Bacteriophage endolysins as novel antimicrobials
By M. Schmelcher, D. Donovan, M. Loessner. Future Microbiology, 2012
721 citations recorded by the source corpus.
Endolysins are enzymes used by bacteriophages at the end of their replication cycle to degrade the peptidoglycan of the bacterial host from within, resulting in cell lysis and release of progeny virions. Due to the absence of an outer membrane in the Gram-positive bacterial cell wall, endolysins can access the peptidoglycan and destroy these organisms when applied externally, making them interesting antimicrobial candidates, particularly in light of increasing bacterial drug resistance. This article reviews the modular structure of these enzymes, in which cell wall binding and catalytic functions are separated, as well as their mechanism of action, lytic activity and potential as antimicrobials. It particularly focuses on molecular engineering as a means of optimizing endolysins for specific applications, highlights new developments that may render these proteins active against Gram-negative and intracellular pathogens and summarizes the most recent applications of endolysins in the fields of medicine, food safety, agriculture and biotechnology.
Subfields: Ecology, Food Science, Molecular Biology
View Paper: https://www.semanticscholar.org/paper/26ed56f559157f4a672cf31b5c9c610bb5d8ab83
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Citations in the corpus
- Antibiotic resistance and persistence—Implications for human health and treatment perspectives (2020, positive): “…serum half-lives, low penetration into eukaryotic cells to kill intracellular bacteria and toxicity, many research groups focus on engineering improved variants that might offer novel treatment options in the future (Schmelcher et al , 2012; Haddad Kashani et al , 2018; R € ohrig et al , 2020).”