1887

Chapter 22 : Unorthodox Secretion by Gram-Negative Bacteria

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

Unorthodox Secretion by Gram-Negative Bacteria, Page 1 of 2

| /docserver/preview/fulltext/10.1128/9781555818340/9781555810825_Chap22-1.gif /docserver/preview/fulltext/10.1128/9781555818340/9781555810825_Chap22-2.gif

Abstract:

This chapter discusses the architecture of the gram-negative bacterial cell and several solutions to the gram-negative secretion dilemma. Gram-negative bacteria enjoy the protection of the outer membrane; however, it does not come without a price. Secretion across two membranes is more than twice the challenge faced by single-membrane cells. DNA is transferred in the case of the T-DNA of and the P conjugation pathway. Protein secretion pathways that use the PulE homologs include those that secrete pertussis toxin and cholera toxin. has evolved numerous pathways for the secretion of its virulence factors. Each of the five pertussis toxin subunits is encoded by a separate gene, and each has an N-terminal secretion signal sequence that is proteolytically processed and absent from the mature toxin. Pertussis toxin is synthesized and accumulated in the cells late in the growth cycle, first appearing after about 20 h in culture. Current efforts in the laboratory are aimed at testing the membrane fusion hypothesis and understanding how the seven Ptl subunits perform the secretion functions.

Citation: Weiss A. 1994. Unorthodox Secretion by Gram-Negative Bacteria, p 341-349. In Miller V, Kaper J, Portnoy D, Isberg R (ed), Molecular Genetics of Bacterial Pathogenesis. ASM Press, Washington, DC. doi: 10.1128/9781555818340.ch22

Key Concept Ranking

Bacterial Pathogenesis
0.5946303
Adenylate Cyclase Toxin
0.53426117
0.5946303
Highlighted Text: Show | Hide
Loading full text...

Full text loading...

Figures

Image of Figure 1
Figure 1

Examples of protein secretion mechanisms in gram-negative bacteria. (A) Sec-mediated secretion results in deposition of the protein in the periplasmic space. For a protein containing a secretion signal to be exported past the outer membrane, a second secretion mechanism must be employed, as shown on the right. Examples of this are discussed in the text. (B) Sec-independent secretion can occur by a process that does not involve a periplasmic intermediate. Examples are the hemolysin (see chapter 23) and the adenylate cyclase toxin.

Citation: Weiss A. 1994. Unorthodox Secretion by Gram-Negative Bacteria, p 341-349. In Miller V, Kaper J, Portnoy D, Isberg R (ed), Molecular Genetics of Bacterial Pathogenesis. ASM Press, Washington, DC. doi: 10.1128/9781555818340.ch22
Permissions and Reprints Request Permissions
Download as Powerpoint
Image of Figure 2
Figure 2

The scrabble family of secretion proteins of gram-negative bacteria. The proteins required for pullulanase (Pul) synthesis, maturation, and secretion are shown from top to bottom. The Ysc secretion pathway of spp. and the Mxi pathway of spp. ( ) have homologs only to the PulD protein ( ). The Ptl secretion pathway for pertussis toxin ( ) and the VirB operon required for T-DNA transfer by have homologs only to the PulE protein ( ).

Citation: Weiss A. 1994. Unorthodox Secretion by Gram-Negative Bacteria, p 341-349. In Miller V, Kaper J, Portnoy D, Isberg R (ed), Molecular Genetics of Bacterial Pathogenesis. ASM Press, Washington, DC. doi: 10.1128/9781555818340.ch22
Permissions and Reprints Request Permissions
Download as Powerpoint
Image of Figure 3
Figure 3

Comparison of the Ptl operon with the VirB operon. The 12-kb chromosomal region of the -encoding pertussis toxin structural genes (denoted S1 to S5) and the closely linked secretion genes (denoted B to H) are shown on the top line. The proteins with a secretion signal are denoted by the shaded region at the start. The homologs and the percent identity with the genes are shown below. , , and are all homologous to , and the percent identities are given.

Citation: Weiss A. 1994. Unorthodox Secretion by Gram-Negative Bacteria, p 341-349. In Miller V, Kaper J, Portnoy D, Isberg R (ed), Molecular Genetics of Bacterial Pathogenesis. ASM Press, Washington, DC. doi: 10.1128/9781555818340.ch22
Permissions and Reprints Request Permissions
Download as Powerpoint
Image of Figure 4
Figure 4

Steps required for proper pertussis toxin (PT) assembly and secretion. The proposed locations of the Ptl proteins B to G are based on the predicted amino acid sequence.

Citation: Weiss A. 1994. Unorthodox Secretion by Gram-Negative Bacteria, p 341-349. In Miller V, Kaper J, Portnoy D, Isberg R (ed), Molecular Genetics of Bacterial Pathogenesis. ASM Press, Washington, DC. doi: 10.1128/9781555818340.ch22
Permissions and Reprints Request Permissions
Download as Powerpoint
Image of Figure 5
Figure 5

Proposed model of pertussis toxin (PT) secretion via a membrane fusion mechanism. For clarity, only two Ptl proteins are shown, but one could envision a secretion compartment formed by a complex of proteins on the inner membrane (IM) and outer membrane (OM). (A) Accumulation and assembly of pertussis toxin subunits occur in the periplasmic space at early times in the cell cycle. (B) Secretion occurs by a fusion mechanism in the late stationary phase.

Citation: Weiss A. 1994. Unorthodox Secretion by Gram-Negative Bacteria, p 341-349. In Miller V, Kaper J, Portnoy D, Isberg R (ed), Molecular Genetics of Bacterial Pathogenesis. ASM Press, Washington, DC. doi: 10.1128/9781555818340.ch22
Permissions and Reprints Request Permissions
Download as Powerpoint

References

/content/book/10.1128/9781555818340.chap22
1. Allaoui, A.,, P. J. Sansonetti,, and C. Parsot. 1993. MxiD, an outer membrane protein necessary for the secretion of the Shigella flexneri Ipa invasins. Mol. Microbiol. 7:5968.
2. Burnette, W. N.,, J. L. Arciniega,, V. L. Mar,, and D. L. Burns. 1992. Properties of pertussis toxin B oligomer assembled in vitro from recombinant polypeptide produced by Escherichia coli. Infect. Immun. 60:22522256.
3. Das, A. 1998. Agrobacterium tumefaciens virE operon encodes a single-stranded DNA-binding protein. Proc. Natl. Acad. Sci. USA 85:29022913.
4. Goodwin, M. S. M.,, and A. A. Weiss. 1990. Adenylate cyclase toxin is critical for bacterial colonization and pertussis toxin is critical for lethal infection by Bordetella pertussis in infant mice. Infect. Immun. 58:34453447.
5. Hancock, R. E. W. 1991. Bacterial outer membranes: evolving concepts. ASM News 57:1751182.
6. Johansson, M.,, I. Nilsson,, and G. von Hetfne. 1993. Positively charged amino acids placed next to a signal sequence block protein translocation more efficiently in Escherichia coli than in mammalian microsomes. Mol. Gen. Genet. 239:251256.
7. Katada, T.,, and M. Ui. 1982. Direct modification of the membrane adenylate cyclase system by islet-activation protein due to ADP-ribosylation of a membrane protein. Proc. Natl. Acad. Sci. USA 79:31293133.
8. Klauser, T.,, J. Pohlner,, and T. F. Meyer. 1993. The secretion pathway of IgA protease-type proteins in gram-negative bacteria. BioEssays 15:799805.
9. Kuldau, G. A.,, G. De Vos,, J. Owen,, G. McCaffrey,, and P. Zambryski. 1990. The virB operon of Agrobacterium tumefaciens pTiC58 encodes 11 open reading frames. Mol. Gen. Genet. 221: 256266.
10. Lessl, M.,, D. Balzer,, and E. Lanka. 1992. Relationship of DNA-transfer-systems: essential factors of plasmids RP4, Ti and F share common sequences. Nucleic Acids Res. 20:60996100.
11. Lessl, M.,, D. Balzer,, W. Pansegrau,, and E. Lanka. 1992. Sequence similarities between the RP4 Tra2 and the Ti VirB region strongly support the conjugation model for T-DNA transfer. J. Biol. Chem. 267:2047120480.
12. Melton, A. R.,, and A. A. Weiss. 1989. Environmental regulation of expression of virulence determinants in Bordetella pertussis. J. Bacteriol. 171:62066212.
13. Melton, A. R.,, and A. A. Weiss. 1993. Characterization of enviromental regulators of Bordetella pertussis. Infect. Immun. 61:807815.
14. Motallebi-Veshareh, M.,, D. Balzar,, E. Lanka,, G. Jagura-Burdzy,, and C. M. Thomas. 1992. Conjugative transfer functions of broad-host-range plasmid RK2 are coregulated with vegetative replication. Mol. Microbiol. 6:907920.
15. Nencioni, L.,, M. Pizza,, G. Volpini,, M. T. de Magistris,, F. Giovannoni,, and R. Rappuoli. 1991. Properties of the B oligomer of pertussis toxin. Infect. Immun. 59:47324734.
16. Nicosia, A.,, M. Perugini,, C. Franzini,, M. C. Casagli,, M. G. Borri,, G. Antoni,, M. Almoni,, P. Neri,, G. Ratti,, and R. Rappuoli. 1986. Cloning and sequencing of the pertussis toxin genes: operon structure and gene duplication. Proc. Natl. Acad. Sci. USA 83:43614635.
17. Pizza, M.,, M. Bugnoli,, R. Manetti,, A. Covacci,, and R. Rappuoli. 1990. The subunit S1 important for pertussis toxin secretion. J. Biol. Chem. 265:1775917763.
18. Pugsley, A. P. 1993. The complete general secretory pathway in gram-negative bacteria. Microbiol. Rev. 57:50108.
19. Pugsley, A. P.,, C. d'Enfert,, I. Reyss,, and M. G. Kornacker. 1990. Genetics of extracellular protein secretion by gram-negative bacteria. Annu. Rev. Genet. 24:6790.
20. Sandkvist, M.,, V. Morales,, and M. Bagdasarian. 1993. A protein required for secretion of cholera toxin through the outer membrane of Vibrio cholerae. Gene 123:8186.
21. Schatz, P. J.,, and J. Beckwith. 1990. Genetic analysis of protein export in Escherichia coli. Annu. Rev. Genet. 24:215248.
22. Shirasn, K.,, Z. Koukolikova-Nicola,, B. Hohn,, and C. I. Kato. 1994. An inner-membrane-associated virulence protein essential for T-DNA transfer from Agrobacterium tumefaciens to plants exhibits ATPase activity and similarities to conjugative transfer genes. Mol. Microbiol. 11:581588.
23. Stein, P. E.,, A. Boodhoo,, G. D. Armstrong,, S. A. Cockle,, M. H. Klein,, and R. J. Read. 1994. The crystal structure of pertussis toxin. Structure 2:4557.
24. Stevens, C. F. 1993. Quantal release of neurotransmitter and long-term potentiation. Cell 72:5563.
25. Taylor, P. W. 1992. Complement-mediated killing of susceptible gram-negative bacteria: an elusive mechanism. Exp. Clin. Immunogenet. 9:4856.
26. Thorstenson, Y. R.,, G. A. Kuldau,, and P. C. Zambryski. 1993. Subcellular localization of seven VirB proteins of Agrobacterium tumefaciens: implications for the formation of a T-DNA transport structure. J. Bacteriol. 175:52335241.
27. Ward, J. E., Jr.,, E. M. Dale,, P. J. Christie,, E. W. Nester,, and A. N. Binns. 1990. Complementation analysis of Agrobacterium tumefaciens Ti plasmid virB genes by use of a vir promoter expression vector: virB9, virB10, and virB11 are essential virulence genes. J. Bacteriol. 172:51875199.
28. Weiss, A. A.,, and E. L. Hewlett. 1986. Virulence factors of Bordetella pertussis. Annu. Rev. Microbiol. 40:661686.
29. Weiss, A. A.,, F. D. Johnson,, and D. L. Burns. 1993. Molecular characterization of an operon required for pertussis toxin secretion. Proc. Natl. Acad. Sci. USA 90:29702974.
30. Whitchurch, C. B.,, M. Hobbs,, S. P. Livingston,, V. Krishnapillai,, and J. S. Mattick. 1990. Characterization of a Pseudomonas aeruginosa twitching motility gene and evidence for a specialised protein export system widespread in eubacteria. Gene 101:3344.
31. Wickner, W.,, A. J. M. Driessen,, and F. U. Hartl. 1991. The enzymology of protein translocation across the Escherichia coli plasma membrane. Annu. Rev. Biochem. 60:101124.
32. Willems, R. J.,, L. C., Geuijen,, H. G. J. van der Heide,, G. Renauld,, P. Bertin,, W. M. R. van den Akker,, C. Locht,, and F. R. Mooi. 1994. Mutational analysis of the Bordetella pertussis flm/fha gene cluster: identification of a gene with sequence similarities to haemolysin accessory genes involved in export of FHA. Mol. Microbiol. 11:337347.

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