Team "innate immunity"

Objectives

To analyse the structures and to identify the molecular mechanisms involved in the early steps of innate immunity. To define the molecular bases of the recognition of pathogens, abnormal forms of proteins from self, and of apoptotic cells. To understand the molecular mechanisms of the activation of the NADPH oxidase complex involved in destruction of pathogens.

Topics

• Proteins of innate immunity : structure and function of the proteolytic complexes that trigger the classical and lectin pathways of complement
• Recognition of apoptotic cells by innate immunity proteins

Key words

Innate immunity - Complement - Molecular recognition - Lectins - Serine proteases - Apoptotic cells - Phagocytosis -

Specialized techniques

Protein sequencing - Amino acid analysis - Protein engineering – Surface plasmon resonance spectroscopy - Flow cytometry - Cell culture

Facilities available to outside users

Protein sequencing and amino acid analysis

Major publications

Païdassi, H., Tacnet-Delorme, P., Garlatti, V., Darnault, C., Ghebrehiwet, B., Gaboriaud, C., Arlaud, G. J. & Frachet, P. (2008) C1q binds phosphatidylserine and likely acts as a multiligand bridging molecule in apoptotic cell recognition. J. Immunol. 180, 2329-2338.

Garlatti, V., Belloy, N., Martin, L., Lacroix, M., Matsushita, M., Endo, Y., Fujita, T., Fontecilla-Camps, J.C., Arlaud, G.J., Thielens, N.M. & Gaboriaud, C. (2007) Structural insights into the innate immune recognition specificities of L- and H-ficolins. EMBO J. 26, 623-633.

Teillet, F., Dublet , B., Andrieu, J.P., Gaboriaud, C., Arlaud, G.J. & Thielens, N.M. (2005) The two major oligomeric forms of human mannan-binding lectin : chemical characterization, carbohydrate-binding properties and interaction with MBL-associated serine proteases. J. Immunol. 174, 2870-2877.

Gaboriaud, C., Juanhuix, J., Gruez, A., Lacroix, M., Darnault, C., Pignol, D., Verger, D., Fontecilla-Camps, J.C. & Arlaud, G.J. (2003) The crystal structure of the globular head of complement protein C1q provides a basis for its versatile recognition properties. J. Biol. Chem., 278, 46974-46982.

Budayova-Spano, M., Lacroix, M., Thielens, N.M., Arlaud, G.J., Fontecilla-Camps, J.C. & Gaboriaud C. (2002) The crystal structure of the zymogen catalytic domain of complement protease C1r reveals that a disruptive mechanical stress is required to trigger activation of the C1 complex. EMBO J. 21, 231-239.