Open AccessDifference in cholesterol‐binding and cytolytic activities between listeriolysin O and seeligeriolysin O: a possible role of alanine residue in tryptophan‐rich undecapeptide
Author(s) -
Ito Yutaka,
Kawamura Ikuo,
Kohda Chikara,
Baba Hisashi,
Kimoto Terumi,
Watanabe Isao,
Nomura Takamasa,
Mitsuyama Masao
Publication year - 2001
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.1574-6968.2001.tb10839.x
Subject(s) - listeriolysin o , hemolysis , hemolysin , cytolysin , recombinant dna , biochemistry , listeria monocytogenes , mutant , cytolysis , biology , toxin , tryptophan , chemistry , microbiology and biotechnology , cytotoxicity , listeria , in vitro , amino acid , bacteria , gene , genetics , virulence , immunology
We have constructed recombinant listeriolysin O (rLLO) and seeligeriolysin O (rLSO) from Listeria monocytogenes and Listeria seeligeri , respectively. In hemolysis and cholesterol‐binding assays, the specific activity of recombinant toxin was lower for LSO as compared to LLO. To understand the molecular basis of this difference, in particular with respect to the conserved Trp‐rich undecapeptide, a naturally occurring Ala to Phe substitution in LSO was introduced into rLLO. The rLLO:A488F hemolysin exhibited a reduced activity in both hemolysis and cholesterol‐binding. The reverse mutation, inserted into rLSO, also increased the hemolytic activity of this mutant LSO. These results suggested that the natural replacement of Ala to Phe is involved in the weak cytolytic activity of LSO.