Staphylococcus haemolyticus prophage φSH2 endolysin is lytic for Staphylococcus aureus

US8980614B2 · kind B2 · utility

Assignee

• The United States of America, as represented by the Secretary of Agriculture · US

Inventors

• David M. Donovan · Baltimore, US
• Igor V. Abaev · Наркевичі, UA
• Mathias Schmelcher · Wanderath, DE

Key dates

• Filing date: Sep 6, 2012
• Grant date: Mar 17, 2015
• Expiry date: Nov 26, 2032

Classification

• Technology area (CPC C): Chemistry; Metallurgy
• CPC primary: C12Y302/01017
• WIPO field: Biotechnology
• WIPO sector: Chemistry

Abstract

Methicillin-resistant (MRSA) and multi-drug resistant strains of Staphylococcus aureus are becoming increasingly prevalent in both human and veterinary clinics. S. aureus-causing bovine mastitis yields high annual losses to the dairy industry. Treatment of mastitis by broad range antibiotics is often not successful and may contribute to development of antibiotic resistance. Bacteriophage endolysins are a promising new source of antimicrobials. The endolysin of prophage φSH2 of Staphylococcus haemolyticus strain JCSC1435 (φSH2 lysin) shows lytic activity against live staphylococcal cells. Deletion constructs were tested in zymograms and turbidity reduction assays to evaluate the contribution of each functional module to lysis. The CHAP domain exhibited three-fold higher activity than the full length protein. Activity was further enhanced in the presence of bivalent calcium ions. The full length enzyme and the CHAP domain showed activity against multiple staphylococcal strains, including MRSA strains, mastitis isolates, and coagulase negative staphylococcal (CoNS) strains.