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Updated: Jul 16, 2026

Measuring Phagosome pH by Ratiometric Fluorescence Microscopy
Published on: December 7, 2015
Rab27a regulates phagosomal pH and NADPH oxidase recruitment to dendritic cell phagosomes
Carolina Jancic1, Ariel Savina, Christina Wasmeier
1Institut Curie, INSERM U653, Immunité et Cancer, 26 rue d'Ulm, 75248 Paris, Cedex 05, France.
Abstract:
To prevent excessive degradation of internalized antigens, which could destroy the peptides recognized by T lymphocytes, dendritic cells have developed several strategies that limit proteolytic activity in phagosomes. The recruitment of the NADPH oxidase NOX2 prevents acidification of phagosomes, limiting antigen degradation. Here, we show that dendritic cells derived from Rab27a-deficient ashen mice show increased phagosome acidification and antigen degradation, causing a defect in antigen cross-presentation. Enhanced acidification results from a delay in the recruitment to phagosomes of a subset of lysosome-related organelles containing the membrane subunits of NOX2. The Rab27a-dependent recruitment of these "inhibitory lysosome-related organelles" to phagosomes continuously limits acidification and degradation of ingested particles in dendritic cells, thus promoting antigen cross-presentation.
Insights
Dendritic cells use Rab27a to recruit inhibitory organelles, limiting phagosome acidification and antigen degradation. This process is crucial for effective antigen cross-presentation to T lymphocytes.
Area of Science:
- Immunology
- Cell Biology
- Molecular Biology
Background:
- Dendritic cells (DCs) process antigens in phagosomes for T cell recognition.
- Excessive phagosome degradation can destroy T cell epitopes.
- NADPH oxidase NOX2 recruitment limits phagosome acidification and degradation.
Purpose of the Study:
- To investigate the role of Rab27a in regulating phagosome acidification and antigen degradation in DCs.
- To understand the mechanism by which DCs control proteolytic activity in phagosomes for antigen cross-presentation.
Main Methods:
- Utilized dendritic cells derived from Rab27a-deficient ashen mice.
- Analyzed phagosome acidification and antigen degradation levels.
- Investigated the recruitment dynamics of lysosome-related organelles containing NOX2 subunits to phagosomes.
Main Results:
- Rab27a-deficient DCs exhibit increased phagosome acidification and antigen degradation.
- This leads to a defect in antigen cross-presentation.
- Delayed recruitment of NOX2-containing organelles to phagosomes underlies enhanced acidification.
Conclusions:
- Rab27a-dependent recruitment of specific lysosome-related organelles to phagosomes is essential for limiting acidification.
- This mechanism continuously controls phagosome degradation in DCs, thereby promoting antigen cross-presentation.
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