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Gutierrez-Martinez, E.

Publications and source records attributed to Gutierrez-Martinez, E..

3 recordsLinked to original sources

The Rab32 small GTPase is required for efficient cross-priming of CD8+ T cellsagainst cell-associated antigens by XCR1+ type 1 DCs in vivo.

Type 1 conventional dendritic cells (cDC1s) are critical for initiating adaptive immune responses through the cross-priming of CD8 T cells against antigens from tumor or virus-infected cells. This function depends on specialized cross-presentation pathways that allow cDC1s to process phagocytosed cell debris and present peptide-MHC I complexes. In this study, we identify the small GTPase Rab32 as being highly and selectively over-expressed in cDC1s as compared to cDC2s. While cDC1s from Rab32-deficient mice develop normally and can respond to maturation signals, their capacity to activate CD8 T cells in vivo is impaired. Notably, Rab32- deficient cDC1s retain the ability to stimulate TCR transgenic CD8 T cells ex vivo using both cell-associated antigens and MHC I-binding peptides of varying affinity. However, in vivo, Rab32 is essential for effective CD8 T cell responses to cell-associated antigens, independent of Rab32 expression in T cells themselves. Importantly, Rab32-mediated cross-priming is required for the efficient expansion of tumor-specific CD8 T cells into solid tumors. These findings underscore a critical role for Rab32 in cDC1-mediated cross-priming, highlighting the contribution of non-antigen processing vesicular pathways in shaping CD8 T cell responses to cellular antigens.

immunology↗

Early steps of multi-receptor viral interactions dissected by high-density, multi-color single molecule mapping in living cells

Direct visualization of the early steps of multi-receptor viral interactions at the singlemolecule level has been largely impeded by the technical challenges associated to imaging individual multi-molecular systems at relevant spatial (nanometer) and temporal (millisecond) scales. Here, we present a four-color, high-density single-molecule spatiotemporal mapping methodology to capture real-time interactions between individual viruses and three different viral (co-)receptors on the membrane of living immune cells derived from donors. Together with quantitative tools, our approach revealed the existence of a coordinated spatiotemporal diffusion of the three different (co-)receptors prior to viral-engagement. By varying the temporal-windows of cumulated single-molecule localizations, we discovered that such a concerted diffusion impacts on the residence time of viruses on the host membrane and potential viral infectivity. Overall, our methodology opens a new door to the systematic analysis of the initial steps of viralhost interactions and paves the way to the investigation of other multi-molecular systems at the single-molecule level.

biophysics↗

Actin-regulated Siglec-1 nanoclustering influences HIV-1 capture and virus-containing compartment formation in dendritic cells

The immunoglobulin-like lectin receptor CD169 (Siglec-1) mediates the capture of HIV-1 by activated dendritic cells (DC) through binding to sialylated ligands. These interactions result in a more efficient virus capture as compared to resting DCs, although the underlying mechanisms are poorly understood. Using a combination of super-resolution microscopy, single particle tracking and biochemical perturbations we studied the nanoscale organization of Siglec-1 on activated DCs and its impact on viral capture and its trafficking to a single viral-containing compartment. We found that activation of DCs leads to Siglec-1 basal nanoclustering at specific plasma membrane regions where receptor diffusion is constrained by Rho-ROCK activation and formin-dependent actin polymerization. Using liposomes with varying ganglioside concentrations, we further demonstrate that Siglec-1 nanoclustering enhances the receptor avidity to limiting concentrations of gangliosides carrying sialic ligands. Binding to either HIV-1 particles or ganglioside-bearing liposomes lead to enhanced Siglec-1 nanoclustering and global actin rearrangements characterized by a drop in RhoA activity, facilitating the final accumulation of viral particles in a single sac-like compartment. Overall, our work provides new insights on the role of the actin machinery of activated DCs in regulating the formation of basal Siglec-1 nanoclustering, being decisive for the capture and actin-dependent trafficking of HIV-1 into the virus-containing compartment.

cell biology↗