Document Detail

Using a bacteriocin structure to engineer a phage lysin that targets Yersinia pestis.
MedLine Citation:
PMID:  23176506     Owner:  NLM     Status:  MEDLINE    
Purified phage lysins present an alternative to traditional antibiotics and work by hydrolysing peptidoglycan. Phage lysins have been developed against Gram-positive pathogens such as Bacillus anthracis and Streptococcus pneumoniae, where the peptidoglycan layer is exposed on the cell surface. Addition of the lysin to a bacterial culture results in rapid death of the organism. Gram-negative bacteria are resistant to phage lysins because they contain an outer membrane that protects the peptidoglycan from degradation. We solved crystal structures of a Yersinia pestis outer-membrane protein and the bacteriocin that targets it, which informed engineering of a bacterial-phage hybrid lysin that can be transported across the outer membrane to kill specific Gram-negative bacteria. This work provides a template for engineering phage lysins against a wide variety of bacterial pathogens.
Petra Lukacik; Travis J Barnard; Susan K Buchanan
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Publication Detail:
Type:  Journal Article; Research Support, N.I.H., Intramural    
Journal Detail:
Title:  Biochemical Society transactions     Volume:  40     ISSN:  1470-8752     ISO Abbreviation:  Biochem. Soc. Trans.     Publication Date:  2012 Dec 
Date Detail:
Created Date:  2012-11-26     Completed Date:  2013-05-09     Revised Date:  2013-07-11    
Medline Journal Info:
Nlm Unique ID:  7506897     Medline TA:  Biochem Soc Trans     Country:  England    
Other Details:
Languages:  eng     Pagination:  1503-6     Citation Subset:  IM    
National Institute of Diabetes and Digestive and Kidney Diseases, National Institutes of Health, Bethesda, MD 20892, USA.
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MeSH Terms
Anti-Bacterial Agents / chemistry*,  pharmacology
Bacterial Proteins / metabolism
Bacteriocins / chemistry*,  genetics
Bacteriophages / enzymology
Drug Design
Models, Molecular
Protein Conformation
Protein Engineering
Protein Structure, Secondary
Protein Structure, Tertiary
Receptors, Cell Surface / metabolism
Viral Proteins / chemistry*,  genetics,  pharmacology
Yersinia pestis / drug effects*,  metabolism
Grant Support
Reg. No./Substance:
0/Anti-Bacterial Agents; 0/Bacterial Proteins; 0/Bacteriocins; 0/FyuA protein, Yersinia; 0/Receptors, Cell Surface; 0/Viral Proteins

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