Turnover of Variant Surface Glycoprotein in Trypanosoma brucei Is Not Altered in Response to Specific Silencing.
RNAi silencing
glycosylphosphatidylinositol
protein turnover
trypanosome
variant surface glycoprotein
Journal
mSphere
ISSN: 2379-5042
Titre abrégé: mSphere
Pays: United States
ID NLM: 101674533
Informations de publication
Date de publication:
31 08 2022
31 08 2022
Historique:
pubmed:
22
6
2022
medline:
9
9
2022
entrez:
21
6
2022
Statut:
ppublish
Résumé
African trypanosomes evade the immune system of the mammalian host by the antigenic variation of the predominant glycosylphosphatidylinositol (GPI)-anchored surface protein, variant surface glycoprotein (VSG). VSG is a very stable protein that is turned over from the cell surface with a long half-life (~26 h), allowing newly synthesized VSG to populate the surface. We have recently demonstrated that VSG turnover under normal growth is mediated by a combination of GPI hydrolysis and direct shedding with intact GPI anchors. VSG synthesis is tightly regulated in dividing trypanosomes, and when subjected to RNA interference (RNAi) silencing, cells display rapid cell cycle arrest in order to conserve VSG density on the cell surface (K. Sheader, S. Vaughan, J. Minchin, K. Hughes, et al., Proc Natl Acad Sci U S A 102:8716-8721, 2005, https://doi.org/10.1073/pnas.0501886102). Arrested cells also display an altered morphology of secretory organelles-engorgement of the
Identifiants
pubmed: 35727016
doi: 10.1128/msphere.00122-22
pmc: PMC9429888
doi:
Substances chimiques
Glycosylphosphatidylinositols
0
Membrane Glycoproteins
0
Variant Surface Glycoproteins, Trypanosoma
0
Types de publication
Journal Article
Research Support, N.I.H., Extramural
Research Support, Non-U.S. Gov't
Langues
eng
Sous-ensembles de citation
IM
Pagination
e0012222Subventions
Organisme : NIAID NIH HHS
ID : R01 AI035739
Pays : United States
Organisme : NIAID NIH HHS
ID : R29 AI035739
Pays : United States
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