endolysin

These products are both based on phage and endolysin technology.

R is an endolysin, an enzyme that escapes through the S holes and cleaves the cell wall.

This family includes lambda phage lysozyme and Escherichia coli endolysin.

E. coli endolysin also functions in bacterial cell lysis and acts as a transglycosylase.

A notable exception is the streptococcal PlyC endolysin, which is 114 kDa.

Lysis, by tailed phages, is achieved by an enzyme called endolysin, which attacks and breaks down the cell wall peptidoglycan.

Rz and Rz1 are membrane proteins that form a complex that somehow destroys the outer membrane, after the endolysin has degraded the cell wall.

Bacteriophages of the pathogen Listeria monocytogenes encode endolysin enzymes which specifically hydrolyse the cross-linking peptide bridges in Listeria peptidoglycan.

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.

Janakiraman Ramachandran argues that this complication can be avoided in those types of infection where this reaction is likely to occur by using genetically engineered bacteriophages which have had their gene responsible for producing endolysin removed.

Genes for endolysins that are responsible for the onset of bacterial lysis are often located near genes that encode for holin-like proteins, suggesting that these holins are responsible for endolysin export to the cell wall.