Please use this identifier to cite or link to this item: http://hdl.handle.net/1822/37259

TitleThe first Paenibacillus larvae bacteriophage endolysin (PlyPl23) with high potential to control American foulbrood
Author(s)Oliveira, A.
Leite, Marta
Kluskens, Leon
Santos, Sílvio Roberto Branco
Melo, Luís D. R.
Azeredo, Joana
KeywordsBacteriophage
Endolysin
Paenibacillus larvae
Issue dateJul-2015
PublisherPublic Library of Science
JournalPLoS ONE
CitationOliveira, A.; Leite, M.; Kluskens, Leon; Santos, S.; Melo, L.; Azeredo, Joana, The first Paenibacillus larvae bacteriophage endolysin (PlyPl23) with high potential to control American foulbrood. PLoS One, 10(7), e0136331, 2015
Abstract(s)Endolysins, which are peptidoglycan-degrading enzymes expressed during the terminal stage of the reproduction cycle of bacteriophages, have great potential to control Gram-pos- itive pathogens. This work describes the characterization of a novel endolysin (PlyPl23) encoded on the genome of Paenibacillus larvae phage phiIBB_Pl23 with high potential to control American foulbrood. This bacterial disease, caused by P. larvae, is widespread in North America and Europe and causes important economic losses in apiculture. The restric- tion to antibiotic residues in honey imposed by the EU legislation hinders its therapeutic use to combat American foulbrood and enforces the development of alternative antimicrobial methods. The new endolysin described herein has an N-acetylmuramoyl-L-alanine ami- dase catalytic domain and exhibits a broad-spectrum activity against common P. larvae genotypes. Moreover, the enzyme displays high antimicrobial activity in a range of pH that matches environmental conditions (pH between 5.0 and 7.0), showing its feasible applica- tion in the field. At pH 7.0, a concentration of 0.2 M of enzyme was enough to lyse 104 CFU.mL-1 of P. larvae in no more than 2 h. The presence of sucrose and of the substances present in the larvae gut content did not affect the enzyme activity. Interestingly, an increase of activity was observed when PlyPl23 was previously incubated in royal jelly. Furthermore, in vivo safety evaluation assays demonstrated that this enzyme is not toxic to the bee lar- vae. The present work describes for the first time an endolysin encoded in a P. larvae phage that presents high potential to integrate a commercial product to control the problematic American foulbrood.
TypeArticle
URIhttp://hdl.handle.net/1822/37259
DOI10.1371/journal.pone.0132095
ISSN1932-6203
e-ISSN1932-6203
Publisher versionhttp://journals.plos.org/plosone/article?id=10.1371/journal.pone.0132095
Peer-Reviewedyes
AccessOpen access
Appears in Collections:CEB - Publicações em Revistas/Séries Internacionais / Publications in International Journals/Series

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