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Title

Endolysins as Antimicrobials

AuthorsNelson, Daniel C.; Schmelcher, Mathias; Rodríguez, Lorena ; Klumpp, Jochen; Pritchard, David G.; Dong, Shengli; Donovan, David M.
Issue Date2012
PublisherAcademic Press
CitationAdvances in Virus Research 83: 299-365 (2012)
AbstractPeptidoglycan (PG) is the major structural component of the bacterial cell wall. Bacteria have autolytic PG hydrolases that allow the cell to grow and divide. A well-studied group of PG hydrolase enzymes are the bacteriophage endolysins. Endolysins are PG-degrading proteins that allow the phage to escape from the bacterial cell during the phage lytic cycle. The endolysins, when purified and exposed to PG externally, can cause > lysis from without.> Numerous publications have described how this phenomenon can be used therapeutically as an effective antimicrobial against certain pathogens. Endolysins have a characteristic modular structure, often with multiple lytic and/or cell wall-binding domains (CBDs). They degrade the PG with glycosidase, amidase, endopeptidase, or lytic transglycosylase activities and have been shown to be synergistic with fellow PG hydrolases or a range of other antimicrobials. Due to the coevolution of phage and host, it is thought they are much less likely to invoke resistance. Endolysin engineering has opened a range of new applications for these proteins from food safety to environmental decontamination to more effective antimicrobials that are believed refractory to resistance development. To put phage endolysin work in a broader context, this chapter includes relevant studies of other well-characterized PG hydrolase antimicrobials. © 2012 Elsevier Inc.
DescriptionBacteriophages, Part B
Publisher version (URL)http://dx.doi.org/10.1016/B978-0-12-394438-2.00007-4
URIhttp://hdl.handle.net/10261/80868
DOI10.1016/B978-0-12-394438-2.00007-4
Identifiersdoi: 10.1016/B978-0-12-394438-2.00007-4
issn: 0065-3527
Appears in Collections:(IPLA) Artículos
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