Unraveling the human dendritic cell phagosome proteome by organellar enrichment ranking

Sonja I. Buschow, Edwin Lasonder, Radek Szklarczyk, Machteld M. Oud, I. Jolanda M. de Vries, Carl G. Figdor*

*Corresponding author for this work

Research output: Contribution to journalArticlepeer-review

25 Citations (Scopus)
14 Downloads (Pure)


Dendritic cells (DC) take up pathogens through phagocytosis and process them into protein and lipid fragments for presentation to T cells. So far, the proteome of the human DC phagosome, a detrimental compartment for antigen processing and presentation as well as for DC activation, remains largely uncharacterized. Here we have analyzed the protein composition of phagosomes from human monocyte-derived DC. For LC-MS/MS analysis we purified phagosomes from DC using latex beads targeted to DC-SIGN, and quantified proteins using a label-free method. We used organellar enrichment ranking (OER) to select proteins with a high potential to be relevant for phagosome function. The method compares phagosome protein abundance with protein abundance in whole DC. Phagosome enrichment indicates specific recruitment to the phagosome rather than co-purification or passive incorporation. Using OER we extracted the most enriched proteins that we further complemented with functionally associated proteins to define a set of 90 phagosomal proteins that included many proteins with established relevance on DC phagosomes as well as high potential novel candidates. We already experimentally confirmed phagosomal recruitment of Galectin-9, which has not been previously associated with phagocytosis, to both bead and pathogen containing phagosomes, suggesting a role for Galectin-9 in DC phagocytosis.

Original languageEnglish
Pages (from-to)1547-1562
Number of pages16
JournalJournal of Proteomics
Issue number5
Early online date3 Dec 2011
Publication statusPublished - 16 Feb 2012
Externally publishedYes


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