The structural peptidoglycan hydrolase gp181 of bacteriophage phiKZ.
Gp181 (2237 amino acids) of Pseudomonas aeruginosa bacteriophage phiKZ (Myoviridae) is a structural virion protein, which bears a peptidoglycan hydrolase domain near its C-terminus. This protein is supposed to degrade the peptidoglycan locally during the infection process. Nine deletional mutants allowed delineation of the peptidoglycan hydrolase domain between amino acids 1880-2042 (gp181M8) and analysis of its biochemical properties. Gp181M8 tolerates a high ionic strength (>320mM) and is less sensitive to long thermal treatments compared to the similar phiKZ endolysin. Gp181M8 lysed all tested outer membrane-permeabilized Gram-negative species. The C-terminal distal end (amino acids 2043-2237) enhances the specific activity of gp181M8 threefold, resulting in a twelve times higher activity than commercial hen egg white lysozyme. These biochemical properties suggest that this novel peptidoglycan hydrolase domain may be suitable for enzybiotic applications.
Briers
Yves
Y
Division of Gene Technology, Department of Biosystems, Katholieke Universiteit Leuven, Kasteelpark Arenberg 21, B-3001 Leuven, Belgium.
Miroshnikov
Konstantin
K
Chertkov
Oleg
O
Nekrasov
Alexei
A
Mesyanzhinov
Vadim
V
Volckaert
Guido
G
Lavigne
Rob
R
D002384:Catalysis; D003001:Cloning, Molecular; D004795:Enzyme Stability; D006868:Hydrolysis; D017900:Myoviridae / Q000201:enzymology*; D009238:N-Acetylmuramoyl-L-alanine Amidase / Q000737:chemistry* / Q000235:genetics; D009994:Osmolar Concentration; D010457:Peptidoglycan / Q000737:chemistry; D017434:Protein Structure, Tertiary; D017105:Pseudomonas Phages / Q000201:enzymology*; D011550:Pseudomonas aeruginosa / Q000821:virology*; D017384:Sequence Deletion; D013379:Substrate Specificity; D015678:Viral Structural Proteins / Q000737:chemistry* / Q000235:genetics
D010457:Peptidoglycan; D015678:Viral Structural Proteins; D009238:N-Acetylmuramoyl-L-alanine Amidase