Discover Community Create You

Loading publication...

Noodle always counts identifier-free feature events for service operation. With your permission, Google Analytics can also estimate audience and engagement. Search text, publication identifiers, cookies, IP addresses and browser fingerprints are never included in Noodle's first-party event counters.

Privacy details

Article

Leishmania donovani lacking the Golgi GDP-Man transporter LPG2 exhibit attenuated virulence in mammalian hosts.

Experimental parasitology - 1 Jul 2009

Gaur Upasna, Showalter Melissa, Hickerson Suzanne, Dalvi Rahul, Turco Salvatore J, Wilson Mary E, Beverley Stephen M

Abstract excerpt

Surface phosophoglycans such as lipophosphoglycan (LPG) or proteophosphoglycan (PPG) and glycosylinositol phospholipids (GIPLs) modulate essential interactions between Leishmania and mammalian macrophages. Phosphoglycan synthesis depends on the Golgi GDP-mannose transporter encoded by LPG2. LPG2-null (lpg2(-)) Leishmania major cannot establish macrophage infections or induce acute pathology, whereas...

Read the complete abstract on PubMed

Topics

Share this publication in a Topic to start or enrich a Post.

Share to Complement System Proteins
Share to Gene Knockout Techniques

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Glycosphingolipids

Share to Leishmania donovani

Share to Leishmaniasis, Visceral

Share to Phagocytosis

Share to Phagosomes

Share to Respiratory Burst

Source

Open in PubMed Open full text

Identifiers

PMID: 19328787
DOI: 10.1016/j.exppara.2009.03.014
PMCID: PMC2720449

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-07.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Leishmania donovani lacking the Golgi GDP-Man transporter LPG2 exhibit attenuated virulence in mammalian hosts.PMID 19328787Read ↗

Comparisons of mutants lacking the Golgi UDP-galactose or GDP-mannose transporters establish that phosphoglycans are important for promastigote but not amastigote virulence in Leishmania major.Semantic proximity Read ↗

Identification of a compensatory mutant (lpg2-REV) of Leishmania major able to survive as amastigotes within macrophages without LPG2-dependent glycoconjugates and its significance to virulence and immunization strategies.Semantic proximity Read ↗

Glycosylation defects and virulence phenotypes of Leishmania mexicana phosphomannomutase and dolicholphosphate-mannose synthase gene deletion mutants.Semantic proximity Read ↗

Persistence without pathology in phosphoglycan-deficient Leishmania major.Semantic proximity Read ↗

The role(s) of lipophosphoglycan (LPG) in the establishment of Leishmania major infections in mammalian hosts.Semantic proximity Read ↗

Two Functionally Divergent UDP-Gal Nucleotide Sugar Transporters Participate in Phosphoglycan Synthesis in Leishmania majorSemantic proximity Read ↗

Phosphoglycan Repeat-deficient Leishmania mexicana Parasites Remain Infectious to Macrophages and MiceSemantic proximity Read ↗

Leishmania LPG3 encodes a GRP94 homolog required for phosphoglycan synthesis implicated in parasite virulence but not viability.Semantic proximity Read ↗

Defective galactofuranose addition in lipophosphoglycan biosynthesis in a mutant of Leishmania donovani.Semantic proximity Read ↗

Proteophosphoglycans of Leishmania mexicana. Molecular cloning and characterization of the Leishmania mexicana ppg2 gene encoding the proteophosphoglycans aPPG and pPPG2 that are secreted by amastigotes and promastigotes.Semantic proximity Read ↗

Disruption of mannose activation in Leishmania mexicana: GDP-mannose pyrophosphorylase is required for virulence, but not for viability.Semantic proximity Read ↗

Evidence that intracellular beta1-2 mannan is a virulence factor in Leishmania parasites.Semantic proximity Read ↗

⌁Select a neighboring publication to make it the new centre.