that attacks membranes of cells and, thus, it defined one of the three main categories of toxins, i.e., those that attack membranes (MacFarlane and Knight, 1941).

Type
Chapter
Information
Bacterial Protein Toxins
Role in the Interference with Cell Growth Regulation
, pp. 1 - 6
Publisher: Cambridge University Press
Print publication year: 2005

Access options

Get access to the full version of this content by using one of the access options below. (Log in options will check for institutional or personal access. Content may require purchase if you do not have access.)

References

Albert, P R and Robillard, L (2002). G protein specificity: Traffic direction required. Cell. Signal., 14, 407–418CrossRefGoogle ScholarPubMed
Cornelis, G R and Gijsegem, F (2000). Assembly and function of type III secretory systems. Annu. Rev. Microbiol., 54, 735–774CrossRefGoogle ScholarPubMed
Ding, Z Y, Atmakuri, K, and Christie, P J (2003). The outs and ins of bacterial type IV secretion substrates. Trends Microbiol., 11, 527–535CrossRefGoogle ScholarPubMed
Fiorentini, C, Gauthier, N, Donelli, G, and Boquet, P (1998). Bacterial toxins and the Rho GTP-binding protein: What microbes teach us about cell regulation. Cell Death Differ., 5, 720–728CrossRefGoogle ScholarPubMed
Guldi-Rontani, C and Mock, M (2002). Macrophage interactions. Curr. Top. Microbiol., 271, 115–141Google Scholar
Lax, A J and Thomas, W (2002). How bacteria could cause cancer – one step at a time. Trends Microbiol., 10, 293–299CrossRefGoogle ScholarPubMed
MacFarlane, M G and Knight, B C J G (1941). The biochemistry of bacterial toxins: The lecithinase activity of Cl. welchii toxins. Biochem. J., 35, 884–902CrossRefGoogle ScholarPubMed
Montecucco, C, Papini, E, and Schiavo, G (1994). Bacterial protein toxins penetrate cells via a four-step mechanism. FEBS Lett., 346, 92–98CrossRefGoogle Scholar
Oxford, G and Theodorescu, D (2003). Ras superefmily monomeric G proteins in carcinoma cell motility. Cancer Lett., 189, 117–128CrossRefGoogle ScholarPubMed
Parsonnet, J, Friedman, G D, Vandersteen, D P, Chang, Y, Vogelman, J H, Orentreich, N, and Sibley, R K (1991). Helicobacter pylori infection and the risk of gastric carcinoma. New Engl. J Med., 325, 1127–1131CrossRefGoogle ScholarPubMed
Roux, E Jr and Yersin, A (1888). Contribution a l'étude de la diphtherie. Ann. Inst. Pasteur, 2, 620–629Google Scholar
Vaandrager, A B, Wiel, E, Hom, M L, Luthjens, L H, and Jonge, H R (1992). Heat-stable enterotoxin receptor/guanylyl cyclase C is an oligomer consisting of functionally distinct subunits, which are non-covalently linked in the intestine. J. Biol. Chem., 269, 16409–16415Google Scholar
Yamaizumi, M, Mekada, E, Uchida, T, and Okada, Y (1978). One molecule of diphtheria-toxin fragment A introduced into a cell can kill cell. Cell, 15, 245–250CrossRefGoogle Scholar

Save book to Kindle

To save this book to your Kindle, first ensure [email protected] is added to your Approved Personal Document E-mail List under your Personal Document Settings on the Manage Your Content and Devices page of your Amazon account. Then enter the ‘name’ part of your Kindle email address below. Find out more about saving to your Kindle.

Note you can select to save to either the @free.kindle.com or @kindle.com variations. ‘@free.kindle.com’ emails are free but can only be saved to your device when it is connected to wi-fi. ‘@kindle.com’ emails can be delivered even when you are not connected to wi-fi, but note that service fees apply.

Find out more about the Kindle Personal Document Service.

Available formats
×

Save book to Dropbox

To save content items to your account, please confirm that you agree to abide by our usage policies. If this is the first time you use this feature, you will be asked to authorise Cambridge Core to connect with your account. Find out more about saving content to Dropbox.

Available formats
×

Save book to Google Drive

To save content items to your account, please confirm that you agree to abide by our usage policies. If this is the first time you use this feature, you will be asked to authorise Cambridge Core to connect with your account. Find out more about saving content to Google Drive.

Available formats
×