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Infection and Immunity, March 2002, p. 1334-1341, Vol. 70, No. 3
0019-9567/02/$04.00+0     DOI: 10.1128/IAI.70.3.1334-1341.2002
Copyright © 2002, American Society for Microbiology. All Rights Reserved.

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

Chikara Kohda,1 Ikuo Kawamura,1 Hisashi Baba,1,2 Takamasa Nomura,1 Yutaka Ito,1 Terumi Kimoto,1 Isao Watanabe,1 and Masao Mitsuyama1*

Department of Microbiology, Kyoto University Graduate School of Medicine, Kyoto 606-8501,1 Department of Internal Medicine, Nagoya University School of Medicine, Nagoya 466-8550, Japan2

Received 29 August 2001/ Returned for modification 1 November 2001/ Accepted 15 December 2001

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.

* Corresponding author. Mailing address: Department of Microbiology, Kyoto University Graduate School of Medicine, Yoshidakonoe-cho, Sakyo-ku, Kyoto 606-8501, Japan. Phone: (81) 75-753-4441. Fax: (81) 75-753-4446. E-mail: mituyama{at}mb.med.kyoto-u.ac.jp.

Infection and Immunity, March 2002, p. 1334-1341, Vol. 70, No. 3
0019-9567/02/$04.00+0     DOI: 10.1128/IAI.70.3.1334-1341.2002
Copyright © 2002, American Society for Microbiology. All Rights Reserved.



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