ArticleJournal of agricultural and food chemistry2010
Recombinant expression of two bacteriophage proteins that lyse clostridium perfringens and share identical sequences in the C-terminal cell wall binding domain of the molecules but are dissimilar in their N-terminal active domains.
Article in Journal of agricultural and food chemistry, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 23 papers.
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Who cites it
23 citing papers in PubMed, 40 citations in OpenAlex.
- Morphological and complete genome analysis of a novelFrontiers in pharmacology · 2026Article
- High lytic activity of endolysin LysDCp1 from phage DCp1 against Clostridium perfringens and biofilms.Veterinary research communications · 2025Article
- Characterization of aFrontiers in veterinary science · 2024Article
- Novel recombinant endolysin ointment with broad antimicrobial activity against methicillin-resistant Staphylococcus aureus isolated from wounds and burns.Archives of microbiology · 2023Article
- AmiP from hyperthermophilic Thermus parvatiensis prophage is a thermoactive and ultrathermostable peptidoglycan lytic amidase.Protein science : a publication of the Protein Society · 2023Article
- Characterization and Genomic Analysis of a Novel Lytic Phage DCp1 againstInternational journal of molecular sciences · 2023Article
- Novel Lytic Enzyme of Prophage Origin fromInternational journal of molecular sciences · 2021Article
- Phage lysin that specifically eliminates Clostridium botulinum Group I cells.Scientific reports · 2020Article
- Optimized production of a biologically active Clostridium perfringens glycosyl hydrolase phage endolysin PlyCP41 in plants using virus-based systemic expression.BMC biotechnology · 2019Article
- Thermophile Lytic Enzyme Fusion Proteins that TargetAntibiotics (Basel, Switzerland) · 2019Article
- Formation of therapeutic phage cocktail and endolysin to highly multi-drug resistantIranian journal of basic medical sciences · 2018Article
- Plant-expressed bacteriophage lysins control pathogenic strains of Clostridium perfringens.Scientific reports · 2018Article
- Whole genome analysis reveals the diversity and evolutionary relationships between necrotic enteritis-causing strains of Clostridium perfringens.BMC genomics · 2018Article
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- Expression and delivery of an endolysin to combat Clostridium perfringens.Applied microbiology and biotechnology · 2014Article
- Expression of a Clostridium perfringens genome-encoded putative N-acetylmuramoyl-L-alanine amidase as a potential antimicrobial to control the bacterium.Archives of microbiology · 2013Article
- Characterization of bacteriophages virulent for Clostridium perfringens and identification of phage lytic enzymes as alternatives to antibiotics for potential control of the bacterium.Poultry science · 2013Article
- Learning from bacteriophages - advantages and limitations of phage and phage-encoded protein applications.Current protein & peptide science · 2012Review
- Bacteriophage endolysins as novel antimicrobials.Future microbiology · 2012Review
Corrections and comments
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Authors and funding
4 authors at 2 institutions in 1 country.
Funding
Abstract
Clostridium perfringens is a Gram-positive anaerobic spore-forming bacterium capable of producing four major toxins that are responsible for disease symptoms and pathogenesis in a variety of animals, humans, and poultry. The organism is the third leading cause of human foodborne bacterial disease, and C. perfringens is the presumptive etiologic agent of necrotic enteritis among chickens, which in the acute form can cause increased mortality among broiler flocks. Countries that have complied with the ban on antimicrobial growth promoters (AGP) in feeds have had increased incidences of C. perfringens-associated necrotic enteritis in poultry. To address this issue, new antimicrobial agents, putative lysins from the genomes of bacteriophages, are identified. Two putative phage lysin genes (ply) from the clostridial phages phiCP39O and phiCP26F were cloned and expressed in Escherichia coli , and the resultant proteins were purified to near homogeneity. Gene and protein sequencing revealed that the predicted and chemically determined amino acid sequences of the two recombinant proteins were homologous to N-acetylmuramoyl-l-alanine amidases. The proteins were identical in the C-terminal putative cell-wall binding domain, but only 55% identical to each other in the presumptive N-terminal catalytic domain. Both recombinant lysins were 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. The observed reduction in turbidity was correlated with up to a 3 log cfu/mL reduction in viable C. perfringens on brain-heart infusion agar plates. However, other member species of the clostridia were resistant to the lytic activity by both assays.
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