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Microbiology 147 (2001), 2679-2688
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Microbiology (2001), 147, 2679-2688.
© 2001 Society for General Microbiology

Genetics and Molecular Biology

Functional assembly of two membrane-binding domains in listeriolysin O, the cytolysin of Listeria monocytogenes

Iharilalao Dubail1, Nicolas Autret1, Jean-Luc Beretti1, Samer Kayal1, Patrick Berche1 and Alain Charbit1

Laboratoire de Microbiologie, INSERM U-411, Faculté de Médecine Necker-Enfants Malades, 156 rue de Vaugirard, 75730 Paris Cedex 15, France1

Author for correspondence: Alain Charbit. Tel: +33 1 40 61 53 76. Fax: +33 1 40 61 55 92. e-mail: charbit{at}necker.fr

Listeriolysin O (LLO) is a major virulence factor secreted by the pathogenic Listeria monocytogenes and acts as pore-forming cytolysin. Based on sequence similarities between LLO and perfringolysin (PFO), the cytolysin from Clostridium perfringens of known crystallographic structure, two truncated LLO proteins were produced: LLO-d123, comprising the first three predicted domains, and LLO-d4, the last C-terminal domain. The two proteins were efficiently secreted into the culture supernatant of L. monocytogenes and were able to bind to cell membranes. Strikingly, when expressed simultaneously, the two secreted domains LLO-d123 and LLO-d4 reassembled into a haemolytically active form. Two in-frame linker insertions were generated in the hinge region between the d123 and d4 domains. In both cases, the insertion created a major cleavage site for proteolytic degradation and abolished cytolytic activity, which might suggest that the region connecting d123 and d4 participates in the interaction between the two portions of the monomer.

Keywords: linker insertions, truncated proteins, domain interactions, LLO mutants

Abbreviations: HRBC, horse red blood cells; LLO, listeriolysin O; PFO, perfringolysin




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Copyright © 2001 Society for General Microbiology.