Production of protegrin-1 with a matrix metalloproteinase/elastase cleavage site and its therapeutic potential for skin wound infections
Year: 2017
Type: dissertation
Abstract: Antibiotic-resistant infections are medically concerning due to their difficulty to control and associated rates of mortality. Methicillin-resistant Staphylococcus aureus (MRSA) is a drug-resistant microbe and a prominent cause of skin wound infections. Protegrin-1 (PG-1) is an antimicrobial peptide with a broad spectrum of activity against bacteria, including antibiotic-resistant strains, and therefore possesses promising therapeutic potential. A previous study demonstrated that PG-1 successfully reduced inflammation in mice with chemically-induced colitis. The current study sought to generate proform PG-1 (ProPG) for more efficient activation at sites of tissue inflammation using a recombinant approach. An MMP cleavage site was introduced into ProPG to allow for the more efficient release of mature PG-1 during skin inflammation. The expression vector was constructed and introduced into expression host Pichia pastoris. Fermentation parameters were optimized and efficient ProPG secretion was confirmed by Western blot. Future studies will verify ProPG therapeutic potential for combatting MRSA skin infections.
Author: Emily Hill
Language: English
Subfield: Microbiology
Field: Immunology and Microbiology
Domain: Life Sciences
Open Access status: green
OpenAlex ID: W2753467802