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LytM Fusion with SH3b-Like Domain Expands Its Activity to Physiological Conditions.

ABSTRACT: Staphylococcus aureus remains one of the most common and at the same time the most dangerous bacteria. The spreading antibiotic resistance calls for intensification of research on staphylococcal physiology and development of new strategies for combating this threatening pathogen. We have engineered new chimeric enzymes comprising the enzymatically active domain (EAD) of autolysin LytM from S. aureus and the cell wall binding domain (CBD) from bacteriocin lysostaphin. They display potent activity in extended environmental conditions. Our results exemplify the possibility of exploring autolytic enzymes in engineering lysins with desired features. Moreover, they suggest a possible mechanism of autolysin physiological activity regulation by local ionic environments in the cell wall.

SUBMITTER: Jagielska E

PROVIDER: S-EPMC5036312 | biostudies-literature | 2016 Sep

REPOSITORIES: biostudies-literature

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LytM Fusion with SH3b-Like Domain Expands Its Activity to Physiological Conditions.

Jagielska Elzbieta E Chojnacka Olga O Sabała Izabela I

Microbial drug resistance (Larchmont, N.Y.) 20160628 6

Staphylococcus aureus remains one of the most common and at the same time the most dangerous bacteria. The spreading antibiotic resistance calls for intensification of research on staphylococcal physiology and development of new strategies for combating this threatening pathogen. We have engineered new chimeric enzymes comprising the enzymatically active domain (EAD) of autolysin LytM from S. aureus and the cell wall binding domain (CBD) from bacteriocin lysostaphin. They display potent activity ...[more]

PMID: 27351490

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