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Streptococcus pneumoniae hijacks host autophagy by deploying CbpC as a decoy for Atg14 depletion
Author(s) -
Shizukuishi Sayaka,
Ogawa Michinaga,
Matsunaga Satoko,
Tomokiyo Mikado,
Ikebe Tadayoshi,
Fushinobu Shinya,
Ryo Akihide,
Ohnishi Makoto
Publication year - 2020
Publication title -
embo reports
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 4.584
H-Index - 184
eISSN - 1469-3178
pISSN - 1469-221X
DOI - 10.15252/embr.201949232
Subject(s) - autophagy , decoy , intracellular , microbiology and biotechnology , streptococcus pneumoniae , biology , chemistry , bacteria , biochemistry , genetics , apoptosis , receptor
Pneumococcal cell surface‐exposed choline‐binding proteins ( CBP s) play pivotal roles in multiple infectious processes with pneumococci. Intracellular pneumococci can be recognized at multiple steps during bactericidal autophagy. However, whether CBP s are involved in pneumococci‐induced autophagic processes remains unknown. In this study, we demonstrate that CbpC from S. pneumoniae strain TIGR 4 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/ SQSTM 1. 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 . Our data provide novel insights into the evolutionary hijacking of host‐defense systems by intracellular pneumococci.