AI Article Synopsis
- Bacteriophages have enzymes called depolymerases that are crucial for infecting bacteria, which act as tail spike proteins.
- These enzymes target and cleave specific polysaccharides on the surface of host bacteria, such as capsular polysaccharides and lipopolysaccharides.
- The review highlights the variety of these depolymerases and their roles in bacterial infection, as well as their potential applications in biotechnology.
Article Abstract
Bacteriophages of the 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 , , and 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.
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| http://www.ncbi.nlm.nih.gov/pmc/articles/PMC6966330 | PMC |
| http://dx.doi.org/10.3389/fmicb.2019.02949 | DOI Listing |
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