Computational protein design of bacteriocins based on structural scaffold of aureocin A53

Abstract

Bacteriocins are highly potent anti-microbial polypeptides and proteins produced by bacteria. They are rapidly degraded in the environment after their use, due to their proteinaceous nature. Some bacteriocins are used as preservatives in foods. Native and engineered bacteriocins are of potential interest as replacements for conventional antibiotics that are losing their efficacy due to the development of antibiotic-resistant strains. Aureocin A53 is a class II bacteriocin. It is a broad spectrum microbicide, with demonstrated ability to inhibit the growth of methicillin-resistant Staphylococcus aureus. Validated computational protein design tools have been used for reengineering of the aureocin A53 sequence to produce novel sequence variants of the bacteriocins aureocin A53 and lacticin Q. The novel proteins are expected to possess an altered spectrum of bactericidal specificity and potency.