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J. Biol. Chem., Vol. 280, Issue 29, 26880-26885, July 22, 2005

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Amyloid Formation Modulates the Biological Activity of a Bacterial Protein^*

Sylvain Bieler, Lisbell Estrada, Rosalba Lagos¶, Marcelo Baeza¶, Joaquín Castilla, and Claudio Soto¶||

From the Department of Neurology, University of Texas Medical Branch, Galveston, Texas 77555, Department of Cell Biology, University of Geneva, CH-1211 Geneva 4, Switzerland, and ^¶Departamento de Biología, Universidad de Chile, Casilla 653, Santiago, Chile

The aggregation of proteins into amyloid fibrils is the hallmark feature of a group of late-onset degenerative diseases including Alzheimer, Parkinson, and prion diseases. We report here that microcin E492, a peptide naturally produced by Klebsiella pneumoniae that kills bacteria by forming pores in the cytoplasmic membrane, assembles in vitro into amyloid-like fibrils. The fibrils have the same structural, morphological, tinctorial, and biochemical properties as the aggregates observed in the disease conditions. In addition, we found that amyloid formation also occurs in vivo where it is associated with a loss of toxicity of the protein. The finding that microcin E492 naturally exists both as functional toxic pores and as harmless fibrils suggests that protein aggregation into amyloid fibrils is an evolutionarily conserved property of proteins that can be successfully employed by bacteria to fulfill specific physiological needs.

Received for publication, February 23, 2005 , and in revised form, May 24, 2005.

^* This work was supported in part by Grants FONDECYT 1020757 and 7020757 and National Institutes of Health Grants AG0224642 and NS549173. The costs of publication of this article were defrayed in part by the payment of page charges. This article must therefore be hereby marked "advertisement" in accordance with 18 U.S.C. Section 1734 solely to indicate this fact.

^|| To whom correspondence should be addressed. Tel.: 409-747-0017; Fax: 409-747-0020; E-mail: clsoto{at}utmb.edu.

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