Domain shuffling and module engineering of Listeria phage endolysins for enhanced lytic activity and binding affinity.

ABSTRACT: Bacteriophage endolysins are peptidoglycan hydrolases employed by the virus to lyse the host at the end of its multiplication phase. They have found many uses in biotechnology; not only as antimicrobials, but also for the development of novel diagnostic tools for rapid detection of pathogenic bacteria. These enzymes generally show a modular organization, consisting of N-terminal enzymatically active domains (EADs) and C-terminal cell wall-binding domains (CBDs) which specifically target the enzymes to their substrate in the bacterial cell envelope. In this work, we used individual functional modules of Listeria phage endolysins to create fusion proteins with novel and optimized properties for labelling and lysis of Listeria cells. Chimaeras consisting of individual EAD and CBD modules from

SUBMITTER: Schmelcher M 

PROVIDER: S-EPMC3819014 | biostudies-literature | 2011 Sep

REPOSITORIES: biostudies-literature