Streptococcus pneumoniae hijacks host autophagy by deploying CbpC as a decoy for Atg14 depletion.
Streptococcus pneumoniae
Atg14
CbpC
autophagy
p62
Journal
EMBO reports
ISSN: 1469-3178
Titre abrégé: EMBO Rep
Pays: England
ID NLM: 100963049
Informations de publication
Date de publication:
06 05 2020
06 05 2020
Historique:
received:
16
09
2019
revised:
28
02
2020
accepted:
06
03
2020
pubmed:
3
4
2020
medline:
28
4
2021
entrez:
3
4
2020
Statut:
ppublish
Résumé
Pneumococcal cell surface-exposed choline-binding proteins (CBPs) play pivotal roles in multiple infectious processes with pneumococci. Intracellular pneumococci can be recognized at multiple steps during bactericidal autophagy. However, whether CBPs are involved in pneumococci-induced autophagic processes remains unknown. In this study, we demonstrate that CbpC from S. pneumoniae strain TIGR4 activates autophagy through an interaction with Atg14. However, S. pneumoniae also interferes with autophagy by deploying CbpC as a decoy to cause autophagic degradation of Atg14 through an interaction with p62/SQSTM1. Thus, S. pneumoniae suppresses the autophagic degradation of intracellular pneumococci and survives within cells. Domain analysis reveals that the coiled-coil domain of Atg14 and residue Y83 of the dp3 domain in the N-terminal region of CbpC are crucial for both the CbpC-Atg14 interaction and the subsequent autophagic degradation of Atg14. Although homology modeling indicates that CbpC orthologs have similar structures in the dp3 domain, autophagy induction through Atg14 binding is an intrinsic property of CbpC
Identifiants
pubmed: 32239622
doi: 10.15252/embr.201949232
pmc: PMC7202210
doi:
Substances chimiques
ATG14 protein, human
0
Adaptor Proteins, Vesicular Transport
0
Autophagy-Related Proteins
0
Bacterial Proteins
0
Membrane Proteins
0
Types de publication
Journal Article
Research Support, Non-U.S. Gov't
Langues
eng
Sous-ensembles de citation
IM
Pagination
e49232Subventions
Organisme : Uehara Memorial Foundation
Pays : International
Organisme : Naito Foundation
Pays : International
Organisme : Grant-in-aid for Scientific Research
ID : 16K08800
Pays : International
Organisme : Grant-in-aid for Scientific Research
ID : 19K07568
Pays : International
Organisme : Grant-in-aid for Scientific Research
ID : 25460555
Pays : International
Informations de copyright
© 2020 The Authors. Published under the terms of the CC BY 4.0 license.
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