The glycosylphosphatidylinositol-PLC in Trypanosoma brucei forms a linear array on the exterior of the flagellar membrane before and after activation.

Bloodstream forms of Trypanosoma brucei contain a glycosylphosphatidylinositol-specific phospholipase C (GPI-PLC) that cleaves the GPI-anchor of the variable surface glycoprotein (VSG). Its location in trypanosomes has been controversial. Here, using confocal microscopy and surface labelling techniq...

Descripción completa

Guardado en:
Detalles Bibliográficos
Autores principales: Orla Hanrahan, Helena Webb, Robert O'Byrne, Elaine Brabazon, Achim Treumann, Jack D Sunter, Mark Carrington, H Paul Voorheis
Formato: article
Lenguaje:EN
Publicado: Public Library of Science (PLoS) 2009
Materias:
Acceso en línea:https://doaj.org/article/bc4fdc332f5d4bddbd0b037ccf2aa5d3
Etiquetas: Agregar Etiqueta
Sin Etiquetas, Sea el primero en etiquetar este registro!
id oai:doaj.org-article:bc4fdc332f5d4bddbd0b037ccf2aa5d3
record_format dspace
spelling oai:doaj.org-article:bc4fdc332f5d4bddbd0b037ccf2aa5d32021-11-25T05:47:51ZThe glycosylphosphatidylinositol-PLC in Trypanosoma brucei forms a linear array on the exterior of the flagellar membrane before and after activation.1553-73661553-737410.1371/journal.ppat.1000468https://doaj.org/article/bc4fdc332f5d4bddbd0b037ccf2aa5d32009-06-01T00:00:00Zhttps://www.ncbi.nlm.nih.gov/pmc/articles/pmid/19503825/?tool=EBIhttps://doaj.org/toc/1553-7366https://doaj.org/toc/1553-7374Bloodstream forms of Trypanosoma brucei contain a glycosylphosphatidylinositol-specific phospholipase C (GPI-PLC) that cleaves the GPI-anchor of the variable surface glycoprotein (VSG). Its location in trypanosomes has been controversial. Here, using confocal microscopy and surface labelling techniques, we show that the GPI-PLC is located exclusively in a linear array on the outside of the flagellar membrane, close to the flagellar attachment zone, but does not co-localize with the flagellar attachment zone protein, FAZ1. Consequently, the GPI-PLC and the VSG occupy the same plasma membrane leaflet, which resolves the topological problem associated with the cleavage reaction if the VSG and the GPI-PLC were on opposite sides of the membrane. The exterior location requires the enzyme to be tightly regulated to prevent VSG release under basal conditions. During stimulated VSG release in intact cells, the GPI-PLC did not change location, suggesting that the release mechanism involves lateral diffusion of the VSG in the plane of the membrane to the fixed position of the GPI-PLC.Orla HanrahanHelena WebbRobert O'ByrneElaine BrabazonAchim TreumannJack D SunterMark CarringtonH Paul VoorheisPublic Library of Science (PLoS)articleImmunologic diseases. AllergyRC581-607Biology (General)QH301-705.5ENPLoS Pathogens, Vol 5, Iss 6, p e1000468 (2009)
institution DOAJ
collection DOAJ
language EN
topic Immunologic diseases. Allergy
RC581-607
Biology (General)
QH301-705.5
spellingShingle Immunologic diseases. Allergy
RC581-607
Biology (General)
QH301-705.5
Orla Hanrahan
Helena Webb
Robert O'Byrne
Elaine Brabazon
Achim Treumann
Jack D Sunter
Mark Carrington
H Paul Voorheis
The glycosylphosphatidylinositol-PLC in Trypanosoma brucei forms a linear array on the exterior of the flagellar membrane before and after activation.
description Bloodstream forms of Trypanosoma brucei contain a glycosylphosphatidylinositol-specific phospholipase C (GPI-PLC) that cleaves the GPI-anchor of the variable surface glycoprotein (VSG). Its location in trypanosomes has been controversial. Here, using confocal microscopy and surface labelling techniques, we show that the GPI-PLC is located exclusively in a linear array on the outside of the flagellar membrane, close to the flagellar attachment zone, but does not co-localize with the flagellar attachment zone protein, FAZ1. Consequently, the GPI-PLC and the VSG occupy the same plasma membrane leaflet, which resolves the topological problem associated with the cleavage reaction if the VSG and the GPI-PLC were on opposite sides of the membrane. The exterior location requires the enzyme to be tightly regulated to prevent VSG release under basal conditions. During stimulated VSG release in intact cells, the GPI-PLC did not change location, suggesting that the release mechanism involves lateral diffusion of the VSG in the plane of the membrane to the fixed position of the GPI-PLC.
format article
author Orla Hanrahan
Helena Webb
Robert O'Byrne
Elaine Brabazon
Achim Treumann
Jack D Sunter
Mark Carrington
H Paul Voorheis
author_facet Orla Hanrahan
Helena Webb
Robert O'Byrne
Elaine Brabazon
Achim Treumann
Jack D Sunter
Mark Carrington
H Paul Voorheis
author_sort Orla Hanrahan
title The glycosylphosphatidylinositol-PLC in Trypanosoma brucei forms a linear array on the exterior of the flagellar membrane before and after activation.
title_short The glycosylphosphatidylinositol-PLC in Trypanosoma brucei forms a linear array on the exterior of the flagellar membrane before and after activation.
title_full The glycosylphosphatidylinositol-PLC in Trypanosoma brucei forms a linear array on the exterior of the flagellar membrane before and after activation.
title_fullStr The glycosylphosphatidylinositol-PLC in Trypanosoma brucei forms a linear array on the exterior of the flagellar membrane before and after activation.
title_full_unstemmed The glycosylphosphatidylinositol-PLC in Trypanosoma brucei forms a linear array on the exterior of the flagellar membrane before and after activation.
title_sort glycosylphosphatidylinositol-plc in trypanosoma brucei forms a linear array on the exterior of the flagellar membrane before and after activation.
publisher Public Library of Science (PLoS)
publishDate 2009
url https://doaj.org/article/bc4fdc332f5d4bddbd0b037ccf2aa5d3
work_keys_str_mv AT orlahanrahan theglycosylphosphatidylinositolplcintrypanosomabruceiformsalineararrayontheexterioroftheflagellarmembranebeforeandafteractivation
AT helenawebb theglycosylphosphatidylinositolplcintrypanosomabruceiformsalineararrayontheexterioroftheflagellarmembranebeforeandafteractivation
AT robertobyrne theglycosylphosphatidylinositolplcintrypanosomabruceiformsalineararrayontheexterioroftheflagellarmembranebeforeandafteractivation
AT elainebrabazon theglycosylphosphatidylinositolplcintrypanosomabruceiformsalineararrayontheexterioroftheflagellarmembranebeforeandafteractivation
AT achimtreumann theglycosylphosphatidylinositolplcintrypanosomabruceiformsalineararrayontheexterioroftheflagellarmembranebeforeandafteractivation
AT jackdsunter theglycosylphosphatidylinositolplcintrypanosomabruceiformsalineararrayontheexterioroftheflagellarmembranebeforeandafteractivation
AT markcarrington theglycosylphosphatidylinositolplcintrypanosomabruceiformsalineararrayontheexterioroftheflagellarmembranebeforeandafteractivation
AT hpaulvoorheis theglycosylphosphatidylinositolplcintrypanosomabruceiformsalineararrayontheexterioroftheflagellarmembranebeforeandafteractivation
AT orlahanrahan glycosylphosphatidylinositolplcintrypanosomabruceiformsalineararrayontheexterioroftheflagellarmembranebeforeandafteractivation
AT helenawebb glycosylphosphatidylinositolplcintrypanosomabruceiformsalineararrayontheexterioroftheflagellarmembranebeforeandafteractivation
AT robertobyrne glycosylphosphatidylinositolplcintrypanosomabruceiformsalineararrayontheexterioroftheflagellarmembranebeforeandafteractivation
AT elainebrabazon glycosylphosphatidylinositolplcintrypanosomabruceiformsalineararrayontheexterioroftheflagellarmembranebeforeandafteractivation
AT achimtreumann glycosylphosphatidylinositolplcintrypanosomabruceiformsalineararrayontheexterioroftheflagellarmembranebeforeandafteractivation
AT jackdsunter glycosylphosphatidylinositolplcintrypanosomabruceiformsalineararrayontheexterioroftheflagellarmembranebeforeandafteractivation
AT markcarrington glycosylphosphatidylinositolplcintrypanosomabruceiformsalineararrayontheexterioroftheflagellarmembranebeforeandafteractivation
AT hpaulvoorheis glycosylphosphatidylinositolplcintrypanosomabruceiformsalineararrayontheexterioroftheflagellarmembranebeforeandafteractivation
_version_ 1718414480577134592