Submitted to: Advances in Virus Research
Publication Type: Book / Chapter
Publication Acceptance Date: 11/15/2011
Publication Date: 1/1/2012
Citation: Nelson, D.C., Schmelcher, M., Rodirguez, L., Klumpp, J., Pritchard, D.G., Dong, S., Donovan, D.M. 2012. Endolysins as antimicrobials. Advances in Virus Research. Interpretive Summary:
Technical Abstract: Peptidoglycan (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. 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 co-evolution of phage and host, it is thought they are much less likely to invoke resistance. Recently, 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 the phage endolysin work in a broader context, this chapter includes relevant studies of other well characterized PG hydrolase antimicrobials.