Potential role of autophagy in proteolysis in Trichomonas vaginalis.
Autophagosomes
Autophagy
/ drug effects
Autophagy-Related Protein 8 Family
/ genetics
Glucose
/ metabolism
Humans
Leupeptins
/ pharmacology
Proteasome Endopeptidase Complex
/ drug effects
Proteasome Inhibitors
/ pharmacology
Proteolysis
Proteostasis
Recombinant Proteins
Trichomonas vaginalis
/ drug effects
Ubiquitination
Autophagy
Proteolysis
Trichomonads
Ubiquitin proteasome system
Journal
Journal of microbiology, immunology, and infection = Wei mian yu gan ran za zhi
ISSN: 1995-9133
Titre abrégé: J Microbiol Immunol Infect
Pays: England
ID NLM: 100956211
Informations de publication
Date de publication:
Apr 2019
Apr 2019
Historique:
received:
14
08
2018
revised:
09
10
2018
accepted:
16
11
2018
pubmed:
7
12
2018
medline:
30
4
2019
entrez:
4
12
2018
Statut:
ppublish
Résumé
Autophagy has been shown to be involved in the pathogenesis of several protists, offering prospects for the developments of new drugs targeting autophagy. However, there is no evidence illustrating functional autophagy in the deep-branching trichomonads. The human parasitic protist Trichomonas vaginalis has been predicted to possess reduced autophagic machinery, with only autophagy-related protein 8 (Atg8) conjugation system required for autophagosome formation. The recombinant protein of TvAtg8 (rTvAtg8) and the polyclonal antibody against rTvAtg8 were generated. The expression and localization of TvAtg8 was monitored upon autophagy induction by glucose restriction (GR) compared with glucose-rich cultivation. The role of TvAtg8 in proteolysis was clarified. Here, we report that T. vaginalis Atg8 (TvAtg8) is upregulated and conjugated to autophagosome-like vesicles upon autophagy induction by GR. Moreover, we investigate, for the first time, the role of autophagy in T. vaginalis. Proteasome inhibition (PI)-induced autophagy compensates for the removal of polyubiquitinated proteins under glucose-rich condition. GR-induced autophagy is a major proteolytic system in T. vaginalis. These results suggest that autophagy is vital for proteolysis in T. vaginalis with an impaired ubiquitin-proteasome system or under glucose-limited environment. Our findings unveiled previously unidentified functions of autophagy in proteostasis in trichomonads, advancing our understanding of this highly conserved process in the ancient eukaryote.
Sections du résumé
BACKGROUND
BACKGROUND
Autophagy has been shown to be involved in the pathogenesis of several protists, offering prospects for the developments of new drugs targeting autophagy. However, there is no evidence illustrating functional autophagy in the deep-branching trichomonads. The human parasitic protist Trichomonas vaginalis has been predicted to possess reduced autophagic machinery, with only autophagy-related protein 8 (Atg8) conjugation system required for autophagosome formation.
METHODS
METHODS
The recombinant protein of TvAtg8 (rTvAtg8) and the polyclonal antibody against rTvAtg8 were generated. The expression and localization of TvAtg8 was monitored upon autophagy induction by glucose restriction (GR) compared with glucose-rich cultivation. The role of TvAtg8 in proteolysis was clarified.
RESULTS
RESULTS
Here, we report that T. vaginalis Atg8 (TvAtg8) is upregulated and conjugated to autophagosome-like vesicles upon autophagy induction by GR. Moreover, we investigate, for the first time, the role of autophagy in T. vaginalis. Proteasome inhibition (PI)-induced autophagy compensates for the removal of polyubiquitinated proteins under glucose-rich condition. GR-induced autophagy is a major proteolytic system in T. vaginalis. These results suggest that autophagy is vital for proteolysis in T. vaginalis with an impaired ubiquitin-proteasome system or under glucose-limited environment.
CONCLUSION
CONCLUSIONS
Our findings unveiled previously unidentified functions of autophagy in proteostasis in trichomonads, advancing our understanding of this highly conserved process in the ancient eukaryote.
Identifiants
pubmed: 30503389
pii: S1684-1182(18)30301-3
doi: 10.1016/j.jmii.2018.11.002
pii:
doi:
Substances chimiques
Autophagy-Related Protein 8 Family
0
Leupeptins
0
Proteasome Inhibitors
0
Recombinant Proteins
0
Proteasome Endopeptidase Complex
EC 3.4.25.1
Glucose
IY9XDZ35W2
benzyloxycarbonylleucyl-leucyl-leucine aldehyde
RF1P63GW3K
Types de publication
Journal Article
Langues
eng
Sous-ensembles de citation
IM
Pagination
336-344Informations de copyright
Copyright © 2018. Published by Elsevier B.V.