Aerolysin - A paradigm for membrane insertion of beta-sheet protein toxins?

Journal of Structural Biology

Volumn 121, Issue 2, 1998, Pages 92-100

  Rossjohn, Jamie ^a   Feil, Susanne C ^a   McKinstry, William J ^a   Tsernoglou, Demetrius ^b   Van Der Goot, Gisou ^c   Buckley, J Thomas ^d   Parker, Michael W ^a  

^a ST VINCENT'S INSTITUTE OF MEDICAL RESEARCH   (Australia)

^b SAPIENZA UNIVERSITY OF ROME   (Italy)

^c UNIVERSITY OF GENEVA   (Switzerland)

^d UNIVERSITY OF VICTORIA   (Canada)

Author keywords

Aerolysin; Membrane channels; Membrane insertion; Protein toxins; X ray crystallography

Indexed keywords

AEROLYSIN; BACTERIAL TOXIN; DIMER; MUTANT PROTEIN; PERTUSSIS TOXIN; UNCLASSIFIED DRUG;

AEROMONAS; ARTICLE; CLOSTRIDIUM SEPTICUM; CRYSTALLOGRAPHY; DIMERIZATION; MEMBRANE CHANNEL; NONHUMAN; OLIGOMERIZATION; PRIORITY JOURNAL; PROTEIN DOMAIN; PROTEIN STRUCTURE; RECEPTOR BINDING;

EID: 0031829174     PISSN: 10478477     EISSN: None     Source Type: Journal    
DOI: 10.1006/jsbi.1997.3947     Document Type: Article

References (33)

1. Altwegg M., Geiss H. K. Aeromonas. CRC Crit. Rev. Microbiol. 16:1989;253-286.
2. Ballard J., Crabtree J., Roe B. A., Tweten R. K. The primary structure ofClostridium septicumAeromonas hydrophila. Infect. Immun. 63:1995;340-344.
3. Ballard J., Sokolov Y., Yuan W.-L., Kagan B. L., Tweten R. K. Activation and mechanism ofClostridium septicum. Mol. Microbiol. 10:1993;627-634.
4. Bennett M. J., Choe S., Eisenberg D. Domain swapping: Entangling alliances between proteins. Proc. Natl. Acad. Sci. USA. 91:1994;3127-3131.
5. Buckley J. T., Wilmsen H-U., Lesieur C., Schulze A., Pattus F., Parker M. W., van der Goot F. Protonation of histidine-132 promotes oligomerization of the channel-forming toxin aerolysin. Biochemistry. 34:1995;16450-16455.
6. Cabiaux V., Buckley J. T., Wattiez R., Ruysschaert J.-M., Parker M. W., van der Goot F. G. Conformational changes in aerolysin during the transition from the water-soluble protoxin to the membrane channel. Biochemistry. 36:1997;15224-15232.
7. Cowan S. W., Schirmer T., Rummel G., Steiert M., Ghosh R., Pauptit R. A., Jansonius J. N., Rosenbusch J. Crystal structures explain functional properties of twoE. coli. Nature. 358:1992;727-733.
8. Cowell S., Aschauer W., Gruber H. J., Nelson K. L., Buckley J. T. The erythrocyte receptor for the channel-forming toxin aerolysin is a novel glycosylphosphatidylinositol-anchored protein. Mol. Microbiol. 25:1997;343-350.
9. Garland W. J., Buckley J. T. The cytolytic toxin aerolysin must aggregate to disrupt erythrocytes, and aggregation is stimulated by human glycophorin. Infect. Immun. 56:1988;1249-1253.
10. Gouaux E. Channel-forming toxins: Tales of transformation. Curr. Opin. Struct. Biol. 7:1997;566-573.
11. Green M. J., Buckley J. T. Site-directed mutagenesis of the hole-forming toxin aerolysin: Studies on the role of histidines in receptor binding and oligomerization of the monomer. Biochemistry. 29:1990;2177-2180.
12. Gruber H. J., Wilmsen H. U., Cowell S., Schindler H., Buckley J. T. Partial purification of the rat erythrocyte receptor for the channel-forming toxin aerolysin and reconstitution into planar lipid bilayers. Mol. Microbiol. 14:1994;1093-1011.
13. Heringa J., Taylor W. R. Three-dimensional domain duplication, swapping and stealing. Curr. Opin. Struct. Biol. 7:1997;416-421.
14. Howard S. P., Garland W. J., Green M. J., Buckley J. T. Nucleotide sequence of the gene for the hole-forming toxin aerolysin ofAeromonas hydrophila. J. Bacteriol. 169:1987;2869-2871.
15. Janda J. M., Duffey P. S. Mesophilic aeromonads in human disease: Current taxonomy, laboratory identification and infectious disease spectrum. Rev. Infect. Dis. 10:1988;980-997.
16. Kraulis P. J. MOLSCRIPT: A program to produce both detailed and schematic plots of protein structures. J. Appl. Crystallogr. 24:1991;946-950.
17. Li J., Koni P. A., Ellar D. J. Structure of the mosquitocidal δ-endotoxin CytB fromBacillus thuringiensiskyushuensis. J. Mol. Biol. 257:1996;129-152.
18. Nelson K. L., Raja S. M., Buckley J. T. The GPI-anchored surface glycoprotein Thy-1 is a receptor for the channel-forming toxin aerolysin. J. Biol. Chem. 272:1997;12170-12174.
19. Parker M. W. More than one way to make a hole. Nature Struct. Biol. 4:1997;250-253.
20. Parker M. W., Buckley J. T., Postma J. P. M., Tucker A. D., Leonard K., Pattus F., Tsernoglou D. Structure of theAeromonas. Nature. 367:1994;292-295.
21. Parker M. W., van der Goot F. G., Buckley J. T. Aerolysin - The ins and outs of a prototypical channel-forming toxin. Mol. Microbiol. 19:1996;205-212.
22. Petosa C., Collier R. J., Klimpel K. R., Leppla S. H., Liddington R. C. Crystal structure of the anthrax toxin protective antigen. Nature. 385:1997;833-838.
23. Rossjohn J., Buckley J. T., Hazes B., Murzin A. G., Read R. J., Parker M. W. Aerolysin and pertussis toxin share a common receptor-binding domain. EMBO J. 16:1997a;3426-3434.
24. Rossjohn J., Feil S. C., McKinstry W. J., Tweten R. K., Parker M. W. Structure of a cholesterol-binding, thiol-activated cytolysin and a model of its membrane form. Cell. 89:1997b;685-692.
25. Song L., Hobaugh M. R., Shustak C., Cheley S., Bayley H., Gouaux J. E. Structure of staphyloccal α-hemolysin, a heptameric transmembrane pore. Science. 274:1996;1859-1866.
26. Sousa M. V., Richardson M., Fontes W., Morhy L. Homology between the seed cytolysin enterolobin and bacterial aerolysins. J. Prot. Chem. 13:1994;659-667.
27. van der Goot F. G., Lakey J., Pattus F., Kay C. M., Sorokine O., Van Dorsselaer A., Buckley J. T. Spectroscopic study of the activation and oligomerization of the channel-forming toxin aerolysin: Identification of the site of proteolytic activation. Biochemistry. 31:1992;8566-8570.
28. van der Goot F. G., Ausio J., Wong K. R., Pattus F., Buckley J. T. Dimerization stabilizes the pore-forming toxin aerolysin in solution. J. Biol. Chem. 268:1993a;18272-18279.
29. van der Goot F. G., Pattus F., Wong K. R., Buckley J. T. Oligomerization of the channel-forming toxin aerolysin precedes insertion into lipid bilayers. Biochemistry. 32:1993b;2636-2642.
30. Wiener M., Freymann D., Ghosh P., Stroud R. M. Crystal structure of colicin Ia. Nature. 385:1997;461-464.
31. Weiss M. S., Abele U., Weckesser J., Welte W., Schiltz E., Schulz G. E. Molecular architecture and electrostatic properties of a bacterial porin. Science. 254:1991;1627-1630.
32. Wilmsen H-U., Leonard K., Tichelaar W., Buckley J. T., Pattus F. The aerolysin membrane channel is formed by heptamerization of the monomer. EMBO J. 11:1992;2457-2463.
33. Wong K. R., Buckley J. T. Site-directed mutagenesis of a single tryptophan near the middle of the channel-forming toxin aerolysin inhibits its transfer across the outer membrane ofAeromonas salmonicida. J. Biol. Chem. 266:1991;14451-14456.