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Biochem Biophys Res Commun. 2000 Jan 27;267(3):897-905.

The lipid component of lipoproteins from Borrelia burgdorferi: structural analysis, antigenicity, and presentation via human dendritic cells.

Author information

1
Institute of Anatomy, Division of Cell Biology, University of Zurich, Winterthurerstrasse 190, Zurich, CH-8057, Switzerland.

Abstract

The spirochaetal bacteria Borrelia burgdorferi (Bb) is the tick-borne causative agent of lyme disease. The major membrane immunogens of Bb are outer surface proteins. The lipid component of these lipoproteins is relevant for the immunogenicity of Bb-lipoproteins. To characterize the antigenic properties, the native lipid component of lipoproteins was isolated and the detailed molecular structure was analyzed. The molecular structure of the lipoprotein-lipid component turned out to be S(propane-2',-3'diol)-3-thio-2-aminopropanic acid (S-glyceryl-cysteine) with one ester-linked fatty acid, one acetyl group, and one N-terminal amide-bound fatty acid. Fatty acid analysis of the lipid component indicated a heterogeneous composition comprising C16:0, C18:0, C18:1, C18:2, and C 20:0. The antigenicity was tested with in vitro bioassays using human blood-derived dendritic cells (DCs) as antigen-presenting cells and autologous Bb-specific T-cells. We found that human DCs present the lipid component of Bb-lipoproteins via MHC class II inducing an antigen-specific T-cell immune response in vitro.

PMID:
10673388
DOI:
10.1006/bbrc.1999.2057
[Indexed for MEDLINE]

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