Open AccessDeletion of a Golgi protein in Trypanosoma cruzi reveals a critical role for Mn2+ in protein glycosylation needed for host cell invasion and intracellular replication
Author(s) -
S. Ramakrishnan,
Linn M. Unger,
Rodrigo P. Baptista,
Teresa CruzBustos,
Roberto Docampo
Publication year - 2021
Publication title -
plos pathogens
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 3.719
H-Index - 206
eISSN - 1553-7374
pISSN - 1553-7366
DOI - 10.1371/journal.ppat.1009399
Subject(s) - biology , microbiology and biotechnology , trypanosoma cruzi , golgi apparatus , glycosylation , secretory pathway , intracellular parasite , viral replication , intracellular , virology , virus , biochemistry , parasite hosting , endoplasmic reticulum , world wide web , computer science
Trypanosoma cruzi is a protist parasite and the causative agent of American trypanosomiasis or Chagas disease. The parasite life cycle in its mammalian host includes an intracellular stage, and glycosylated proteins play a key role in host-parasite interaction facilitating adhesion, invasion and immune evasion. Here, we report that a Golgi-localized Mn 2+ -Ca 2+ /H + exchanger of T . cruzi (TcGDT1) is required for efficient protein glycosylation, host cell invasion, and intracellular replication. The Golgi localization was determined by immunofluorescence and electron microscopy assays. TcGDT1 was able to complement the growth defect of Saccharomyces cerevisiae null mutants of its ortholog ScGDT1 but ablation of TcGDT1 by CRISPR/Cas9 did not affect the growth of the insect stage of the parasite. The defect in protein glycosylation was rescued by Mn 2+ supplementation to the growth medium, underscoring the importance of this transition metal for Golgi glycosylation of proteins.