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Phage Endolysin: A Way To Understand A Binding Function Of C-Terminal Domains A Mini Review

Phage Endolysin: A Way To Understand A Binding Function Of C-Terminal Domains A Mini Review Abstract Endolysins are bacteriophage-encoded peptidoglycan hydrolases, which are synthesized in the end of phage reproduction cycle, in an infected host cell. Usually, for endolysins from phages that infect Gram-positive bacteria, a modular structure is typical. Therefore, these are composed of at least two separate functional domains: an N-terminal catalytic domain (EAD) and a C-terminal cell wall binding domain (CBD). Specific ligand recognition of CBDs and following peptidoglycan (PG) binding mostly allows a rapid lytic activity of an EAD. Here we briefly characterize phage endolysin CBDs in conjuction with their domain architecture, (non)necessity for the following lytic activity and a high/low specificity of their ligands as well. Such an overall assessment of CBDs may help to find new ways to widen opportunities in their protein design to create ‛designer recombinant endolysins’ with diverse applications. http://www.deepdyve.com/assets/images/DeepDyve-Logo-lg.png Nova Biotechnologica et Chimica de Gruyter

Phage Endolysin: A Way To Understand A Binding Function Of C-Terminal Domains A Mini Review

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Publisher
de Gruyter
Copyright
Copyright © 2015 by the
ISSN
1338-6905
eISSN
1338-6905
DOI
10.1515/nbec-2015-0021
Publisher site
See Article on Publisher Site

Abstract

Abstract Endolysins are bacteriophage-encoded peptidoglycan hydrolases, which are synthesized in the end of phage reproduction cycle, in an infected host cell. Usually, for endolysins from phages that infect Gram-positive bacteria, a modular structure is typical. Therefore, these are composed of at least two separate functional domains: an N-terminal catalytic domain (EAD) and a C-terminal cell wall binding domain (CBD). Specific ligand recognition of CBDs and following peptidoglycan (PG) binding mostly allows a rapid lytic activity of an EAD. Here we briefly characterize phage endolysin CBDs in conjuction with their domain architecture, (non)necessity for the following lytic activity and a high/low specificity of their ligands as well. Such an overall assessment of CBDs may help to find new ways to widen opportunities in their protein design to create ‛designer recombinant endolysins’ with diverse applications.

Journal

Nova Biotechnologica et Chimicade Gruyter

Published: Dec 1, 2015

References