Document Detail


Characterization of bacteriophages virulent for Clostridium perfringens and identification of phage lytic enzymes as alternatives to antibiotics for potential control of the bacterium.
MedLine Citation:
PMID:  23300321     Owner:  NLM     Status:  MEDLINE    
Abstract/OtherAbstract:
There has been a resurgent interest in the use of bacteriophages or their gene products to control bacterial pathogens as alternatives to currently used antibiotics. Clostridium perfringens is a gram-positive, spore-forming anaerobic bacterium that plays a significant role in human foodborne disease as well as non-foodborne human, animal, and avian diseases. Countries that have complied with the ban on antimicrobial growth promoters in feeds have reported increased incidences of C. perfringens-associated diseases in poultry. To address these issues, new antimicrobial agents, putative lysins encoded by the genomes of bacteriophages, are being identified in our laboratory. Poultry intestinal material, soil, sewage, and poultry processing drainage water were screened for virulent bacteriophages that could lyse C. perfringens and produce clear plaques in spot assays. Bacteriophages were isolated that had long noncontractile tails, members of the family Siphoviridae, and with short noncontractile tails, members of the family Podoviridae. Several bacteriophage genes were identified that encoded N-acetylmuramoyl-l-alanine amidases, lysozyme-endopeptidases, and a zinc carboxypeptidase domain that has not been previously reported in viral genomes. Putative phage lysin genes (ply) were cloned and expressed in Escherichia coli. The recombinant lysins were amidases capable of lysing both parental phage host strains of C. perfringens as well as other strains of the bacterium in spot and turbidity reduction assays, but did not lyse any clostridia beyond the species. Consequently, bacteriophage gene products could eventually be used to target bacterial pathogens, such as C. perfringens via a species-specific strategy, to control animal and human diseases without having deleterious effects on beneficial probiotic bacteria.
Authors:
Bruce S Seal
Publication Detail:
Type:  Journal Article; Research Support, N.I.H., Extramural; Research Support, Non-U.S. Gov't; Research Support, U.S. Gov't, Non-P.H.S.    
Journal Detail:
Title:  Poultry science     Volume:  92     ISSN:  0032-5791     ISO Abbreviation:  Poult. Sci.     Publication Date:  2013 Feb 
Date Detail:
Created Date:  2013-01-09     Completed Date:  2013-03-05     Revised Date:  2014-07-10    
Medline Journal Info:
Nlm Unique ID:  0401150     Medline TA:  Poult Sci     Country:  United States    
Other Details:
Languages:  eng     Pagination:  526-33     Citation Subset:  IM    
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MeSH Terms
Descriptor/Qualifier:
Animals
Carboxypeptidases / genetics,  metabolism
Chickens*
Clostridium Infections / microbiology,  therapy*,  virology
Clostridium perfringens / genetics,  virology*
Endopeptidases / genetics,  metabolism
Escherichia coli / genetics
Mucoproteins / chemistry,  genetics,  metabolism
N-Acetylmuramoyl-L-alanine Amidase / genetics,  metabolism
Phylogeny
Podoviridae / classification,  enzymology*,  genetics,  isolation & purification
Poultry Diseases / microbiology,  therapy*,  virology
Recombinant Proteins / chemistry,  genetics,  metabolism
Sequence Analysis, DNA / veterinary
Sequence Analysis, Protein / veterinary
Siphoviridae / classification,  enzymology*,  genetics,  isolation & purification
Viral Proteins / genetics,  metabolism
Grant Support
ID/Acronym/Agency:
1S10 RR023587-01A2/RR/NCRR NIH HHS; P20 GM103440/GM/NIGMS NIH HHS; P20 RR-016464/RR/NCRR NIH HHS; P20 RR016464/RR/NCRR NIH HHS
Chemical
Reg. No./Substance:
0/Mucoproteins; 0/Recombinant Proteins; 0/Viral Proteins; 0/lysin; EC 3.4.-/Carboxypeptidases; EC 3.4.-/Endopeptidases; EC 3.5.1.28/N-Acetylmuramoyl-L-alanine Amidase

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine


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