Note to users. If you're seeing this message, it means that your browser cannot find this page's style/presentation instructions -- or possibly that you are using a browser that does not support current Web standards. Find out more about why this message is appearing, and what you can do to make your experience of our site the best it can be.
Johnson & Johnson

Site Tools

  • AAAS
  • Subscribe
  • Feedback

Site Search

Search Advanced

Science 27 November 1992:
Vol. 258. no. 5087, pp. 1479 - 1481
DOI: 10.1126/science.1279810
Prev | Table of Contents | Next

Articles

Science, Vol 258, Issue 5087, 1479-1481
Copyright © 1992 by American Association for the Advancement of Science

articles

Porins in the cell wall of mycobacteria

J Trias, V Jarlier, and R Benz

Laboratoire de Bacteriologie-Virologie, Faculte de Medecine Pitie-Salpetriere, Paris, France.

The cell wall of mycobacteria is an efficient permeability barrier that makes mycobacteria naturally resistant to most antibiotics. Liposome swelling assays and planar bilayer experiments were used to investigate the diffusion process of hydrophilic molecules through the cell wall of Mycobacterium chelonae and identify the main hydrophilic pathway. A 59-kilodalton cell wall protein formed a water-filled channel with a diameter of 2.2 nanometers and an average single-channel conductance equal to 2.7 nanosiemens in 1 M potassium chloride. These results suggest that porins can be found in the cell wall of a Gram-positive bacterium. A better knowledge of the hydrophilic pathways should help in the design of more effective antimycobacterial agents.


THIS ARTICLE HAS BEEN CITED BY OTHER ARTICLES:
Bacterial Growth and Cell Division: a Mycobacterial Perspective.
E. C. Hett and E. J. Rubin (2008)
Microbiol. Mol. Biol. Rev. 72, 126-156
   Abstract »    Full Text »    PDF »
Corynebacterium diphtheriae: Identification and Characterization of a Channel-Forming Protein in the Cell Wall.
B. Schiffler, E. Barth, M. Daffe, and R. Benz (2007)
J. Bacteriol. 189, 7709-7719
   Abstract »    Full Text »    PDF »
The N-Terminal Domain of OmpATb Is Required for Membrane Translocation and Pore-Forming Activity in Mycobacteria.
A. Alahari, N. Saint, S. Campagna, V. Molle, G. Molle, and L. Kremer (2007)
J. Bacteriol. 189, 6351-6358
   Abstract »    Full Text »    PDF »
Methyl-beta-cyclodextrin alters growth, activity and cell envelope features of sterol-transforming mycobacteria.
M. V. Donova, V. M. Nikolayeva, D. V. Dovbnya, S. A. Gulevskaya, and N. E. Suzina (2007)
Microbiology 153, 1981-1992
   Abstract »    Full Text »    PDF »
Crystal Structure and Activity Studies of the Mycobacterium tuberculosis {beta}-Lactamase Reveal Its Critical Role in Resistance to {beta}-Lactam Antibiotics..
F. Wang, C. Cassidy, and J. C. Sacchettini (2006)
Antimicrob. Agents Chemother. 50, 2762-2771
   Abstract »    Full Text »    PDF »
Topology of the Porin MspA in the Outer Membrane of Mycobacterium smegmatis.
M. Mahfoud, S. Sukumaran, P. Hulsmann, K. Grieger, and M. Niederweis (2006)
J. Biol. Chem. 281, 5908-5915
   Abstract »    Full Text »    PDF »
The Porinologist.
P. E. Klebba (2005)
J. Bacteriol. 187, 8232-8236
   Full Text »    PDF »
PorH, a new channel-forming protein present in the cell wall of Corynebacterium efficiens and Corynebacterium callunae.
P. Hunten, B. Schiffler, F. Lottspeich, and R. Benz (2005)
Microbiology 151, 2429-2438
   Abstract »    Full Text »    PDF »
The Structure of a Mycobacterial Outer-Membrane Channel.
M. Faller, M. Niederweis, and G. E. Schulz (2004)
Science 303, 1189-1192
   Abstract »    Full Text »    PDF »
Importance of mycoloyltransferases on the physiology of Corynebacterium glutamicum.
R. Kacem, C. De Sousa-D'Auria, M. Tropis, M. Chami, P. Gounon, G. Leblon, C. Houssin, and M. Daffe (2004)
Microbiology 150, 73-84
   Abstract »    Full Text »    PDF »
Molecular Basis of Bacterial Outer Membrane Permeability Revisited.
H. Nikaido (2003)
Microbiol. Mol. Biol. Rev. 67, 593-656
   Abstract »    Full Text »    PDF »
PorA Represents the Major Cell Wall Channel of the Gram-Positive Bacterium Corynebacterium glutamicum.
N. Costa-Riu, A. Burkovski, R. Kramer, and R. Benz (2003)
J. Bacteriol. 185, 4779-4786
   Abstract »    Full Text »    PDF »
The Core of the Tetrameric Mycobacterial Porin MspA Is an Extremely Stable beta -Sheet Domain.
C. Heinz, H. Engelhardt, and M. Niederweis (2003)
J. Biol. Chem. 278, 8678-8685
   Abstract »    Full Text »    PDF »
The impact of the absence of glycopeptidolipids on the ultrastructure, cell surface and cell wall properties, and phagocytosis of Mycobacterium smegmatis.
G. Etienne, C. Villeneuve, H. Billman-Jacobe, C. Astarie-Dequeker, M.-A. Dupont, and M. Daffe (2002)
Microbiology 148, 3089-3100
   Abstract »    Full Text »    PDF »
A Tetrameric Porin Limits the Cell Wall Permeability of Mycobacterium smegmatis.
H. Engelhardt, C. Heinz, and M. Niederweis (2002)
J. Biol. Chem. 277, 37567-37572
   Abstract »    Full Text »    PDF »
Signal-sequence-independent secretion of the staphylococcal nuclease in Mycobacterium smegmatis.
C. Recchi, J. Rauzier, B. Gicquel, and J.-M. Reyrat (2002)
Microbiology 148, 529-536
   Abstract »    Full Text »    PDF »
Structure of the cell envelope of corynebacteria: importance of the non-covalently bound lipids in the formation of the cell wall permeability barrier and fracture plane.
V. Puech, M. Chami, A. Lemassu, M.-A. Lanéelle, B. Schiffler, P. Gounon, N. Bayan, R. Benz, and M. Daffé (2001)
Microbiology 147, 1365-1382
   Abstract »    Full Text »
Identification of the Outer Membrane Porin of Thermus thermophilus HB8: the Channel-Forming Complex Has an Unusually High Molecular Mass and an Extremely Large Single-Channel Conductance.
E. Maier, G. Polleichtner, B. Boeck, R. Schinzel, and R. Benz (2001)
J. Bacteriol. 183, 800-803
   Abstract »    Full Text »
Biochemical Identification and Biophysical Characterization of a Channel-Forming Protein from Rhodococcus erythropolis.
T. Lichtinger, G. Reiss, and R. Benz (2000)
J. Bacteriol. 182, 764-770
   Abstract »    Full Text »
Porins in the Cell Wall of Mycobacterium tuberculosis.
B. Kartmann, S. Stengler, and M. Niederweis (1999)
J. Bacteriol. 181, 6543-6546
   Abstract »    Full Text »
The C-Terminal Domain of the Bordetella pertussis Autotransporter BrkA Forms a Pore in Lipid Bilayer Membranes.
J. L. Shannon and R. C. Fernandez (1999)
J. Bacteriol. 181, 5838-5842
   Abstract »    Full Text »
Expression of a Gene for a Porin-Like Protein of the OmpA Family from Mycobacterium tuberculosis H37Rv.
R. H. Senaratne, H. Mobasheri, K. G. Papavinasasundaram, P. Jenner, E. J. A. Lea, and P. Draper (1998)
J. Bacteriol. 180, 3541-3547
   Abstract »    Full Text »
Multidrug Resistance following Expression of the Escherichia coli marA Gene in Mycobacterium smegmatis.
P. F. McDermott, D. G. White, I. Podglajen, M. N. Alekshun, and S. B. Levy (1998)
J. Bacteriol. 180, 2995-2998
   Abstract »    Full Text »
Accumulation of Norfloxacin by Mycobacterium aurum and Mycobacterium smegmatis.
K. J. Williams, G. A. C. Chung, and L. J. V. Piddock (1998)
Antimicrob. Agents Chemother. 42, 795-800
   Abstract »    Full Text »
Voltage-dependent Porin-like Ion Channels in the Archaeon Haloferax volcanii.
M. Besnard, B. Martinac, and A. Ghazi (1997)
J. Biol. Chem. 272, 992-995
   Abstract »    Full Text »    PDF »
Mycolic Acid Structure Determines the Fluidity of the Mycobacterial Cell Wall.
J. Liu, C. E. Barry III, G. S. Besra, and H. Nikaido (1996)
J. Biol. Chem. 271, 29545-29551
   Abstract »    Full Text »    PDF »
Prevention of drug access to bacterial targets: permeability barriers and active efflux.
H Nikaido (1994)
Science 264, 382-388
   Abstract »    PDF »


ADVERTISEMENT
Click Me!

ADVERTISEMENT
Click Me!

To Advertise     Find Products

Science. ISSN 0036-8075 (print), 1095-9203 (online)