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Lookup NU author(s): Professor Jeff ErringtonORCiD
This work is licensed under a Creative Commons Attribution 4.0 International License (CC BY 4.0).
© 2017 The Author(s). The peptidoglycan (PG) cell wall is a defining feature of the bacteria. It emerged very early in evolution and must have contributed significantly to the success of these organisms. The wall features prominently in our thinking about bacterial cell function, and its synthesis involves the action of several dozen proteins that are normally essential for viability. Surprisingly, it turns out to be relatively simple to generate bacterial genetic variants called L-forms that completely lack PG. They grow robustly provided that lack of the cell wall is compensated for by an osmoprotective growth medium. Although their existence has been noted and studied on and off for many decades, it is only recently that modern molecular and cellular methods have been applied to L-forms. We used Bacillus subtilis as an experimental model to understand the molecular basis for the L-form switch. Key findings included the discovery that L-forms use an unusual blebbing, or tubulation and scission mechanism to proliferate. This mechanism is completely independent of the normal FtsZ-based division machinery and seems to require only an increased rate of membrane synthesis, leading to an increased surface area-to-volume ratio. Antibiotics that block cell wall precursor synthesis, such as phosphomycin, efficiently induce the L-form switch without the need for genetic change. The same antibiotics turned out to induce a similar L-form switch in a wide range of bacteria, including Escherichia coli, in which we showed that proliferation was again FtsZ-independent. Aside from further basic science, future work on L-forms is likely to focus on their possible role in chronic or recurrent infections, their use as a model in studies of the origins of life, and possibly, biotechnological applications.
Author(s): Errington J
Publication type: Review
Publication status: Published
Journal: Biochemical Society Transactions
Year: 2017
Volume: 45
Issue: 2
Pages: 287-295
Print publication date: 13/04/2017
Online publication date: 13/04/2017
Acceptance date: 02/04/2016
ISSN (print): 0300-5127
ISSN (electronic): 1470-8752
Publisher: Portland Press Ltd
URL: https://doi.org/10.1042/BST20160435
DOI: 10.1042/BST20160435
