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Leishmania promastigotes: building a safe niche within macrophages

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Moradin, Neda, Descoteaux, Albert·2012·Frontiers in Cellular and Infection Microbiology
DOI 10.3389/fcimb.2012.00121PMC PMC3445913
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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.

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  • Leishmania promastigotes cripple the microbicidal power of the phagosome, rendering it a propitious parasitophorous vacuole for the parasite.

    “Leishmania promastigotes are able to cripple the microbicidal power of the phagosome, rendering it a propitious parasitophorous vacuole (PV) for the parasite (105, 106).”

    From Macrophage Cytokines: Involvement in Immunity and Infectious Diseases (2014) · cites this paper as [105]

    The Abstract and “Arrested phagosome maturation by promastigotes” describe how promastigotes impair microbicidal functions and remodel their parasitophorous vacuoles. The Concluding remark says this creates an environment that *may* be propitious to differentiation; the citing sentence presents that benefit as established. Page numbers are not available in our copy. (LLM, conf=0.86)

    Experimental — accuracy not yet measured

  • GP63 is a multifaceted Leishmania pathogenicity factor and one of the most abundant molecules on the surface of promastigotes.

    “The GP63 zinc metalloprotease is a multifaceted Leishmania pathogenicity factor and is also one of the most abundant molecules on the surface of promastigotes (105, 108, 109).”

    From Macrophage Cytokines: Involvement in Immunity and Infectious Diseases (2014) · cites this paper as [105]

    The section “Promastigote-induced phagosome remodeling requires lipophosphoglycan” (page unavailable) describes LPG as an abundant promastigote surface glycoconjugate, not GP63. Searches for “GP63” and “metalloprotease” found no passage in our copy addressing GP63’s pathogenic roles or surface abundance. (LLM, conf=0.75)

    Experimental — accuracy not yet measured

  • GP63 can cleave members of the SNARE complex.

    “Of particular note is the capacity of GP63 to cleave members of the SNARE complex (105), which raises the possibility that GP63 may cleave other membrane fusion regulators.”

    From Macrophage Cytokines: Involvement in Immunity and Infectious Diseases (2014) · cites this paper as [105]

    The section “The impact of lipophosphoglycan on phagosome properties” discusses LPG disrupting lipid microdomains and excluding synaptotagmin V from phagosomes. Searches for GP63 and SNARE cleavage found no passage in our copy stating that GP63 cleaves SNARE-complex members. (LLM, conf=0.75)

    Experimental — accuracy not yet measured

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Cited by

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Authors
Moradin, N., & Descoteaux, A.
Affiliations
Institut National de la Recherche Scientifique (CA)
Corresponding author
Descoteaux, Albert
ORCID
Descoteaux, Albert
Venue
Frontiers in Cellular and Infection Microbiology
Publisher
Frontiers Media SA
Published
2012
Volume
2
Issue
2
Pages
121-121
ISSN
2235-2988 (ISSN-L)
DOI
10.3389/fcimb.2012.00121
PMC
PMC3445913
OpenAlex
W2001153614
Cited by
157
References
2
Citations by year
2026: 5 · 2025: 11 · 2024: 8 · 2023: 12 · 2022: 14 · 2021: 17 · 2020: 14 · 2019: 24 · 2018: 6 · 2017: 14 · 2016: 11 · 2015: 7 · 2014: 10 · 2013: 4
FWCI
1.05
Type
journal article
Language
en
Open access
Licence
cc-by
Locations
  • Frontiers in Cellular and Infection Microbiology (publishedVersion, cc-by)
  • PubMed Central (publishedVersion)
  • PubMed (publishedVersion)
  • EspaceINRS (National Institute for Scientific Research (Canada)) (submittedVersion)
  • HAL (submittedVersion)
  • DOAJ (DOAJ: Directory of Open Access Journals) (submittedVersion, cc-by-sa)
Funders
  • Armand-Frappier Foundation
  • Canada Research Chairs
  • Canadian Institutes of Health Research (MOP-12933)
Topics
  • Health Sciences › Medicine › Public Health, Environmental and Occupational Health › Research on Leishmaniasis Studies
  • Health Sciences › Medicine › Infectious Diseases › Leprosy Research and Treatment
  • Health Sciences › Medicine › Physiology › Histiocytic Disorders and Treatments
Keywords
Leishmania promastigotes, Leishmania donovani, macrophages, lipophosphoglycan, phagolysosome biogenesis, phagosome maturation, parasitophorous vacuole, NADPH oxidase, F-actin, lipid rafts, host-pathogen interaction
MeSH terms
Animals, Proton-Translocating ATPases, Humans, Leishmania donovani, Macrophages, Phagosomes, NADPH Oxidases, Host-Pathogen Interactions

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