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Tropheryma whipplei , the agent of Whipple's disease, inhibits phago-lysosome biogenesis to create a suitable niche for its survival and replication in macrophages. To understand the mechanism by which it subverts phagosome maturation, we used biochemical and cell biological approaches to purify and characterise the intracellular compartment where  Tropheryma whipplei  resides using mouse bone-marrow-derived macrophages. We showed that in addition to Lamp-1, the  Tropheryma whipplei  phagosome is positive for Rab5 and Rab7, two GTPases required for the early to late phagosome transition. Unlike other pathogens, inhibition of PI(3)P production was not the mechanism for Rab5 stabilisation at the phagosome. Overexpression of the inactive, GDP-bound form of Rab5 bypassed the pathogen-induced blockade of phago-lysosome biogenesis. This suggests that  Tropheryma whipplei  blocks the switch from Rab5 to Rab7 by acting on the Rab5 GTPase cycle. A bio-informatic analysis of the  Tropheryma whipplei  genome revealed a glyceraldehyde-3-phosphate dehydrogenase (GAPDH) homologous with the GAPDH of  Listeria monocytogenes , and this may be the bacterial protein responsible for blocking Rab5 activity. To our knowledge,  Tropheryma whipplei  is the first pathogen described to induce a “chimeric” phagosome stably expressing both Rab5 and Rab7, suggesting a novel and specific mechanism for subverting phagosome maturation.

plos one

Tropheryma whipplei, the Agent of Whipple's Disease, Affects the Early to Late Phagosome Transition and Survives in a Rab5- and Rab7-Positive Compartment