Characterization of phosphoglycan-containing secretory products of Leishmania

T Ilg, Y D Stierhof, M Wiese, M J McConville, P Overath

Research output: Contribution to journalArticle

59 Citations (Scopus)

Abstract

This article presents an overview on phosphoglycan-containing components secreted by the insect and mammalian stages of several species of Leishmania, the causative agents of leishmaniasis in the Old and New World. Firstly, promastigotes of all three species considered, L. mexicana, L. donovani and L. major, shed lipophosphoglycan (LPG) into the culture medium possibly by release of micelles from the cell surface. Like the cell-associated LPG, culture supernatant LPG is arhphiphilic and composed of a lysoalkylphosphatidylinositol-phosphosaccharide core connected to species-specific phosphosaccharide repeats and oligosaccharide caps. Secondly, all three species release hydrophilic phosphoglycan. Thirdly, all three species appear to secrete proteins covalently modified by phosphosaccharide repeats and oligosaccharide caps. In the case of promastigotes of L. mexicana, these components are organized as two filamentous polymers released from the flagellar pocket: the secreted acid phosphatase (sAP) composed of a 100 kDa phosphoglycoprotein and a protein- containing high-molecular-weight-phosphoglycan (proteo-HMWPG) and fibrous networks likewise composed of phosphoglycan possibly linked to protein. Structural analyses and gene cloning suggest that the parasites can covalently modify protein regions rich in serine and threonine residues by the attachment of phosphosaccharide repeats capped by oligosaccharides. We propose that the networks formed in vitro correspond to fibrous material previously demonstrated in the digestive tract of infected sandflies. In the case of L. donovani, the sAP is also modified by phosphoglycans but contains neither proteo-HMWPG nor does it aggregate to filaments. Finally, L. mexicana amastigotes release proteo-HMWPG via the flagellar pocket into the parasitophorous vacuole of infected macrophages. This material appears to be released into the tissue of the infected mammal upon rupture of infected macrophages during lesion development. This secretory product may contribute to the pathology of lesion development.

Original languageEnglish
Pages (from-to)S63-71
JournalParasitology
Volume108
Issue numberS1
DOIs
Publication statusPublished - Mar 1994

Fingerprint

Leishmania
Oligosaccharides
oligosaccharides
promastigotes
Cutaneous Leishmaniasis
Proteins
proteins
Molecular Weight
molecular weight
Acid Phosphatase
acid phosphatase
lesions (animal)
macrophages
Leishmania mexicana
Macrophages
amastigotes
Psychodidae
Leishmania donovani
Phlebotominae
leishmaniasis

Keywords

  • acid phosphatase
  • animals
  • carbohydrate sequence
  • glycosphingolipids
  • Leishmania
  • models, biological
  • molecular sequence data
  • polysaccharides
  • lipophosphoglycan
  • secreted acid phosphatase
  • proteo-high-molecular-weight phosphoglycan
  • flagellar pocket
  • parasitophorous vacuole
  • secretion

Cite this

Ilg, T ; Stierhof, Y D ; Wiese, M ; McConville, M J ; Overath, P. / Characterization of phosphoglycan-containing secretory products of Leishmania. In: Parasitology. 1994 ; Vol. 108, No. S1. pp. S63-71.
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Characterization of phosphoglycan-containing secretory products of Leishmania. / Ilg, T; Stierhof, Y D; Wiese, M; McConville, M J; Overath, P.

In: Parasitology, Vol. 108, No. S1, 03.1994, p. S63-71.

Research output: Contribution to journalArticle

TY - JOUR

T1 - Characterization of phosphoglycan-containing secretory products of Leishmania

AU - Ilg, T

AU - Stierhof, Y D

AU - Wiese, M

AU - McConville, M J

AU - Overath, P

PY - 1994/3

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N2 - This article presents an overview on phosphoglycan-containing components secreted by the insect and mammalian stages of several species of Leishmania, the causative agents of leishmaniasis in the Old and New World. Firstly, promastigotes of all three species considered, L. mexicana, L. donovani and L. major, shed lipophosphoglycan (LPG) into the culture medium possibly by release of micelles from the cell surface. Like the cell-associated LPG, culture supernatant LPG is arhphiphilic and composed of a lysoalkylphosphatidylinositol-phosphosaccharide core connected to species-specific phosphosaccharide repeats and oligosaccharide caps. Secondly, all three species release hydrophilic phosphoglycan. Thirdly, all three species appear to secrete proteins covalently modified by phosphosaccharide repeats and oligosaccharide caps. In the case of promastigotes of L. mexicana, these components are organized as two filamentous polymers released from the flagellar pocket: the secreted acid phosphatase (sAP) composed of a 100 kDa phosphoglycoprotein and a protein- containing high-molecular-weight-phosphoglycan (proteo-HMWPG) and fibrous networks likewise composed of phosphoglycan possibly linked to protein. Structural analyses and gene cloning suggest that the parasites can covalently modify protein regions rich in serine and threonine residues by the attachment of phosphosaccharide repeats capped by oligosaccharides. We propose that the networks formed in vitro correspond to fibrous material previously demonstrated in the digestive tract of infected sandflies. In the case of L. donovani, the sAP is also modified by phosphoglycans but contains neither proteo-HMWPG nor does it aggregate to filaments. Finally, L. mexicana amastigotes release proteo-HMWPG via the flagellar pocket into the parasitophorous vacuole of infected macrophages. This material appears to be released into the tissue of the infected mammal upon rupture of infected macrophages during lesion development. This secretory product may contribute to the pathology of lesion development.

AB - This article presents an overview on phosphoglycan-containing components secreted by the insect and mammalian stages of several species of Leishmania, the causative agents of leishmaniasis in the Old and New World. Firstly, promastigotes of all three species considered, L. mexicana, L. donovani and L. major, shed lipophosphoglycan (LPG) into the culture medium possibly by release of micelles from the cell surface. Like the cell-associated LPG, culture supernatant LPG is arhphiphilic and composed of a lysoalkylphosphatidylinositol-phosphosaccharide core connected to species-specific phosphosaccharide repeats and oligosaccharide caps. Secondly, all three species release hydrophilic phosphoglycan. Thirdly, all three species appear to secrete proteins covalently modified by phosphosaccharide repeats and oligosaccharide caps. In the case of promastigotes of L. mexicana, these components are organized as two filamentous polymers released from the flagellar pocket: the secreted acid phosphatase (sAP) composed of a 100 kDa phosphoglycoprotein and a protein- containing high-molecular-weight-phosphoglycan (proteo-HMWPG) and fibrous networks likewise composed of phosphoglycan possibly linked to protein. Structural analyses and gene cloning suggest that the parasites can covalently modify protein regions rich in serine and threonine residues by the attachment of phosphosaccharide repeats capped by oligosaccharides. We propose that the networks formed in vitro correspond to fibrous material previously demonstrated in the digestive tract of infected sandflies. In the case of L. donovani, the sAP is also modified by phosphoglycans but contains neither proteo-HMWPG nor does it aggregate to filaments. Finally, L. mexicana amastigotes release proteo-HMWPG via the flagellar pocket into the parasitophorous vacuole of infected macrophages. This material appears to be released into the tissue of the infected mammal upon rupture of infected macrophages during lesion development. This secretory product may contribute to the pathology of lesion development.

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KW - molecular sequence data

KW - polysaccharides

KW - lipophosphoglycan

KW - secreted acid phosphatase

KW - proteo-high-molecular-weight phosphoglycan

KW - flagellar pocket

KW - parasitophorous vacuole

KW - secretion

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