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Endolysins as antimicrobials.
Identification of a Broadly Active Phage Lytic Enzyme with Lethal Activity against Antibiotic-Resistant Enterococcus faecalis and Enterococcus faecium
PlyV12, a bacteriophage lytic enzyme, was isolated and shown to effectively kill both E. faecalis and E. Faecium, as well as other human pathogens, is proposed for development and use as an alternative therapeutic tool.
PlyC: a multimeric bacteriophage lysin.
- D. Nelson, R. Schuch, Peter Chahales, Shiwei Zhu, V. Fischetti
- BiologyProceedings of the National Academy of Sciences…
- 11 July 2006
A unique lysin from the streptococcal bacteriophage C(1), termed PlyC, is cloned and expressed, which defines a previously uncharacterized structural family of cell-wall hydrolases.
Purification and Characterization of Biofilm-Associated EPS Exopolysaccharides from ESKAPE Organisms and Other Pathogens
- Patrick M. Bales, Emilija Miljkovic Renke, Sarah L. May, Yang Shen, D. Nelson
- BiologyPloS one
- 21 June 2013
Methods to extract and purify high molecular weight exopolysaccharides from biofilms of eight human pathogens, including species of Staphylcococcus, Klebsiella, Acinetobacter, Pseudomonas, and a toxigenic strain of Escherichia coli O157:H7 are reported.
PlyPH, a Bacteriolytic Enzyme with a Broad pH Range of Activity and Lytic Action against Bacillus anthracis
PlyPH remains active between pH 4 and 10.5, and a single dose rescued a significant percentage of mice infected intraperitoneally with an attenuated B. anthracis strain, and is proposed as a novel therapeutic agent.
Removal of Group B Streptococci Colonizing the Vagina and Oropharynx of Mice with a Bacteriophage Lytic Enzyme
- Q. Cheng, D. Nelson, Shiwei Zhu, V. Fischetti
- Biology, MedicineAntimicrobial Agents and Chemotherapy
- 1 January 2005
A bacteriophage (phage) lytic enzyme to remove colonizing GBS and may be used to reduce vaginal GBS colonization in pregnant women before delivery or to decontaminate newborns, thus reducing the incidence of GBS-associated neonatal meningitis and sepsis.
X-ray crystal structure of the streptococcal specific phage lysin PlyC
The structural data reveal that PlyCA contains a glycoside hydrolase domain in addition to the previously recognized cysteine, histidine-dependent amidohydrolases/peptidases catalytic domain, which may explain the extraordinary potency of the PlyC holoenyzme toward target bacteria.
Cysteine proteinase SpeB from Streptococcus pyogenes – a potent modifier of immunologically important host and bacterial proteins
All known host and bacterial protein substrates for SpeB, their cleavage sites, and the role of this enzyme in streptococcal pathogenesis based on the current literature are reviewed.
Reinventing phage therapy: are the parts greater than the sum?
Although whole phage continue to generate interest as an alternative to antibiotics, focus is shifting to the use of purified phage components as antibacterial agents.
Rapid degradation of Streptococcus pyogenes biofilms by PlyC, a bacteriophage-encoded endolysin.
- Yang Shen, T. Köller, B. Kreikemeyer, D. Nelson
- Biology, MedicineThe Journal of antimicrobial chemotherapy
- 1 August 2013
It is indicated that while streptococcal cells within a biofilm rapidly become refractory to traditional antibiotics, the biofilm matrix is readily destroyed by the lytic actions of PlyC.