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Antibiotics

Blocking bacterial defences

Nature Chemistry volume 5, pages 642–643 (2013)Cite this article

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Electrochemical sensing of the function of cell-membrane proteins has led to the identification of inhibitors that could provide a new approach to the identification of antimicrobial drugs.

The increasing prevalence of microbial resistance to antibiotics presents an enormous challenge to society, and an opportunity for innovative solutions1. Although efforts to improve agents acting on validated targets continue, the exploitation of prospective new targets or modes of drug action is highly desirable2. Biogenesis of the microbial lipid- and carbohydrate-rich cell wall has proved a valuable target for antimicrobial agents, notably in connection with tuberculosis chemotherapy3. Most of these drugs are directed against the enzymes that synthesize the complex lipids and glycopolymers that decorate the cell surface, with the intent to introduce defects in this glycocalyx that might sensitize the bacterium to host-mediated lysis. An alternative approach might be to block either the export of the protective polysaccharide from the interior of the cell where it is synthesized, or its assembly on the outer face of the cell membrane4. The identification of polysaccharide export systems has moved forward greatly in the past decade, but assays of such integral membrane protein transporters have, until recently, proved far from trivial. The latest single-molecule detection techniques are now paving the way to monitoring the dynamic translocation of analytes and polymers through these large multi-subunit protein nanopores.

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Figure 1: Blocking the bacterial nanopore Wza.

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Authors and Affiliations

  1. Ellis O'Neill and Robert Field are in the Department of Biological Chemistry, John Innes Centre, Norwich Research Park, Norwich NR4 7UH, UK,

    Ellis C. O'Neill & Robert A. Field

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  1. Ellis C. O'Neill
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  2. Robert A. Field
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Correspondence to Robert A. Field.

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O'Neill, E., Field, R. Blocking bacterial defences. Nature Chem 5, 642–643 (2013). https://doi.org/10.1038/nchem.1718

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