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Published online before print April 1, 2004

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© by The Society for Leukocyte Biology
Journal of Leukocyte Biology, doi:10.1189/jlb.1203656

Received for publication December 26, 2003.
Revised February 19, 2004.
Accepted for publication February 25, 2004.

Article

Identification of two immunogenic domains of the prion protein--PrP--which activate class II-restricted T cells and elicit antibody responses against the native molecule

Sylvie Gregoire ^*, Caroline Logre ^*, Pat Metharom ^*, Estelle Loing , Jacques Chomilier , Martine Bruley Rosset ^*, Pierre Aucouturier ^*, and Claude Carnaud ^*@

*INSERM E209, Hospital Saint-Antoine, Paris, France; SEDAC Therapeutics, Le Galenis, Loos, France; and Laboratory of Mineralogy-Crystallography, CNRS, University of Paris 6 and Paris 7, France

^@ To whom correspondence should be addressed. E-mail: carnaud{at}st-antoine.inserm.fr.

	Abstract

Recent reports suggest that immunity against the prion protein (PrP) retards transmissible spongiform encephalopathies progression in infected mice. A major obstacle to the development of vaccines comes from the fact that PrP is poorly immunogenic, as it is seen as self by the host immune system. Additional questions concern the immune mechanisms involved in protection and the risk of eliciting adverse reactions in the central nervous system of treated patients. Peptide-based vaccines offer an attractive strategy to overcome these difficulties. We have undertaken the identification of the immunogenic regions of PrP, which triggers helper T cells (Th) associated with antibody production. Our results identify two main regions, one between the structured and flexible portion of PrP (98-127) and a second between 1 and 2 helix (143-187). Peptides (30-mer) corresponding to these regions elicit class II-restricted Th cells and antibody production against native PrP and could therefore be of potential interest for a peptide-based vaccination.

Key Words: TSE • prion diseases • epitope mapping • peptide-based vaccine

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