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Muralytic activity and modular structure of the endolysins of Pseudomonas aeruginosa bacteriophages φKZ and EL

(2007) MOLECULAR MICROBIOLOGY. 65(5). p.1334-1344
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Abstract
Pseudomonas aeruginosa bacteriophage endolysins KZ144 (phage phi KZ) and EL188 (phage EL) are highly lytic peptidoglycan hydrolases (210 000 and 390 000 units mg(-1)), active on a broad range of outer membrane-permeabilized Gram-negative species. Site-directed mutagenesis indicates E115 (KZ144)and E155 (EL188) as their respective essential catalytic residues. Remarkably, both endolysins have a modular structure consisting of an N-terminal substrate-binding domain and a predicted C-terminal catalytic module, a property previously only demonstrated in endolysins originating from phages infecting Gram-positives and only in an inverse arrangement. Both binding domains contain conserved repeat sequences, consistent with those of some peptidoglycan hydrolases of Gram-positive bacteria. Fusions of these domains with green fluorescent protein immediately label all outer membrane-permeabilized Gram-negative bacteria tested, isolated P. aeruginosa peptidoglycan and N-acetylated Bacillus subtilis peptidoglycan, demonstrating the broad range of peptidoglycan-binding capacity by these domains. Specifically, A1 chemotype pepticloglycan and fully N-acetylated glucosamine units are essential for binding. Both KZ144 and EL188 appear to be a natural chimeric enzyme, originating from a recombination of a cell wall-binding domain encoded by a Bacillus or Clostridium species and a catalytic domain of an unknown ancestor.
Keywords
WALL LYTIC ENZYME, BACILLUS-SUBTILIS 168, CELL-WALL, ESCHERICHIA-COLI, MUREIN HYDROLASES, PEPTIDOGLYCAN, PROTEIN, LYSIN, TRANSGLYCOSYLASE, LYSOZYME

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Chicago
Briers, Yves, Guido Volckaert, Anneleen Cornelissen, Stijn Lagaert, Chris W Michiels, Kirsten Hertveldt, and Rob Lavigne. 2007. “Muralytic Activity and Modular Structure of the Endolysins of Pseudomonas Aeruginosa Bacteriophages φKZ and EL.” Molecular Microbiology 65 (5): 1334–1344.
APA
Briers, Y., Volckaert, G., Cornelissen, A., Lagaert, S., Michiels, C. W., Hertveldt, K., & Lavigne, R. (2007). Muralytic activity and modular structure of the endolysins of Pseudomonas aeruginosa bacteriophages φKZ and EL. MOLECULAR MICROBIOLOGY, 65(5), 1334–1344.
Vancouver
1.
Briers Y, Volckaert G, Cornelissen A, Lagaert S, Michiels CW, Hertveldt K, et al. Muralytic activity and modular structure of the endolysins of Pseudomonas aeruginosa bacteriophages φKZ and EL. MOLECULAR MICROBIOLOGY. 2007;65(5):1334–44.
MLA
Briers, Yves, Guido Volckaert, Anneleen Cornelissen, et al. “Muralytic Activity and Modular Structure of the Endolysins of Pseudomonas Aeruginosa Bacteriophages φKZ and EL.” MOLECULAR MICROBIOLOGY 65.5 (2007): 1334–1344. Print.
@article{6846502,
  abstract     = {Pseudomonas aeruginosa bacteriophage endolysins KZ144 (phage phi KZ) and EL188 (phage EL) are highly lytic peptidoglycan hydrolases (210 000 and 390 000 units mg(-1)), active on a broad range of outer membrane-permeabilized Gram-negative species. Site-directed mutagenesis indicates E115 (KZ144)and E155 (EL188) as their respective essential catalytic residues. Remarkably, both endolysins have a modular structure consisting of an N-terminal substrate-binding domain and a predicted C-terminal catalytic module, a property previously only demonstrated in endolysins originating from phages infecting Gram-positives and only in an inverse arrangement. Both binding domains contain conserved repeat sequences, consistent with those of some peptidoglycan hydrolases of Gram-positive bacteria. Fusions of these domains with green fluorescent protein immediately label all outer membrane-permeabilized Gram-negative bacteria tested, isolated P. aeruginosa peptidoglycan and N-acetylated Bacillus subtilis peptidoglycan, demonstrating the broad range of peptidoglycan-binding capacity by these domains. Specifically, A1 chemotype pepticloglycan and fully N-acetylated glucosamine units are essential for binding. Both KZ144 and EL188 appear to be a natural chimeric enzyme, originating from a recombination of a cell wall-binding domain encoded by a Bacillus or Clostridium species and a catalytic domain of an unknown ancestor.},
  author       = {Briers, Yves and Volckaert, Guido and Cornelissen, Anneleen and Lagaert, Stijn and Michiels, Chris W and Hertveldt, Kirsten and Lavigne, Rob},
  issn         = {0950-382X},
  journal      = {MOLECULAR MICROBIOLOGY},
  keyword      = {WALL LYTIC ENZYME,BACILLUS-SUBTILIS 168,CELL-WALL,ESCHERICHIA-COLI,MUREIN HYDROLASES,PEPTIDOGLYCAN,PROTEIN,LYSIN,TRANSGLYCOSYLASE,LYSOZYME},
  language     = {eng},
  number       = {5},
  pages        = {1334--1344},
  title        = {Muralytic activity and modular structure of the endolysins of Pseudomonas aeruginosa bacteriophages \ensuremath{\phi}KZ and EL},
  url          = {http://dx.doi.org/10.1111/j.1365-2958.2007.05870.x},
  volume       = {65},
  year         = {2007},
}

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