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First published online July 1, 2009
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Macrophages respond to infection by phagocytosing microorganisms and sequestering them in phagosomes, which are vesicular bodies that undergo a progressive maturation process that culminates in the digestion of their contents. The acidification of phagosomes (a key step in their maturation) is mediated by the vacuolar-type ATPase (V-ATPase), which pumps protons into the phagosomal lumen – but how and when do phagosomes acquire V-ATPase? On page 2504, Yoh Wada and colleagues address this question. Using immunocytochemistry, the authors first show that a3, an isoform of the V-ATPase a-subunit that is associated with late endosomes and lysosomes, also localises to phagosomes. They next create mice that express an a3-GFP fusion protein, and show that, in macrophages, phagosomes receive a3-GFP from tubular lysosomal extensions located in the perinuclear region. Moreover, they show that nascent phagosomes acquire a3-GFP at an early stage in maturation. Importantly, the authors demonstrate that genetic inactivation of the a3 subunit results in impaired phagosomal acidification and bacteriocidal function. Their data shed light on V-ATPase dynamics in pathogen-infected macrophages, and on the sequence of events in phagosome maturation.
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