Institut de Biologie StructuraleGrenoble / France

Contacts relatifs à cet article / ROSSI Véronique

Defense collagens and immune response

The efficient elimination from the body of pathogens and altered self elements such as apoptotic cells (efferocytosis), is crucial for the anti-infectious defense and immune tolerance. Defense collagens, and in particular C1q, a soluble effector of innate immunity are very important actors of the maintenance of tolerance and play a central role in the recognition and phagocytosis of the elements that have to be eliminated. Phagocytosis involves the interaction of defense collagens with cellular receptors that are different according to the physiological context and modulate the production of cytokines towards an appropriate response (pro-inflammatory or anti-inflammatory), according to the danger signal that is recognized (pathogen or apoptotic cell). Our present work is focused on the study of the interaction of C1q with its phagocytic receptors using a multidisciplinary integrated approach combining
(a) protein engineering, biochemistry and structural biology, (b) functional imaging of the C1q-receptors complexes at the efferocytosis synapse using super resolution fluorescence microscopy and (c) cellular biology in order to analyze the interactions between apoptotic cells oposinized by C1q or its variants and the receptor on different type of phagocytes and examination of the consequences of these cells capture on immune tolerance.

Calreticulin Release at an Early Stage of Death Modulates the Clearance by Macrophages of Apoptotic Cells


Structures of parasite calreticulins provide insights into their flexibility and dual carbohydrate/peptide-binding properties


C1q protein engineering and elucidation of its recognition and complement activation properties

Recombinant C1q expression and identification of the interaction sites with its cognate proteases
Patent : Method for preparing C1q recombinant protein (N Thielens & I. Bally)


Structural and Functional Characterization of a Single-Chain Form of the Recognition Domain of Complement Protein C1q


Structural basis of the recognition versatility of ficolin-2

Human ficolin-2 recognition versatility extended : An update on the binding of ficolin-2 to sulfated/phosphated carbohydrates


Human L-Ficolin Recognizes Phosphocholine Moieties of Pneumococcal Teichoic Acid


Molecular and cellular characterization of the interaction of defense collagens with phagocytic receptors CR1/CD35 et LRP1/CD91

Deciphering Complement Receptor Type 1 Interactions with
Recognition Proteins of the Lectin Complement Pathway


Molecular dissection of the interaction of C1q with CD91



-  Institut des Sciences Biomédicales, Université du Chili, Santiago, Arturo FERREIRA
-  CRCINA (Centre de Recherche en Cancérologie et Immunologie Nantes-Angers), Angers, Equipe Innate immunity and Immunotherapy, Yves Delneste
-  IAB (Institut pour l’Avancée des Biosciences), Grenoble, Arnaud Millet
-  IBS, équipe PG (Groupe Pneumocoque), Grenoble, Anne-Marie Di Guilmi


-  Subvention d’échange ECOS-CONYCIT
-  ANR Piribio
-  ANR PRC - C1qEffero