The host recognition of bacteriophages occur via bacteria-binding proteins that have strong binding affinities to specific protein or carbohydrate structures on the surface of the bacterial host. At the end of the infection life cycle the bacteria-lysing Endolysin is synthesized and degrades the bacterial peptidoglycan cell wall, resulting in lysis (and therefore killing) of the bacterial cell.
Bacteriophage derived proteins are used for detection and removal of bacteria   and bacterial components (especially endotoxin contaminations) in pharmaceutical and biological products, human diagnostics, food,   and decolonization of bacteria causing nosocomial infections (e.g. MRSA). Protein modifications allow the biotechnological adaption to specific requirements.
- Technological background
- Kretzer JW, Lehmann R, Banz M, Kim KP, Korn C. Loessner MJ (2007) Use of high affinity cell wall-binding domains of bacteriophage endolysins for immobilization and separation of bacterial cells. Appl Environ Microbiol 73:1992-2000
- Rozand, C., Feng, P. C. H. (2009). Specificity analysis of a novel phage-derived ligand in an Enzyme-linked fluorescent assay for detection of Escherichia coli O157:H7. J. food protection 72, 1078-1081.
- "Bacteriophages - New Applications in Food Microbiology" (PDF), BioFood (3): 2, December 2006, archived from the original (PDF) on 1 October 2011
- Applications of the phage-ligand technology (endotoxin detection, endotoxin removal, food safety testing)