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Structural basis of Toxoplasma gondii MIC2-associated protein interaction with MIC2.
Huynh, My-Hang; Liu, Bing; Henry, Maud; Liew, Lloyd; Matthews, Stephen J; Carruthers, Vern B.
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  • Huynh MH; From the Department of Microbiology and Immunology, University of Michigan Medical School, Ann Arbor, Michigan 48109 and.
  • Liu B; the Division of Molecular Biosciences, Imperial College London, South Kensington Campus, London SW7 2AZ, United Kingdom.
  • Henry M; the Division of Molecular Biosciences, Imperial College London, South Kensington Campus, London SW7 2AZ, United Kingdom.
  • Liew L; the Division of Molecular Biosciences, Imperial College London, South Kensington Campus, London SW7 2AZ, United Kingdom.
  • Matthews SJ; the Division of Molecular Biosciences, Imperial College London, South Kensington Campus, London SW7 2AZ, United Kingdom s.j.matthews@imperial.ac.uk.
  • Carruthers VB; From the Department of Microbiology and Immunology, University of Michigan Medical School, Ann Arbor, Michigan 48109 and vcarruth@umich.edu.
J Biol Chem ; 290(3): 1432-41, 2015 Jan 16.
Article en En | MEDLINE | ID: mdl-25411252
Toxoplasma gondii parasites must actively invade host cells to propagate. Secretory microneme proteins have been shown to be important for both gliding motility and active invasion. MIC2-M2AP is a protein complex that is essential for productive motility and rapid invasion by binding to host cell surface receptors. To investigate the architecture of the MIC2 and M2AP complex, we identified the minimal domains sufficient for interaction and solved the NMR solution structure of the globular domain of M2AP. We found that M2AP adopts a modified galectin fold similar to the C-terminal domain of another microneme protein, MIC1. NMR and immunoprecipitation analyses implicated hydrophobic residues on one face of the M2AP galectin fold in binding to the membrane proximal sixth thrombospondin type I repeat domain of MIC2. Our findings provide a second example of a galectin fold adapted for microneme protein-protein interactions and suggest a conserved strategy for the assembly and folding of diverse protein complexes.
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Texto completo: 1 Colección: 01-internacional Base de datos: MEDLINE Asunto principal: Toxoplasma / Proteínas Protozoarias / Proteínas de la Membrana Tipo de estudio: Prognostic_studies / Risk_factors_studies Límite: Animals / Humans Idioma: En Revista: J Biol Chem Año: 2015 Tipo del documento: Article Pais de publicación: Estados Unidos
Texto completo
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Texto completo: 1 Colección: 01-internacional Base de datos: MEDLINE Asunto principal: Toxoplasma / Proteínas Protozoarias / Proteínas de la Membrana Tipo de estudio: Prognostic_studies / Risk_factors_studies Límite: Animals / Humans Idioma: En Revista: J Biol Chem Año: 2015 Tipo del documento: Article Pais de publicación: Estados Unidos