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ARS Home » Northeast Area » Beltsville, Maryland (BARC) » Beltsville Agricultural Research Center » Animal Biosciences & Biotechnology Laboratory » Research » Publications at this Location » Publication #260044

Title: Lysostaphin: molecular changes that preserve staphylolytic activity.

item Becker, Stephen
item Foster Frey, Juli
item Powell, Anne
item KERR, DAVID - University Of Vermont
item Donovan, David

Submitted to: Meeting Abstract
Publication Type: Proceedings
Publication Acceptance Date: 2/20/2011
Publication Date: N/A
Citation: N/A

Interpretive Summary: Brief explanation of the reason for, accomplishment of, and significance of the research in language intelligible to the general public. A. Problem— Mastitis causes the dairy industry in the USA over $2 billion in losses every year. Staphylococcus aureus is a notorious pathogen for both humans and animals, causing up to 40% of the bovine mastitis in the USA. There is a need for novel antimicrobials due to the high incidence of resistance development and multi-drug resistant strains of this pathogen. Lysostaphin is one such antimicrobial that has application to bovine mastitis and human staphylococcal disease. We have made numerous molecular changes to this staphylolytic protein. Many of these changes do alter its staphylolytic activity, but have never been reported in the literature. B. Accomplishment— This manuscript describes and characterizes numerous molecular changes to an important staphylolytic protein lysostaphin. C. Contribution of Accomplishment to Solving the Problem-- This report should help to inform others in the field of the molecular changes that can be made to lysostaphin that do not disrupt the staphylolytic activity of this important enzyme.

Technical Abstract: Lysostaphin is a potent staphylolytic enzyme with known resistance mechanisms. To avoid resistance development, this lab is developing lysostaphin-LysK fusion proteins harboring three synergistic lytic activities in one protein. Some of the molecular changes to lysostaphin and their effects on staphylolytic activity are described.