11/11/19, Parc des Princes, rugby, équipe de Paris : [photographie de presse] / [Agence Rol]

Référence bibliographique : Rol, 56883

5-11-19, [MM. Clemenceau et Millerand] dans le port de Kehl : [photographie de presse] / [Agence Rol]

Référence bibliographique : Rol, 56812

13/11/19, affiches électorales [panneaux électoraux dans la rue pour les élections législatives du 16 novembre 1919] : [photographie de presse] / [Agence Rol]

Référence bibliographique : Rol, 56909

5-11-19, M. Clemenceau dans le fort de Kirchbach [avec M. Millerand] : [photographie de presse] / [Agence Rol]

Référence bibliographique : Rol, 56807

Structural determinants for membrane association and dynamic organization of the hepatitis C virus NS3-4A complex.

Hepatitis C virus (HCV) NS3-4A is a membrane-associated multifunctional protein harboring serine protease and RNA helicase activities. It is an essential component of the HCV replication complex and a prime target for antiviral intervention. Here, we show that membrane association and structural organization of HCV NS3-4A are ensured in a cooperative manner by two membrane-binding determinants. We demonstrate that the N-terminal 21 amino acids of NS4A form a transmembrane alpha-helix that may be involved in intramembrane protein-protein interactions important for the assembly of a functional replication complex. In addition, we demonstrate that amphipathic helix alpha(0), formed by NS3 residues 12-23, serves as a second essential determinant for membrane association of NS3-4A, allowing proper positioning of the serine protease active site on the membrane. These results allowed us to propose a dynamic model for the membrane association, processing, and structural organization of NS3-4A on the membrane. This model has implications for the functional architecture of the HCV replication complex, proteolytic targeting of host factors, and drug design.

1-11-19, Toussaint au Père Lachaise [cénotaphe de la ville de Paris à la mémoire des soldats morts pour la France] : [photographie de presse] / [Agence Rol]

Référence bibliographique : Rol, 56746

Dissecting TCR-MHC/peptide complex interactions with A2/peptide multimers incorporating tumor antigen peptide variants: crucial role of interaction kinetics on functional outcomes.

Soluble peptide/MHC-class-I (pMHC) multimers have recently emerged as unique reagents for the study of specific interactions between the pMHC complex and the TCR. Here, we assessed the relative binding efficiency of a panel of multimers incorporating single-alanine-substituted variants of the tumor-antigen-derived peptide MAGE-A10(254-262) to specific CTL clones displaying different functional avidity. For each individual clone, the efficiency of binding of multimers incorporating MAGE-A10 peptide variants was, in most cases, in good although not linear correlation with the avidity of recognition of the corresponding variant. In addition, we observed two types of discrepancies between efficiency of recognition and multimer binding. First, for some peptide variants, efficient multimer binding was detected in the absence of measurable effector functions. Some of these peptide variants displayed antagonist activity. Second, when comparing different clones we found clear discrepancies between the dose of peptide required to obtain half-maximal lysis in CTL assays and the binding efficiency of the corresponding multimers. These discrepancies, however, were resolved when the differential stability of the TCR/pMHC complexes was determined. For individual clones, decreased recognition correlated with increased TCR/pMHC off-rate. TCR/pMHC complexes formed by antagonist ligands displayed off-rates faster than those of TCR/pMHC complexes formed with weak agonists. In addition, when comparing different clones, the efficiency of multimer staining correlated better with relative multimer off-rates than with half-maximal lysis values. Altogether, the data presented here reconcile and extend our previous results on the impact of the kinetics of interaction of TCR with pMHC complexes on multimer binding and underline the crucial role of TCR/pMHC off-rates for the functional outcome of such interactions.

4/6/19, grévistes [des transports publics parisiens] au lac Daumesnil [Bois de Vincennes] : [photographie de presse] / [Agence Rol]

Référence bibliographique : Rol, 54236

4/6/19, grévistes [des transports publics parisiens] au lac Daumesnil [Bois de Vincennes] : [photographie de presse] / [Agence Rol]

Référence bibliographique : Rol, 54233

Lamoureux, 22/7/19 [présentant un drapeau tricolore où est inscrit : "honneur et patrie, oublier... jamais !"] : [photographie de presse] / [Agence Rol]

Référence bibliographique : Rol, 55118

5/6/19, grève des autobus [parisiens] : [photographie de presse] / [Agence Rol]

Référence bibliographique : Rol, 54249

5/6/19, grève des autobus [parisiens] : [photographie de presse] / [Agence Rol]

Référence bibliographique : Rol, 54248

5/6/19, grève des autobus [parisiens] : [photographie de presse] / [Agence Rol]

Référence bibliographique : Rol, 54247

5-11-19, M. Clemenceau sur le pont de Kehl : [photographie de presse] / [Agence Rol]

Référence bibliographique : Rol, 56817

Parc des Princes, 9/11/19, rugby, équipe de Nantes [battue par le Stade Français] : [photographie de presse] / [Agence Rol]

Référence bibliographique : Rol, 56858