Abstract
The porins are proteins involved in the exchange of hydrophilic solutes between Gram-negative bacteria and their outer environment (1). These proteins, which are exclusively localized in the outer membrane, are transmembranous and interact with the constituents of the membrane, lipids, and lipopolysaccha-ride. They also interact with the periplasmic peptidoglycan layer (2).
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References
Nikaido, H. (1992) Porins and specific channels of bacterial outer membranes. Mol. Microbiol. 6, 435–442.
Rosenbusch, J.P. (1974) Characterization of the major envelope protein from Escherichia coli. Regular arrangement on the peptidoglycan and unusual dodecylsulfate binding. J. Biol. Chem. 249, 8019–8029.
Nakae, T. (1976) Identification of the outer membrane protein of Escherichia coli that produces transmembrane channels in reconstituted vesicle membranes. Biochem. Biophys. Res. Commun. 71, 877–884.
Nikaido, H. (1996) Outer membrane, in Escherichia coli and Salmonella, Cellular and Molecular Biology (Neidhardt, F.C., ed.), ASM, Washington, DC, pp. 29–47.
Jeanteur, D., Lakey, J. H., and Pattus, F. (1991) The bacterial porin superfamily: sequence alignment and structure prediction. Mol. Microbiol. 5, 2153–2164.
Cowan, S. W., Schirmer, T., Rummel, G., Steiert, M., Ghosh, R., Pauptit, R. A., et al. (1992) Crystal structure explain functional properties of two E. coli porins. Nature 358, 727–733.
Jap, B.K. and Walian P.J. (1996) Structure and functional mechanism of porins. Physiol. Rev. 76, 1073–1087.
Koebnik, R., Locher, K. P., and van Gelder, P. (2000) Structure and function of bacterial outer membrane proteins: barrel in a nutshell. Mol. Microbiol. 37, 239–253.
Weiss, M.S. and Schulz, G E. (1992) Structure of porin refined at 1.8 A resolution. J. Mol. Biol. 227, 493–509.
Huyer, M., Parr, T. R., Hancock, R. E. W, and Page, W.J. (1986) Outer membrane porin protein in Campylobacter jejuni. FEMS Microbiol. Lett. 37, 247–250.
Bolla, J-M., Loret, E., Zalewski, M., and Pagès, J.-M. (1995) Conformational analysis of the Campylobacter jejuni porin. J. Bacteriol. 177, 4266–4271.
Zhuang, J., Engel, A., Pagès, J.-M., and Bolla, J.-M. (1997) The Campylobacter jejuni porin trimers pack into different lattice types when reconstituted in the presence of lipid. Eur. J. Biochem. 244, 575–579.
Dé, E., Jullien, M., Labesse, G., Pagès, J.-M., Molle, G., and Bolla, J.-M. (2000) MOMP (Major Outer Membrane Protein) of Campylobacter jejuni; a versatile pore forming protein. FEBS Lett. 469, 93–97.
Labesse, G., Garnotel, E., Bonnel, S., Dumas, C., Pagès, J.-M., and Bolla, J.-M. (2001) MOMP a divergent porin from Campylobacter, cloning and primary structural characterization. Biochem. Biophys. Res. Commun. 280, 380–387.
Bolla, J.-M., E. Dé, A. Dorez, and Pagès, J.-M. (2000) Purification, characterization and sequence analysis of Omp50, a new porin isolated from Campylobacter jejuni. Biochem. J. 352, 637–643.
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Bolla, J.M. (2003). Purification of Omp50, a Minor Porin of Campylobacter jejuni . In: Selinsky, B.S. (eds) Membrane Protein Protocols. Methods in Molecular Biology, vol 228. Humana Press. https://doi.org/10.1385/1-59259-400-X:131
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DOI: https://doi.org/10.1385/1-59259-400-X:131
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