Size and dynamics of the vibrio cholerae porins OmpU and OmpT probed by polymer exclusion

Biophysical Journal

Volumn 98, Issue 9, 2010, Pages 1820-1829

  Duret, Guillaume ^a,b   Delcour, Anne H ^a  

^a University of Houston   (United States)

^b INSTITUT PASTEUR   (France)

Author keywords

[No Author keywords available]

Indexed keywords

VIBRIO CHOLERAE;

EID: 77952259198     PISSN: 00063495     EISSN: 15420086     Source Type: Journal    
DOI: 10.1016/j.bpj.2010.01.010     Document Type: Article

References (35)

1. Benz, R., K. Janko, P. Läuger. 1978. Formation of large, ionpermeable membrane channels by the matrix protein (porin) of Escherichia coli. Biochim. Biophys. Acta. 511:305-319.
2. Schindler, H., and J. P. Rosenbusch. 1978. Matrix protein from Escherichia coli outer membranes forms voltage-controlled channels in lipid bilayers. Proc. Natl. Acad. Sci. USA. 75:3751-3755.
3. Delcour, A. H. 2003. Solute uptake through general porins. Front. Biosci. 8:d1055-d1071.
4. Nikaido, H. 2003. Molecular basis of bacterial outer membrane permeability revisited. Microbiol. Mol. Biol. Rev. 67:593-656.
5. Baslé, A., G. Rummel, T. Schirmer. 2006. Crystal structure of osmoporin OmpC from E. coli at 2.0 Å. J. Mol. Biol. 362:933-942.
6. Cowan, S. W., T. Schirmer, J. P. Rosenbusch. 1992. Crystal structures explain functional properties of two E. coli porins. Nature. 358:727-733.
7. Provenzano, D., and K. E. Klose. 2000. Altered expression of the ToxR-regulated porins OmpU and OmpT diminishes Vibrio cholerae bile resistance, virulence factor expression, and intestinal colonization. Proc. Natl. Acad. Sci. USA. 97:10220-10224.
8. Provenzano, D., C. M. Lauriano, and K. E. Klose. 2001. Characterization of the role of the ToxR-modulated outer membrane porins OmpU and OmpT in Vibrio cholerae virulence. J. Bacteriol. 183: 3652-3662. (Pubitemid 32510434)
9. Klose, K. E. 2001. Regulation of virulence in Vibrio cholerae. Int. J. Med. Microbiol. 291:81-88.
10. Duret, G., and A. H. Delcour. 2006. Deoxycholic acid blocks Vibrio cholerae OmpT but not OmpU porin. J. Biol. Chem. 281: 19899-19905.
11. Wibbenmeyer, J. A., D. Provenzano, A. H. Delcour. 2002. Vibrio cholerae OmpU and OmpT porins are differentially affected by bile. Infect. Immun. 70:121-126.
12. Chakrabarti,S.R.,K.Chaudhuri,J.Das.1996.PorinsofVibriocholerae: purificationandcharacterizationofOmpU.J.Bacteriol.178:524-530. (Pubitemid26030608)
13. Duret, G., V. Simonet, and A. H. Delcour. 2007. Modulation of Vibrio cholerae porin function by acidic pH. Channels (Austin). 1:70-79.
14. Baslé, A., R. Iyer, and A. H. Delcour. 2004. Subconductance states in OmpF gating. Biochim. Biophys. Acta. 1664:100-107.
15. Baslé, A., R. Qutub, A. H. Delcour. 2004. Deletions of single extracellular loops affect pH sensitivity, but not voltage dependence, of the Escherichia coli porin OmpF. Protein Eng. Des. Sel. 17:665-672.
16. Liu, N., and A. H. Delcour. 1998. Inhibitory effect of acidic pH on OmpC porin: wild-type and mutant studies. FEBS Lett. 434:160-164. (Pubitemid 28404681)
17. Nestorovich, E. M., T. K. Rostovtseva, and S. M. Bezrukov. 2003. Residue ionization and ion transport through OmpF channels. Biophys. J. 85:3718-3729.
18. Todt, J. C., W. J. Rocque, and E. J. McGroarty. 1992. Effects of pH on bacterial porin function. Biochemistry. 31:10471-10478.
19. Simonet, V. C., A. Baslé, A. H. Delcour. 2003. The Vibrio cholerae porins OmpU and OmpT have distinct channel properties. J. Biol. Chem. 278:17539-17545.
20. Rostovtseva, T. K., E. M. Nestorovich, and S. M. Bezrukov. 2002. Partitioning of differently sized poly(ethylene glycol)s into OmpF porin. Biophys. J. 82:160-169.
21. Vodyanoy, I., and S. M. Bezrukov. 1992. Sizing of an ion pore by access resistance measurements. Biophys. J. 62:10-11.
22. Movileanu, L., and H. Bayley. 2001. Partitioning of a polymer into a nanoscopic protein pore obeys a simple scaling law. Proc. Natl. Acad. Sci. USA. 98:10137-10141.
23. Merzlyak, P. G., L. N. Yuldasheva, S. M. Bezrukov. 1999. Polymeric nonelectrolytes to probe pore geometry: application to the alpha-toxin transmembrane channel. Biophys. J. 77:3023-3033.
24. Carneiro, C. M., P. G. Merzlyak, O. V. Krasilnikov. 2003. Probing the volume changes during voltage gating of Porin 31BM channel with nonelectrolyte polymers. Biochim. Biophys. Acta. 1612:144-153.
25. Bezrukov, S. M., and I. Vodyanoy. 1993. Probing alamethicin channels with water-soluble polymers. Effect on conductance of channel states. Biophys. J. 64:16-25.
26. Stojilkovic, K. S., A. M. Berezhkovskii, S. M. Bezrukov. 2003. Conductivity and microviscosity of electrolyte solutions containing polyethylene glycols. J. Chem. Phys. 119:6973-6978.
27. Korchev, Y. E., C. L. Bashford, C. A. Pasternak. 1995. Low conductance states of a single ion channel are not 'closed'. J. Membr. Biol. 147:233-239.
28. Montal, M., and P. Mueller. 1972. Formation of bimolecular membranes from lipid monolayers and a study of their electrical properties. Proc. Natl. Acad. Sci. USA. 69:3561-3566.
29. Nestorovich, E. M., E. Sugawara, S. M. Bezrukov. 2006. Pseudomonas aeruginosa porin OprF: properties of the channel. J. Biol. Chem. 281:16230-16237.
30. Delcour, A. H., B. Martinac, C. Kung. 1989. Modified reconstitution method used in patch-clamp studies of Escherichia coli ion channels. Biophys. J. 56:631-636.
31. Lauman, B., M. Pagel, and A. H. Delcour. 2008. Altered pore properties and kinetic changes in mutants of the Vibrio cholerae porin OmpU. Mol. Membr. Biol. 25:498-505.
32. Danelon, C., E. M. Nestorovich, S. M. Bezrukov. 2006. Interaction of zwitterionic penicillins with the OmpF channel facilitates their translocation. Biophys. J. 90:1617-1627.
33. Koronakis, V., A. Sharff, C. Hughes. 2000. Crystal structure of the bacterial membrane protein TolC central to multidrug efflux and protein export. Nature. 405:914-919. (Pubitemid 30435040)
34. Pagel, M., V. Simonet, A. H. Delcour. 2007. Phenotypic characterization of pore mutants of the Vibrio cholerae porin OmpU. J. Bacteriol. 189:8593-8600. (Pubitemid 350210029)
35. Gurnev, P. A., A. B. Oppenheim, S. M. Bezrukov. 2006. Docking of a single phage lambda to its membrane receptor maltoporin as a timeresolved event. J. Mol. Biol. 359:1447-1455.