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Review
. 2020 Jan 10:10:2949.
doi: 10.3389/fmicb.2019.02949. eCollection 2019.

Diversity and Function of Phage Encoded Depolymerases

Leandra E Knecht  1 , Marjan Veljkovic  1 , Lars Fieseler  1
Affiliations
Review

Diversity and Function of Phage Encoded Depolymerases

Leandra E Knecht et al. Front Microbiol. .

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.

Keywords: bacteriophage; capsule; depolymerase; lipopolysaccharide; polysaccharide.

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Figures

FIGURE 1
FIGURE 1
Phylogenetic analysis of phage encoded tail spike proteins. The unrooted cladogram was calculated using neighbor joining and jukes-cantor correction. Bootstrap values are indicated at the nodes. A bootstrap value of 90 is considered significant.
FIGURE 2
FIGURE 2
TSP architecture and connection to the virion or baseplate in different phage genera. The schematic is not drawn to scale. For a better overview only one TSP ore branch of TSPs, respectively, is illustrated.
See this image and copyright information in PMC

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