Modulation of Endolysin LysECD7 Bactericidal Activity by Different Peptide Tag Fusion.

ABSTRACT: The use of recombinant endolysins is a promising approach for antimicrobial therapy capable of counteracting the spread of antibiotic-resistant strains. To obtain the necessary biotechnological product, diverse peptide tags are often fused to the endolysin sequence to simplify enzyme purification, improve its ability to permeabilize the bacterial outer membrane, etc. We compared the effects of two different types of protein modifications on endolysin LysECD7 bactericidal activity in vitro and demonstrated that it is significantly modulated by specific permeabilizing antimicrobial peptides, as well as by widely used histidine tags. Thus, the tags selected for the study of endolysins and during the development of biotechnological preparations should be used with the appropriate precautions t

SUBMITTER: Antonova NP 

PROVIDER: S-EPMC7175214 | biostudies-literature | 2020 Mar

REPOSITORIES: biostudies-literature