Abstract
The porin MspA from Mycobacterium smegmatis has many unique properties, one being that it is the longest and the most stable porin identified to date. It is formed by supramolecular interaction of eight identical monomers of 184 amino acid residues (m = 20,000 Da). With dimensions of approx 10 nm in length and a diameter ranging from 1 nm (constriction zone) to 4.8 nm (opening of the MspA-goblet), it is ideal for bio-nanotechnological applications. The porin possesses a hydrophobic “docking zone,” which enables it to reconstitute not only in lipid membranes, but also in numerous artificial (mono)membranes and hydrophobic, water-soluble polymer layers. Furthermore, we demonstrate here the design and proof-of-principle of an MspA porin-based biosensor for the TB-antibiotic isoniazid.
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References
Brennan PJ, Nikaido H. The envelope of mycobacteria. Annu Rev Biochem 1995; 64:29–63.
Nikaido H, Kim SH, Rosenberg EY. Physical organization of lipids in the cell wall of Mycobacterium chelonae. Mol Microbiol 1993; 8:1025–1030.
Liu J, Barry CE III, Besra GS, Nikaido H. Mycolic acid structure determines the fluidity of the mycobacterial cell wall. J Biol Chem 1996; 271:29,545–29,551.
Trias J, Jarlier V, Benz R. Porins in the cell wall of mycobacteria. Science 1992; 258:1479–1481.
Dmitriev BA, Ehlers S, Rietschel ET, Brennan PJ. Molecular mechanics of the mycobacterial cell wall: from horizontal layers to vertical scaffolds. Int J Med Microbiol 2000; 290:251–258.
Niederweis M. Mycobacterial porins-new channel proteins in unique outer membranes. Mol Microbiol 2003; 49:1167–1177.
Faller M, Niederweis M, Schulz GE. The structure of a mycobacterial outermembrane channel. Science 2004; 303:1189–1192.
Stahl C, Kubetzko S, Kaps I, Seeber S, Engelhardt H, Niederweis M. MspA provides the main hydrophilic pathway through the cell wall of Mycobacterium smegmatis. Mol Microbiol 2001; 40:451–464.
Engelhardt H, Heinz C, Niederweis M. A tetrameric porin limits the cell wall permeability of Mycobacterium smegmatis. J Biol Chem 2002; 277:37,567–37,572.
Heinz C, Niederweis M. Selective extraction and purification of a mycobacterial outer membrane protein. Anal Biochem 2000; 285:113–120.
Heinz C, Roth E, Niederweis M. Purification of porins from Mycobacterium smegmatis. Meth Mol Biol 2003; 228:139–150.
Niederweis M, Heinz C, Janik K, Bossmann SH. Nanostructuring by deposition of protein channels formed on carbon surfaces. Nano Lett 2002: 2;1263–1268.
Bossmann SH, Janik K, Pokhrel MR, Heinz C, Niederweis M. Reconstitution of a porin from Mycobacterium smegmatis at HOPG covered with hydrophobic host layers. Surface and Interface Analysis 2004; 36:127–134.
Ottaviani MF, Winnik FM, Bossmann SH, Turro NJ. Phase separation of poly(Nisopropylacrylamide) in mixtures of water and methanol: a spectroscopic study of the phase-transition process with a polymer tagged with a fluorescent dye and a spin label. Helv Chim Acta 2001; 84:2476–2492.
Mailaender C, Reiling N, Engelhardt H, Bossmann S, Ehlers S, Niederweis M. The MspA porin promotes growth and increases antibiotic susceptibility of both Mycobacterium bovis BCG and Mycobacterium tuberculosis. Microbiology 2004; 150:853–864.
Nikaido H, Nikaido K, Harayama S. Identification and characterization of porins in Pseudomonas aeruginosa. J Biol Chem 1991; 266:770–779.
Hu YZ, van Loyen D, Schwarz O, et al. Intramolecular electron transfer between noncovalently linked donor and acceptor in a [2]catenane. J Am Chem Soc 1998; 120:5822–5823.
Hu YZ, Bossmann SH, Van Loyen D, Schwarz O, Duerr H. A novel 2,2′ bipyridine[2]catenane and its ruthenium complex: synthesis, structure, and intramolecular electron transfer-a model for the photosynthetic reaction center. Chemistry-A European Journal 1999; 5:1267–1277.
Duerr H, Bossmann S. Ruthenium polypyridine complexes. On the route to biomimetic assemblies as models for the photosynthetic reaction center. Acc Chem Res 2001; 34:905–917.
O’Neil MJ. The Merck Index: An Encyclopedia of Chemicals, Drugs and Biologicals, 12th ed. Whithouse Station, New Jersey: Merck Research Laboratories, 2000.
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© 2008 Humana Press Inc., Totowa, NJ
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Bossmann, S.H., Janik, K., Pokhrel, M.R., Niederweis, M. (2008). Experimental Strategies Toward the Use of the Porin MspA as a Nanotemplate and for Biosensors. In: Shoseyov, O., Levy, I. (eds) NanoBioTechnology. Humana Press. https://doi.org/10.1007/978-1-59745-218-2_2
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DOI: https://doi.org/10.1007/978-1-59745-218-2_2
Publisher Name: Humana Press
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