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Characterization of phosphoglycan-containing secretory products of Leishmania

Published online by Cambridge University Press:  06 April 2009

T. Ilg ,
Y.-D. Stierhof ,
M. Wiese ,
M. J. McConville  and
P. Overath
T. Ilg
Affiliation:
Max-Planck-Institut für Biologic, Abteilung Membranbiochemie Corrensstrasse 38, D72076 Tübingen, Germany
Y.-D. Stierhof
Affiliation:
Max-Planck-Institut für Biologic, Abteilung Membranbiochemie Corrensstrasse 38, D72076 Tübingen, Germany
M. Wiese
Affiliation:
Max-Planck-Institut für Biologic, Abteilung Membranbiochemie Corrensstrasse 38, D72076 Tübingen, Germany
M. J. McConville
Affiliation:
Department of Biochemistry, University of Dundee, Dundee DD1 4HN, UK
P. Overath
Affiliation:
Max-Planck-Institut für Biologic, Abteilung Membranbiochemie Corrensstrasse 38, D72076 Tübingen, Germany
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Summary

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.

Keywords

Leishmaniasecretionlipophosphoglycansecreted acid phosphataseproteo-high-molecular-weight phosphoglycanflagellar pocketparasitophorous vacuole.
Type
Research Article
Information
Parasitology , Volume 108 , supplement S1: Symposia of the British Society for Parasitology Volume 31:Functional molecules on the surface of protozoan parasites , March 1994 , pp. S63 - S71
Copyright
Copyright © Cambridge University Press 1994

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