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Review
. 2012 Sep 19:2:121.
doi: 10.3389/fcimb.2012.00121. eCollection 2012.

Leishmania promastigotes: building a safe niche within macrophages

Neda Moradin  1 , Albert Descoteaux
Affiliations
Review

Leishmania promastigotes: building a safe niche within macrophages

Neda Moradin et al. Front Cell Infect Microbiol. .

Abstract

Upon their internalization by macrophages, Leishmania promastigotes inhibit phagolysosome biogenesis. The main factor responsible for this inhibition is the promastigote surface glycolipid lipophosphoglycan (LPG). This glycolipid has a profound impact on the phagosome, causing periphagosomal accumulation of F-actin and disruption of phagosomal lipid microdomains. Functionally, this LPG-mediated inhibition of phagosome maturation is characterized by an impaired assembly of the NADPH oxidase and the exclusion of the vesicular proton-ATPase from phagosomes. In this chapter, we review the current knowledge concerning the nature of the intra-macrophage compartment in which Leishmania donovani promastigotes establish infection. We also describe how LPG enables this parasite to remodel the parasitophorous vacuole.

Keywords: Leishmania; lipophosphoglycan; macrophage; phagosome; virulence.

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Figures

Figure 1
Figure 1
Diagram illustrating inhibition of phagosome maturation induced by L. donovani promastigotes. Periphagosomal F-actin (red) accumulates, whereas promastigote-harboring phagosomes interact with early endosomes (tan). In contrast to amastigote-containing phagosomes, those harboring promastigotes interact poorly with late endosomes/lysosomes (purple). The V-ATPase is excluded from promastigote-phagosomes, contrasting with those containing amastigotes, which are acidic. Assembly of the NADPH oxidase is impaired in both types of phagosomes.
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