Functional analysis of antibacterial activity of Bacillus amyloliquefaciens phage endolysin against Gram-negative bacteria.
To analyze the antibacterial activity of Bacillus amyloliquefaciens phage endolysin, nine deletion derivatives of the endolysin were constructed. Each deletion mutant was overexpressed, purified and characterized. The catalytic domain was located on the N-terminal region and the C-terminus had an affinity with the bacterial envelope. The enzymatic activity remained in spite of the deletion of the C-terminal 116-amino acid region; however, the antibacterial activity was lost. These results indicate that antibacterial action requires both the C-terminal cell-binding and the N-terminal enzymatic activities.
Morita
M
M
Department of Bioengineering, Tokyo Institute of Technology, 4259 Nagatsuta-cho, Midori-ku, Yokohama 226-8501, Japan.
Tanji
Y
Y
Orito
Y
Y
Mizoguchi
K
K
Soejima
A
A
Unno
H
H
D000900:Anti-Bacterial Agents; D000890:Anti-Infective Agents / Q000494:pharmacology*; D017103:Bacillus Phages / Q000737:chemistry* / Q000235:genetics; D001665:Binding Sites; D010450:Endopeptidases / Q000235:genetics / Q000378:metabolism / Q000494:pharmacology*; D017353:Gene Deletion; D006090:Gram-Negative Bacteria / Q000187:drug effects*; D008826:Microbial Sensitivity Tests; D009154:Mutation
D000900:Anti-Bacterial Agents; D000890:Anti-Infective Agents; D010450:Endopeptidases; C001143:endolysin