Dissociated Linkage of Cytokine-Inducing Activity and Cytotoxicity to Different Domains of Listeriolysin O from Listeria monocytogenes

Kohda, Chikara, Kawamura, Ikuo, Baba, Hisashi, Nomura, Takamasa, Ito, Yutaka, Kimoto, Terumi, Watanabe, Isao and Mitsuyama, Masao (2002) Dissociated Linkage of Cytokine-Inducing Activity and Cytotoxicity to Different Domains of Listeriolysin O from Listeria monocytogenes. Infection and Immunity, 70 3: 1334-1341. doi:10.1128/IAI.70.3.1334-1341.2002

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Author Kohda, Chikara
Kawamura, Ikuo
Baba, Hisashi
Nomura, Takamasa
Ito, Yutaka
Kimoto, Terumi
Watanabe, Isao
Mitsuyama, Masao
Title Dissociated Linkage of Cytokine-Inducing Activity and Cytotoxicity to Different Domains of Listeriolysin O from Listeria monocytogenes
Formatted title
Dissociated Linkage of Cytokine-Inducing Activity and Cytotoxicity to Different Domains of Listeriolysin O from Listeria monocytogenes
Journal name Infection and Immunity   Check publisher's open access policy
ISSN 0019-9567
1098-5522
Publication date 2002-03-01
Sub-type Article (original research)
DOI 10.1128/IAI.70.3.1334-1341.2002
Open Access Status File (Publisher version)
Volume 70
Issue 3
Start page 1334
End page 1341
Total pages 8
Place of publication Washington, DC, United States
Publisher American Society for Microbiology
Language eng
Formatted abstract
Listeriolysin O (LLO), a cholesterol-binding cytolysin of Listeria monocytogenes, exhibits cytokine-inducing and cytolytic activities. Because the cytolytic activity was abolished by cholesterol treatment but the cytokine-inducing activity was not, these activities appeared to be linked to different domains of the LLO molecule. In this study, we constructed recombinant full-length LLO (rLLO529) and various truncated derivatives and examined their cytolytic, cholesterol-binding, and gamma interferon (IFN-{gamma})-inducing activities. rLLO529 exhibited both IFN-{gamma}-inducing and cytolytic activities. Four truncated rLLOs possessing different C termini, which did not exert either cytolytic or cholesterol-binding activity, stimulated IFN-{gamma} production in normal spleen cells. However, a truncated rLLO corresponding to domain 4 (rLLO416-529) did not exhibit IFN-{gamma}-inducing activity, whereas it did bind to immobilized cholesterol. In addition, though the hemolysis induced by rLLO529 was inhibited by rLLO416-529, such inhibition was not detected upon rLLO529-induced IFN-{gamma} production. These data indicated that domain 4 was responsible for binding of LLO to membrane cholesterol followed by oligomerization and pore formation by the entire LLO molecule. In contrast, the other part of LLO, corresponding to domain 1-3, was essential for IFN-{gamma}-inducing activity. These findings implied a novel aspect of the function of LLO as a bacterial modulin.
Q-Index Code C1
Q-Index Status Provisional Code
Institutional Status Non-UQ

Document type: Journal Article
Sub-type: Article (original research)
Collections: Excellence in Research Australia (ERA) - Collection
School of Medicine Publications
 
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Created: Wed, 08 Apr 2009, 22:41:02 EST by Juliette Grosvenor on behalf of Anaesthesiology and Critical Care - RBWH