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Diversity and Function of Phage Encoded Depolymerases
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 bacter...
Autores principales: | , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
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Frontiers Media S.A.
2020
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Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6966330/ https://www.ncbi.nlm.nih.gov/pubmed/31998258 http://dx.doi.org/10.3389/fmicb.2019.02949 |
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author | Knecht, Leandra E. Veljkovic, Marjan Fieseler, Lars |
author_facet | Knecht, Leandra E. Veljkovic, Marjan Fieseler, Lars |
author_sort | Knecht, Leandra E. |
collection | PubMed |
description | 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. |
format | Online Article Text |
id | pubmed-6966330 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2020 |
publisher | Frontiers Media S.A. |
record_format | MEDLINE/PubMed |
spelling | pubmed-69663302020-01-29 Diversity and Function of Phage Encoded Depolymerases Knecht, Leandra E. Veljkovic, Marjan Fieseler, Lars Front Microbiol Microbiology 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. Frontiers Media S.A. 2020-01-10 /pmc/articles/PMC6966330/ /pubmed/31998258 http://dx.doi.org/10.3389/fmicb.2019.02949 Text en Copyright © 2020 Knecht, Veljkovic and Fieseler. http://creativecommons.org/licenses/by/4.0/ This is an open-access article distributed under the terms of the Creative Commons Attribution License (CC BY). The use, distribution or reproduction in other forums is permitted, provided the original author(s) and the copyright owner(s) are credited and that the original publication in this journal is cited, in accordance with accepted academic practice. No use, distribution or reproduction is permitted which does not comply with these terms. |
spellingShingle | Microbiology Knecht, Leandra E. Veljkovic, Marjan Fieseler, Lars Diversity and Function of Phage Encoded Depolymerases |
title | Diversity and Function of Phage Encoded Depolymerases |
title_full | Diversity and Function of Phage Encoded Depolymerases |
title_fullStr | Diversity and Function of Phage Encoded Depolymerases |
title_full_unstemmed | Diversity and Function of Phage Encoded Depolymerases |
title_short | Diversity and Function of Phage Encoded Depolymerases |
title_sort | diversity and function of phage encoded depolymerases |
topic | Microbiology |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6966330/ https://www.ncbi.nlm.nih.gov/pubmed/31998258 http://dx.doi.org/10.3389/fmicb.2019.02949 |
work_keys_str_mv | AT knechtleandrae diversityandfunctionofphageencodeddepolymerases AT veljkovicmarjan diversityandfunctionofphageencodeddepolymerases AT fieselerlars diversityandfunctionofphageencodeddepolymerases |