Diversity and Function of Phage Encoded Depolymerases

被引:187
作者
Knecht, Leandra E. [1 ]
Veljkovic, Marjan [1 ]
Fieseler, Lars [1 ]
机构
[1] Zurich Univ Appl Sci, Inst Food & Beverage Innovat, Wadenswil, Switzerland
来源
FRONTIERS IN MICROBIOLOGY | 2020年 / 10卷
关键词
bacteriophage; depolymerase; polysaccharide; capsule; lipopolysaccharide; POLY-GAMMA-GLUTAMATE; TAILSPIKE PROTEIN; KLEBSIELLA-PNEUMONIAE; CRYSTAL-STRUCTURE; BACTERIOPHAGE; INFECTION; CAPSULE; POLYSACCHARIDE; EVOLUTION; K1;
D O I
10.3389/fmicb.2019.02949
中图分类号
Q93 [微生物学];
学科分类号
071005 ; 100705 ;
摘要
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.
引用
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页数:16
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