Abstract
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.
Highlights
Bacteriophages of the Podoviridae family often exhibit so-called depolymerases as structural components of the virion
The infection begins with the adsorption, the recognition of specific ligands at the host surface by tail fiber or tail spike proteins (TSPs)
A bacteriophage infects a particular serotype of the target bacterium only
Summary
Chen et al, 2019b Chen et al, 2018 Hernandez-Morales et al, 2018 Lin et al, 2014. Popova et al, 2017 Popova et al, 2017 Lai et al, 2016 Liu et al, 2019 Oliveira et al, 2019b Oliveira et al, 2017 Oliveira et al, 2017 Oliveira et al, 2017 Oliveira et al, 2017 Oliveira et al, 2017 Oliveira et al, 2017 Oliveira et al, 2017 Oliveira et al, 2017 Oliveira et al, 2017.
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