Diversity and Function of Phage Encoded Depolymerases.
- Knecht LE Institute of Food and Beverage Innovation, Zurich University of Applied Sciences, Wädenswil, Switzerland.
- Veljkovic M Institute of Food and Beverage Innovation, Zurich University of Applied Sciences, Wädenswil, Switzerland.
- Fieseler L Institute of Food and Beverage Innovation, Zurich University of Applied Sciences, Wädenswil, Switzerland.
- 2020-01-31
Published in:
- Frontiers in microbiology. - 2019
English
Bacteriophages of the Podoviridae family often exhibit so-called depolymerases as structural components of the virion. These enzymes appear as tail spike proteins (TSPs). After specific binding to capsular polysaccharides (CPS), exopolysaccharides (EPS) or lipopolysaccharide (LPS) of the host bacteria, polysaccharide-repeating units are specifically cleaved. Finally, the phage reaches the last barrier, the cell wall, injects its DNA, and infects the cell. Recently, similar enzymes from bacteriophages of the Ackermannviridae, Myoviridae, and Siphoviridae families were also described. In this mini-review the diversity and function of phage encoded CPS-, EPS-, and LPS-degrading depolymerases is summarized. The function of the enzymes is described in terms of substrate specificity and applications in biotechnology.
- Language
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- English
- Open access status
- gold
- Identifiers
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- DOI 10.3389/fmicb.2019.02949
- PMID 31998258
- Persistent URL
- https://sonar.ch/global/documents/248848
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