Open AccessCharacterization of the catalytic activity of the γ‐phage lysin, PlyG, specific for Bacillus anthracis
Author(s) -
Kikkawa Hitomi S.,
Ueda Takuya,
Suzuki Shinichi,
Yasuda Jiro
Publication year - 2008
Publication title -
fems microbiology letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.899
H-Index - 151
eISSN - 1574-6968
pISSN - 0378-1097
DOI - 10.1111/j.1574-6968.2008.01280.x
Subject(s) - bacillus anthracis , lysin , amidase , lysozyme , mutant , peptide sequence , chemistry , biology , biochemistry , bacteriophage , enzyme , escherichia coli , genetics , bacteria , gene
Bacillus anthracis causes anthrax, a lethal disease affecting humans that has attracted attention due to its bioterrorism potential. PlyG is a lysin of γ‐phage, which specifically infects B. anthracis and lyses its cell wall. PlyG contains a T7 lysozyme‐like amidase domain, which appears to be the catalytic domain, in the N‐terminal region and has a high degree of sequence similarity with PlyL, which is an N ‐acetylmuramoyl‐ l ‐alanine amidase encoded by the B. anthracis genome. Here, we demonstrated that two amino acid residues of PlyG, H29 and E90, are necessary for its catalytic activity in B. anthracis . These residues are structurally analogous to residues whose mutation in T7 lysozyme abolished its catalytic activity. A C‐terminal deletion mutant of PlyG lacking the core sequence for binding to B. anthracis showed completely abolished binding activity, unlike PlyL, despite high sequence similarity with PlyL in the N‐terminal region. This suggests that the C‐terminal binding domain, as well as the N‐terminal catalytic domain, is essential for the catalytic activity of PlyG. Our observations provide new insights into the mechanism of specific catalysis of PlyG in B. anthracis and may contribute to the establishment of new methods for anthrax therapy.