1887

Chapter 10 : Direct Penetration of Bacterial Toxins across the Plasma Membrane

MyBook is a cheap paperback edition of the original book and will be sold at uniform, low price.

Ebook: Choose a downloadable PDF or ePub file. Chapter is a downloadable PDF file. File must be downloaded within 48 hours of purchase

Buy this Chapter
Digital (?) $15.00

Preview this chapter:
Zoom in
Zoomout

Direct Penetration of Bacterial Toxins across the Plasma Membrane, Page 1 of 2

| /docserver/preview/fulltext/10.1128/9781555817893/9781555812454_Chap10-1.gif /docserver/preview/fulltext/10.1128/9781555817893/9781555812454_Chap10-2.gif

Abstract:

Adenylate (or adenylyl) cyclase (AC) toxin is an essential virulence factor for , as mutants lacking this molecule are virtually avirulent in an animal infection model. Receptor-mediated endocytosis (RME) is characterized by several features that can be used to determine whether a particular toxin is entering by that pathway. First, it is generally true that ligand binding can occur at 4 and 37°C, but internalization only occurs at 37°C. Second, binding is saturable and limited by the number of receptor molecules on the target cell. Third, toxins that enter target cells by RME exhibit a lag phase between toxin addition and biological effects, due to the time necessary for uptake into an endosome, acidification of the endosome, and resultant translocation of the catalytic portion into the cytoplasm. All toxins that act on intracellular targets must have a mechanism by which at least a part of their structure can traverse the plasma membrane of the host cell. Divalent metal binding to AC toxin and the membrane potential of the target cell are clearly critical factors in the processes of insertion and translocation of the toxin, but the signals that initiate this sequence of events from the cell surface remain unknown. Most of the understanding of the structure and function of AC toxin comes from work utilizing soluble material obtained by urea extraction of organisms or recombinant expressing AC toxin. Infection with is not systemic; organisms remain localized to the respiratory mucosa.

Citation: Zaretzky F, Gray M, Hewlett E. 2003. Direct Penetration of Bacterial Toxins across the Plasma Membrane, p 149-156. In Burns D, Barbieri J, Iglewski B, Rappuoli R (ed), Bacterial Protein Toxins. ASM Press, Washington, DC. doi: 10.1128/9781555817893.ch10

Key Concept Ranking

Major Histocompatibility Complex Class I
0.41886914
0.41886914
Highlighted Text: Show | Hide
Loading full text...

Full text loading...

Figures

Image of Figure 1
Figure 1

Domain structure of AC toxin and description of domain-associated activities.

Citation: Zaretzky F, Gray M, Hewlett E. 2003. Direct Penetration of Bacterial Toxins across the Plasma Membrane, p 149-156. In Burns D, Barbieri J, Iglewski B, Rappuoli R (ed), Bacterial Protein Toxins. ASM Press, Washington, DC. doi: 10.1128/9781555817893.ch10
Permissions and Reprints Request Permissions
Download as Powerpoint
Image of Figure 2
Figure 2

Characteristics of the functional activities of AC toxin.

Citation: Zaretzky F, Gray M, Hewlett E. 2003. Direct Penetration of Bacterial Toxins across the Plasma Membrane, p 149-156. In Burns D, Barbieri J, Iglewski B, Rappuoli R (ed), Bacterial Protein Toxins. ASM Press, Washington, DC. doi: 10.1128/9781555817893.ch10
Permissions and Reprints Request Permissions
Download as Powerpoint
Image of Figure 3
Figure 3

AC toxin is delivered by adherent (A) to human monocytes and following phagocytosis (B) by these cells.

Citation: Zaretzky F, Gray M, Hewlett E. 2003. Direct Penetration of Bacterial Toxins across the Plasma Membrane, p 149-156. In Burns D, Barbieri J, Iglewski B, Rappuoli R (ed), Bacterial Protein Toxins. ASM Press, Washington, DC. doi: 10.1128/9781555817893.ch10
Permissions and Reprints Request Permissions
Download as Powerpoint

References

/content/book/10.1128/9781555817893.chap10
1. Confer, D. L.,, and J. W. Eaton. 1982. Phagocyte impotence caused by an invasive bacterial adenylate cyclase. Science 217:948950.
2. Gordon, V. M.,, S. H. Leppla,, and E. L. Hewlett. 1988. Inhibitors of receptor-mediated endocytosis block the entry of Bacillus anthracis adenylate cyclase toxin but not that of Bordetella pertussis adenylate cyclase toxin. Infect. Immun. 56:10661069.
3. Gray, M.,, G. Szabo,, A. S. Otero,, L. Gray,, and E. Hewlett. 1998. Distinct mechanisms for K+ efflux, intoxication, and hemolysis by Bordetella pertussis AC toxin. J. Biol. Chem. 273:1826018267.
4. Guermonprez, P.,, N. Khelef,, E. Blouin,, P. Rieu,, P. Ricciardi-Castagnoli,, N. Guiso,, D. Ladant,, and C. Leclerc. 2001. The adenylate cyclase toxin of Bordetella pertussis binds to target cells via the aMb2 integrin (CD11b/CD18). J. Exp. Med. 193:10351044.
5. Karimova, G.,, C. Fayolle,, S. Gmira,, A. Ullmann,, C. Leclerc,, and D. Ladant. 1998. Charge-dependent translocation of Bordetella pertussis adenylate cyclase toxin into eukaryotic cells: implication for the in vivo delivery of CD8+ T cell epitopes into antigenpresenting cells. Proc. Natl. Acad. Sci. USA 95:1253212537.
6. Lenz, D. H.,, C. L. Weingart,, and A. A. Weiss. 2000. Phagocytosed Bordetella pertussis fails to survive in human neutrophils. Infect. Immun. 68:956959.
7. Otero, A. S.,, X. B. Yi,, M. C. Gray,, G. Szabo,, and E. L. Hewlett. 1995. Membrane depolarization prevents cell invasion by Bordetella pertussis adenylate cyclase toxin. J. Biol. Chem. 270:96959697.
8. Weingart, C. L.,, P. S. Mobberley-Schuman,, E. L. Hewlett,, M. C. Gray,, and A. A. Weiss. 2000. Neutralizing antibodies to adenylate cyclase toxin promote phagocytosis of Bordetella pertussis by human neutrophils. Infect. Immun. 68:71527155.
1. Hewlett, E. L.,, and M. C. Gray,. 2000. Adenylyl-cyclase toxin from Bordetella pertussis, p. 473488. In K. Aktories, and I. Just (ed.), Bacterial Protein Toxins. Springer-Verlag, Berlin, Germany.
2. Ladant, D.,, and A. Ullmann. 1999. Bordetella pertussis adenylate cyclase: a toxin with multiple talents. Trends Microbiol. 7:172176.
3. Rappuoli, R.,, and M. Pizza,. 2000. Bacterial toxins, p. 19342202. In P. Cossart,, P. Boquet,, S. Normark,, and R. Rappuoli (ed.), Cellular Microbiology. ASM Press, Washington, D.C. 270:96959697.

This is a required field
Please enter a valid email address
Please check the format of the address you have entered.
Approval was a Success
Invalid data
An Error Occurred
Approval was partially successful, following selected items could not be processed due to error