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Originally published In Press as doi:10.1074/mcp.M700391-MCP200 on January 9, 2008.
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Molecular & Cellular Proteomics 7:891-910, 2008.
© 2008 by The American Society for Biochemistry and Molecular Biology, Inc.

Research

Proteomics and Glycomics Analyses of N-Glycosylated Structures Involved in Toxoplasma gondii-Host Cell Interactions*,S

Sylvain Fauquenoy{ddagger}, Willy Morelle{ddagger}, Agnès Hovasse§, Audrey Bednarczyk§, Christian Slomianny, Christine Schaeffer§, Alain Van Dorsselaer§ and Stanislas Tomavo{ddagger},||

From the {ddagger} Unité de Glycobiologie Structurale et Fonctionnelle, CNRS UMR 8576, Université des Sciences et Technologies de Lille, 59655 Villeneuve d'Ascq, France, § Laboratoire de Spectrométrie de Masse Bioorganique, CNRS UMR 7178, Université Louis Pasteur, 67087 Strasbourg, France, and Laboratoire de Physiologie Cellulaire, INSERM U 800, Université des Sciences et Technologies de Lille, 59655 Villeneuve d'Ascq, France

The apicomplexan parasite Toxoplasma gondii recognizes, binds, and penetrates virtually any kind of mammalian cell using a repertoire of proteins released from late secretory organelles and a unique form of gliding motility (also named glideosome) that critically depends on actin filaments and myosin. How T. gondii glycosylated proteins mediate host-parasite interactions remains elusive. To date, only limited evidence is available concerning N-glycosylation in apicomplexans. Here we report comprehensive proteomics and glycomics analyses showing that several key components required for host cell-T. gondii interactions are N-glycosylated. Detailed structural characterization confirmed that N-glycans from T. gondii total protein extracts consist of oligomannosidic (Man5–8(GlcNAc)2) and paucimannosidic (Man3–4(GlcNAc)2) sugars, which are rarely present on mature eukaryotic glycoproteins. In situ fluorescence using concanavalin A and Pisum sativum agglutinin predominantly stained the entire parasite body. Visualization of Toxoplasma glycoproteins purified by affinity chromatography followed by detailed proteomics and glycan analyses identified components involved in gliding motility, moving junction, and other additional functions implicated in intracellular development. Importantly tunicamycin-treated parasites were considerably reduced in motility, host cell invasion, and growth. Collectively these results indicate that N-glycosylation probably participates in modifying key proteins that are essential for host cell invasion by T. gondii.

|| To whom correspondence should be addressed: Equipe de Parasitologie Moléculaire, Unité de Glycobiologie Structurale et Fonctionnelle, CNRS UMR 8576, Bâtiment C9, Université des Sciences et Technologies de Lille, 59655 Villeneuve d'Ascq, France. Tel.: 33-3-20-43-69-41; Fax: 33-3-20-33-65-55; E-mail: Stan.Tomavo{at}univ-lille1.fr


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Copyright © 2008 by the American Society for Biochemistry and Molecular Biology.