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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 #328638

Research Project: DEVELOPING GENETIC BIOTECHNOLOGIES FOR INCREASED FOOD ANIMAL PRODUCTION, INCLUDING NOVEL ANTIMICROBIALS FOR IMPROVED HEALTH & PRODUCT SAFETY

Location: Animal Biosciences & Biotechnology Laboratory

Title: Four phage endolysins that are lytic for clostridium perfringens

Author
item Rowley, Dayana
item OAKLEY, BRIAN - Western University Of Health Sciences
item Donovan, David
item Swift, Steven

Submitted to: Stem Cells and Development
Publication Type: Abstract Only
Publication Acceptance Date: 7/17/2016
Publication Date: N/A
Citation: N/A

Interpretive Summary:

Technical Abstract: Clostridium perfringens is a bacterial pathogen and the cause of necrotic enteritis in poultry, and a source of food poisoning and gas gangrene in people. C. perfringens can also cause mild to severe enteritis in pigs. In the EU, the occurrence of C. perfringens-associated necrotic enteritis in poultry has increased as antibiotic use has decreased. As the US moves away from use of antibiotics in animal feed, we may expect an increase in necrotic enteritis with subsequent losses from morbidity and, in subclinical cases, losses from morbidity as reflected in decreased chicken weight gain. For the purpose of maintaining animal production efficiency, alternatives to antibiotics in animal feed will be needed in the near future. The genomes of 43 unique Clostridium perfringens isolates from chicken were sequenced, examined for peptidoglycan hydrolase enzymes by homology to known enzymes. There were more than 120 putative peptidoglycan hydrolases identified that clustered into 15 groups according to homology [less than 50% amino acid identity between groups and more than 90% amino acid identity within group]. Of 15 representative lysins (one from each group) four lyins were shown to have high lytic activity against all 43 of the initial isolates in plate lysis assays but not other Gram positive or Gram negative species tested. Activity was also demonstrated in both zymogram, and turbidity reduction assays. One lysin was shown to have an internal translational start site producing two products when expressed in E. coli. The domain architecture and relative activity of the four lysins will be discussed.