TY  - JOUR
A1  - Moll, Heidrun
A1  - Röllinghoff, Martin
T1  - T-cell reactivity to purified lipophosphoglycan from Leishmania major: A model for analysis of the cellular immune response to microbial carbohydrates.
N2  - The major macromolecule on the surface o/Leishmania majorpromastigotes is a lipophosphoglycan (LPG). This glycoconjugate plays a key role in determining infectivity and survival of para-sites in the mammalian host cell. In addition, L. major LPG is able to induce a host-protective immune response. In this article, we summarise the evidence for recognition of highly purified LPG by T cells and we discuss the potential mechanisms of T-cell Stimulation by this non-protein antigen.
KW  - Leishmania
KW  - T lymphocytes
KW  - glycosyl phosphatidyl-inostitols.
Y1  - 1991
U6  - http://nbn-resolving.de/urn/resolver.pl?urn:nbn:de:bvb:20-opus-33022
ER  - 
TY  - JOUR
A1  - Cull, Benjamin
A1  - Lima Prado Godinho, Joseane
A1  - Fernandes Rodrigues, Juliany Cola
A1  - Frank, Benjamin
A1  - Schurigt, Uta
A1  - Williams, Roderick AM
A1  - Coombs, Graham H
A1  - Mottram, Jeremy C
T1  - Glycosome turnover in Leishmania major is mediated by autophagy
JF  - Autophagy
N2  - Autophagy is a central process behind the cellular remodeling that occurs during differentiation of Leishmania, yet the cargo of the protozoan parasite's autophagosome is unknown. We have identified glycosomes, peroxisome-like organelles that uniquely compartmentalize glycolytic and other metabolic enzymes in Leishmania and other kinetoplastid parasitic protozoa, as autophagosome cargo. It has been proposed that the number of glycosomes and their content change during the Leishmania life cycle as a key adaptation to the different environments encountered. Quantification of RFP-SQL-labeled glycosomes showed that promastigotes of L. major possess ~20 glycosomes per cell, whereas amastigotes contain ~10. Glycosome numbers were significantly greater in promastigotes and amastigotes of autophagy-defective L. major Δatg5 mutants, implicating autophagy in glycosome homeostasis and providing a partial explanation for the previously observed growth and virulence defects of these mutants. Use of GFP-ATG8 to label autophagosomes showed glycosomes to be cargo in ~15% of them; glycosome-containing autophagosomes were trafficked to the lysosome for degradation. The number of autophagosomes increased 10-fold during differentiation, yet the percentage of glycosome-containing autophagosomes remained constant. This indicates that increased turnover of glycosomes was due to an overall increase in autophagy, rather than an upregulation of autophagosomes containing this cargo. Mitophagy of the single mitochondrion was not observed in L. major during normal growth or differentiation; however, mitochondrial remnants resulting from stress-induced fragmentation colocalized with autophagosomes and lysosomes, indicating that autophagy is used to recycle these damaged organelles. These data show that autophagy in Leishmania has a central role not only in maintaining cellular homeostasis and recycling damaged organelles but crucially in the adaptation to environmental change through the turnover of glycosomes.
KW  - ATG8
KW  - Leishmania
KW  - TEM
KW  - glycosome
KW  - protozoan parasite
KW  - ATG
KW  - autophagy-related
KW  - GFP
KW  - green fluorescent protein
KW  - MVT
KW  - multivesicular tubule
KW  - RFP
KW  - red fluorescent protein
KW  - transmission electron microscopy
KW  - adaptation
KW  - autophagy
KW  - mC
KW  - mCherry
KW  - fluorescent protein
Y1  - 2014
U6  - http://nbn-resolving.de/urn/resolver.pl?urn:nbn:de:bvb:20-opus-150277
VL  - 10
IS  - 12
ER  -