Izabela Sabała attended the ISSSI meeting (Internal Symposium on Staphylococci and Staphylococcal infections) in Copenhagen, Denmark (August 23-26, 2018) and presented Auresine project recent achievements.
Abstract
Application of bacteriolytic enzyme Auresine in elimination of Staphylococcus
LytM is an autolysin present in S. aureus cell wall, but its native form is inactive. Based on structural studies we have engineered the active form of this enzyme, called Auresine. Auresine is a peptidolytic enzyme cleaving cell walls of Staphylococcus sp. including S. aureus leading to instant cell lysis. The enzyme is a member of the M23 family of zinc-dependent metallopeptidases, which are recognized primarily for their glycylglycine endopeptidase activity. Auresine with its exceptional staphylolytic activity and stability is a potent, non-antibiotic weapon against Staphylococcus. It acts instantly on contact and is very effective against various antibiotic resistant strains and biofilms. The enzyme cleaves only staphylococcal cell walls, leaving natural microflora untouched. Moreover, Auresine is active in a wide range of temperatures (even on ice) and in low conductivity conditions (e.g. water). Auresine can serve as a selective, non-toxic, biodegradable antibacterial agent. It can be applied as additive to surface disinfectants, food biopreservatives, component of veterinary and human hygiene products for skin infection prevention and treatment, as well as a part of wound dressings. Based on our structural studies we are engineering this enzyme to overcome potential resistance and tune its features to various applications.