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Article ; Online: Molecular mechanism of Streptococcus pneumoniae-targeting xenophagy recognition and evasion: Reinterpretation of pneumococci as intracellular bacteria.

Ogawa, Michinaga / Shizukuishi, Sayaka / Akeda, Yukihiro / Ohnishi, Makoto

2023 Volume 67, Issue 5, Page(s) 224–227

Abstract: Streptococcus pneumoniae is a major, encapsulated Gram-positive pathogen that causes diseases including community-acquired pneumonia, meningitis, and sepsis. This pathogen colonizes the nasopharyngeal epithelia asymptomatically but can often migrate to ... ...

Abstract	Streptococcus pneumoniae is a major, encapsulated Gram-positive pathogen that causes diseases including community-acquired pneumonia, meningitis, and sepsis. This pathogen colonizes the nasopharyngeal epithelia asymptomatically but can often migrate to sterile tissues and cause life-threatening invasive infections (invasive pneumococcal disease). Although multivalent pneumococcal polysaccharides and conjugate vaccines are available and effective, they also have major shortcomings with respect to the emergence of vaccine-resistant serotypes. Therefore, alternative therapeutic approaches are needed, and the molecular analysis of host-pathogen interactions and their applications to pharmaceutical development and clinical practice has recently received increased attention. In this review, we introduce pneumococcal surface virulence factors involved in pathogenicity and highlight recent advances in our understanding of host autophagy recognition mechanisms against intracellular S. pneumoniae and pneumococcal evasion from autophagy.
MeSH term(s)	Humans ; Streptococcus pneumoniae/genetics ; Macroautophagy ; Pneumococcal Infections/microbiology ; Virulence Factors ; Virulence ; Pneumococcal Vaccines
Chemical Substances	Virulence Factors ; Pneumococcal Vaccines
Language	English
Publishing date	2023-03-21
Publishing country	Australia
Document type	Journal Article ; Review
ZDB-ID	224792-6
ISSN	1348-0421 ; 0385-5600
ISSN (online)	1348-0421
ISSN	0385-5600
DOI	10.1111/1348-0421.13060
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Article ; Online: Streptococcus pneumoniae

Shizukuishi, Sayaka / Ogawa, Michinaga / Ryo, Akihide / Ohnishi, Makoto

Autophagy

2020 Volume 16, Issue 8, Page(s) 1529–1531

Abstract: Streptococcus pneumoniae: is an opportunistic bacterial pathogen that can promote severe infection by overcoming the epithelial and blood-brain barrier. Pneumococcal cell-surface virulence factors, including cell wall-anchored choline-binding proteins ( ... ...

Abstract	Streptococcus pneumoniae: is an opportunistic bacterial pathogen that can promote severe infection by overcoming the epithelial and blood-brain barrier. Pneumococcal cell-surface virulence factors, including cell wall-anchored choline-binding proteins (Cbps) play pivotal roles in promoting invasive disease. We reported previously that intracellular pneumococci were detected by hierarchical macroautophagic/autophagic processes that ultimately lead to bacterial elimination. However, whether intracellular pneumococci can evade autophagy by deploying Cbps remains unclear. In this study, we explore the biological functions of Cbps and reveal their roles in manipulating the autophagic process. Specifically, we found that CbpC-activated autophagy takes place via its interactions with ATG14 (autophagy related 14) and SQSTM1/p62 (sequestosome1). Importantly, CbpC dampens host autophagy by promoting ATG14 degradation via the ATG14-CbpC-SQSTM1/p62 axis. CbpC-induced reductions in ATG14 levels result in impaired ATG14-STX17 complex formation. In pneumococcal-infected cells, ATG14 levels are dramatically reduced in a CbpC-dependent manner that results in suppression of autophagy-mediated degradation and enhanced bacterial survival. Taken together, our results reveal a novel mechanism via which pneumococci can manipulate host autophagy responses, in this case, by employing CbpC as a trap to promote ATG14 depletion. Our findings highlight a novel and sophisticated tactic used by
Language	English
Publishing date	2020-06-17
Publishing country	United States
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	2454135-7
ISSN	1554-8635 ; 1554-8627
ISSN (online)	1554-8635
ISSN	1554-8627
DOI	10.1080/15548627.2020.1776475
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Article ; Online: The multi-step mechanism and biological role of noncanonical autophagy targeting

Shizukuishi, Sayaka / Ogawa, Michinaga / Ryo, Akihide / Ohnishi, Makoto

Autophagy

2020 Volume 16, Issue 6, Page(s) 1152–1153

Abstract: Multiple autophagic processes are triggered in response to bacterial infection as the host attempts to eliminate intracellular invaders. However, it is still unclear how the mechanisms contributing to canonical macroautophagy/autophagy, including ... ...

Abstract	Multiple autophagic processes are triggered in response to bacterial infection as the host attempts to eliminate intracellular invaders. However, it is still unclear how the mechanisms contributing to canonical macroautophagy/autophagy, including xenophagy, coordinate with the more recently described features that are characteristic of noncanonical autophagy. Recently, we revealed that infection with
MeSH term(s)	Autophagosomes ; Autophagy ; Bacterial Proteins ; Phagosomes ; Streptococcus pneumoniae
Chemical Substances	Bacterial Proteins
Language	English
Publishing date	2020-03-21
Publishing country	United States
Document type	Journal Article ; Research Support, Non-U.S. Gov't ; Comment
ZDB-ID	2454135-7
ISSN	1554-8635 ; 1554-8627
ISSN (online)	1554-8635
ISSN	1554-8627
DOI	10.1080/15548627.2020.1743937
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Article ; Online: Pneumococcal sialidase promotes bacterial survival by fine-tuning of pneumolysin-mediated membrane disruption.

Shizukuishi, Sayaka / Ogawa, Michinaga / Kuroda, Eisuke / Hamaguchi, Shigeto / Sakuma, Chisato / Kakuta, Soichiro / Tanida, Isei / Uchiyama, Yasuo / Akeda, Yukihiro / Ryo, Akihide / Ohnishi, Makoto

Cell reports

2024 Volume 43, Issue 3, Page(s) 113962

Abstract: Pneumolysin (Ply) is an indispensable cholesterol-dependent cytolysin for pneumococcal infection. Although Ply-induced disruption of pneumococci-containing endosomal vesicles is a prerequisite for the evasion of endolysosomal bacterial clearance, its ... ...

Abstract	Pneumolysin (Ply) is an indispensable cholesterol-dependent cytolysin for pneumococcal infection. Although Ply-induced disruption of pneumococci-containing endosomal vesicles is a prerequisite for the evasion of endolysosomal bacterial clearance, its potent activity can be a double-edged sword, having a detrimental effect on bacterial survivability by inducing severe endosomal disruption, bactericidal autophagy, and scaffold epithelial cell death. Thus, Ply activity must be maintained at optimal levels. We develop a highly sensitive assay to monitor endosomal disruption using NanoBiT-Nanobody, which shows that the pneumococcal sialidase NanA can fine-tune Ply activity by trimming sialic acid from cell-membrane-bound glycans. In addition, oseltamivir, an influenza A virus sialidase inhibitor, promotes Ply-induced endosomal disruption and cytotoxicity by inhibiting NanA activity in vitro and greater tissue damage and bacterial clearance in vivo. Our findings provide a foundation for innovative therapeutic strategies for severe pneumococcal infections by exploiting the duality of Ply activity.
MeSH term(s)	Humans ; Neuraminidase/metabolism ; Streptococcus pneumoniae/metabolism ; Streptolysins/metabolism ; Pneumococcal Infections ; Bacterial Proteins/metabolism
Chemical Substances	plY protein, Streptococcus pneumoniae ; Neuraminidase (EC 3.2.1.18) ; Streptolysins ; Bacterial Proteins
Language	English
Publishing date	2024-03-13
Publishing country	United States
Document type	Journal Article
ZDB-ID	2649101-1
ISSN	2211-1247 ; 2211-1247
ISSN (online)	2211-1247
ISSN	2211-1247
DOI	10.1016/j.celrep.2024.113962
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Article ; Online: Individual Atg8 paralogs and a bacterial metabolite sequentially promote hierarchical CASM-xenophagy induction and transition.

Sakuma, Chisato / Shizukuishi, Sayaka / Ogawa, Michinaga / Honjo, Yuko / Takeyama, Haruko / Guan, Jun-Lin / Weiser, Jeffery / Sasai, Miwa / Yamamoto, Masahiro / Ohnishi, Makoto / Akeda, Yukihiro

Cell reports

2024 Volume 43, Issue 5, Page(s) 114131

Abstract: Atg8 paralogs, consisting of LC3A/B/C and GBRP/GBRPL1/GATE16, function in canonical autophagy; however, their function is controversial because of functional redundancy. In innate immunity, xenophagy and non-canonical single membranous autophagy called " ... ...

Abstract	Atg8 paralogs, consisting of LC3A/B/C and GBRP/GBRPL1/GATE16, function in canonical autophagy; however, their function is controversial because of functional redundancy. In innate immunity, xenophagy and non-canonical single membranous autophagy called "conjugation of Atg8s to single membranes" (CASM) eliminate bacteria in various cells. Previously, we reported that intracellular Streptococcus pneumoniae can induce unique hierarchical autophagy comprised of CASM induction, shedding, and subsequent xenophagy. However, the molecular mechanisms underlying these processes and the biological significance of transient CASM induction remain unknown. Herein, we profile the relationship between Atg8s, autophagy receptors, poly-ubiquitin, and Atg4 paralogs during pneumococcal infection to understand the driving principles of hierarchical autophagy and find that GATE16 and GBRP sequentially play a pivotal role in CASM shedding and subsequent xenophagy induction, respectively, and LC3A and GBRPL1 are involved in CASM/xenophagy induction. Moreover, we reveal ingenious bacterial tactics to gain intracellular survival niches by manipulating CASM-xenophagy progression by generating intracellular pneumococci-derived H
Language	English
Publishing date	2024-04-23
Publishing country	United States
Document type	Journal Article
ZDB-ID	2649101-1
ISSN	2211-1247 ; 2211-1247
ISSN (online)	2211-1247
ISSN	2211-1247
DOI	10.1016/j.celrep.2024.114131
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Article ; Online: Clinical features relating to pneumococcal colony phase variation in hospitalized adults with pneumonia.

Ideguchi, Shuhei / Yamamoto, Kazuko / Takazono, Takahiro / Fukuda, Yuichi / Tashiro, Takahiro / Shizukuishi, Sayaka / Chang, Bin / Ogawa, Michinaga / Izumikawa, Koichi / Yanagihara, Katsunori / Yatera, Kazuhiro / Mukae, Hiroshi

Journal of medical microbiology

2024 Volume 73, Issue 1

Abstract: Background. ...

Abstract	Background.
MeSH term(s)	Animals ; Male ; Humans ; Aged ; Streptococcus pneumoniae ; Pneumonia, Pneumococcal ; Phase Variation ; Retrospective Studies ; Pneumococcal Infections
Language	English
Publishing date	2024-01-08
Publishing country	England
Document type	Journal Article
ZDB-ID	218356-0
ISSN	1473-5644 ; 0022-2615
ISSN (online)	1473-5644
ISSN	0022-2615
DOI	10.1099/jmm.0.001784
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Article ; Online: Streptococcus pneumoniae hijacks host autophagy by deploying CbpC as a decoy for Atg14 depletion.

Shizukuishi, Sayaka / Ogawa, Michinaga / Matsunaga, Satoko / Tomokiyo, Mikado / Ikebe, Tadayoshi / Fushinobu, Shinya / Ryo, Akihide / Ohnishi, Makoto

EMBO reports

2020 Volume 21, Issue 5, Page(s) e49232

Abstract: 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 ...

Abstract	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
MeSH term(s)	Adaptor Proteins, Vesicular Transport ; Animals ; Autophagy ; Autophagy-Related Proteins/genetics ; Bacterial Proteins/metabolism ; Cell Line ; Humans ; Membrane Proteins ; Mice ; Streptococcus pneumoniae/genetics
Chemical Substances	ATG14 protein, human ; Adaptor Proteins, Vesicular Transport ; Autophagy-Related Proteins ; Bacterial Proteins ; Membrane Proteins
Language	English
Publishing date	2020-04-02
Publishing country	England
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	2020896-0
ISSN	1469-3178 ; 1469-221X
ISSN (online)	1469-3178
ISSN	1469-221X
DOI	10.15252/embr.201949232
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Zs.A 5433: Show issues			Location: Je nach Verfügbarkeit (siehe Angabe bei Bestand) bis Jg. 1994: Bestellungen von Artikeln über das Online-Bestellformular Jg. 1995 - 2021: Lesesall (2.OG) ab Jg. 2022: Lesesaal (EG)
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Article ; Online: Engineering Cellular Biosensors with Customizable Antiviral Responses Targeting Hepatitis B Virus.

Matsunaga, Satoko / Jeremiah, Sundararaj S / Miyakawa, Kei / Kurotaki, Daisuke / Shizukuishi, Sayaka / Watashi, Koichi / Nishitsuji, Hironori / Kimura, Hirokazu / Tamura, Tomohiko / Yamamoto, Naoki / Shimotohno, Kunitada / Wakita, Takaji / Ryo, Akihide

iScience

2020 Volume 23, Issue 3, Page(s) 100867

Abstract: SynNotch receptor technology is a versatile tool that uses the regulatory notch core portion with an extracellular scFv and an intracellular transcription factor that enables to program customized input and output functions in mammalian cells. In this ... ...

Abstract	SynNotch receptor technology is a versatile tool that uses the regulatory notch core portion with an extracellular scFv and an intracellular transcription factor that enables to program customized input and output functions in mammalian cells. In this study, we designed a novel synNotch receptor comprising scFv against HBs antigen linked with an intracellular artificial transcription factor and exploited it for viral sensing and cellular immunotherapy. The synNotch receptor expressing cells sensed HBV particles and membrane-bound HBs antigens and responded by expressing reporter molecules, secNL or GFP. We also programmed these cells to dispense antiviral responses such as type I interferon and anti-HBV neutralizing mouse-human chimeric antibodies. Our data reveal that synNotch receptor signaling works for membrane-bound ligands such as enveloped viral particles and proteins borne on liposomal vesicles. This study establishes the concepts of "engineered immunity" where the synNotch platform is utilized for cellular immunotherapy against viral infections.
Language	English
Publishing date	2020-02-26
Publishing country	United States
Document type	Journal Article
ISSN	2589-0042
ISSN (online)	2589-0042
DOI	10.1016/j.isci.2020.100867
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Article ; Online: Streptococcus pneumoniae triggers hierarchical autophagy through reprogramming of LAPosome-like vesicles via NDP52-delocalization.

Ogawa, Michinaga / Takada, Naoki / Shizukuishi, Sayaka / Tomokiyo, Mikado / Chang, Bin / Yoshida, Mitsutaka / Kakuta, Soichiro / Tanida, Isei / Ryo, Akihide / Guan, Jun-Lin / Takeyama, Haruko / Ohnishi, Makoto

Communications biology

2020 Volume 3, Issue 1, Page(s) 25

Abstract: In innate immunity, multiple autophagic processes eliminate intracellular pathogens, but it remains unclear whether noncanonical autophagy and xenophagy are coordinated, and whether they occur concomitantly or sequentially. Here, we show that ... ...

Abstract	In innate immunity, multiple autophagic processes eliminate intracellular pathogens, but it remains unclear whether noncanonical autophagy and xenophagy are coordinated, and whether they occur concomitantly or sequentially. Here, we show that Streptococcus pneumoniae, a causative of invasive pneumococcal disease, can trigger FIP200-, PI3P-, and ROS-independent pneumococcus-containing LC3-associated phagosome (LAPosome)-like vacuoles (PcLVs) in an early stage of infection, and that PcLVs are indispensable for subsequent formation of bactericidal pneumococcus-containing autophagic vacuoles (PcAVs). Specifically, we identified LC3- and NDP52-delocalized PcLV, which are intermediates between PcLV and PcAV. Atg14L, Beclin1, and FIP200 were responsible for delocalizing LC3 and NDP52 from PcLVs. Thus, multiple noncanonical and canonical autophagic processes are deployed sequentially against intracellular S. pneumoniae. The Atg16L1 WD domain, p62, NDP52, and poly-Ub contributed to PcLV formation. These findings reveal a previously unidentified hierarchical autophagy mechanism during bactericidal xenophagy against intracellular bacterial pathogens, and should improve our ability to control life-threating pneumococcal diseases.
MeSH term(s)	Animals ; Autophagy ; Biomarkers ; Cell Line ; Cytoplasmic Vesicles/metabolism ; Fluorescent Antibody Technique ; Gene Expression ; Genes, Reporter ; Host-Pathogen Interactions ; Humans ; Mice ; Models, Biological ; Nuclear Proteins/metabolism ; Pneumococcal Infections/metabolism ; Pneumococcal Infections/microbiology ; Reactive Oxygen Species/metabolism ; Streptococcus pneumoniae/physiology
Chemical Substances	Biomarkers ; CALCOCO2 protein, human ; Nuclear Proteins ; Reactive Oxygen Species
Language	English
Publishing date	2020-01-13
Publishing country	England
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ISSN	2399-3642
ISSN (online)	2399-3642
DOI	10.1038/s42003-020-0753-3
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Article ; Online: Molecular mechanisms of Streptococcus pneumoniae-targeted autophagy via pneumolysin, Golgi-resident Rab41, and Nedd4-1-mediated K63-linked ubiquitination.

Cellular microbiology

2018 Volume 20, Issue 8, Page(s) e12846

Abstract: Streptococcus pneumoniae is the most common causative agent of community-acquired pneumonia and can penetrate epithelial barriers to enter the bloodstream and brain. We investigated intracellular fates of S. pneumoniae and found that the pathogen is ... ...

Abstract	Streptococcus pneumoniae is the most common causative agent of community-acquired pneumonia and can penetrate epithelial barriers to enter the bloodstream and brain. We investigated intracellular fates of S. pneumoniae and found that the pathogen is entrapped by selective autophagy in pneumolysin- and ubiquitin-p62-LC3 cargo-dependent manners. Importantly, following induction of autophagy, Rab41 was relocated from the Golgi apparatus to S. pneumoniae-containing autophagic vesicles (PcAV), which were only formed in the presence of Rab41-positive intact Golgi apparatuses. Moreover, subsequent localization and regulation of K48- and K63-linked polyubiquitin chains in and on PcAV were clearly distinguishable from each other. Finally, we found that E3 ligase Nedd4-1 was recruited to PcAV and played a pivotal role in K63-linked polyubiquitin chain (K63Ub) generation on PcAV, promotion of PcAV formation, and elimination of intracellular S. pneumoniae. These findings suggest that Nedd4-1-mediated K63Ub deposition on PcAV acts as a scaffold for PcAV biogenesis and efficient elimination of host cell-invaded pneumococci.
MeSH term(s)	Animals ; Autophagy ; Bacterial Proteins/metabolism ; Cell Line ; Epithelial Cells/immunology ; Epithelial Cells/microbiology ; Humans ; Nedd4 Ubiquitin Protein Ligases/metabolism ; Polyubiquitin/metabolism ; Streptococcus pneumoniae/immunology ; Streptolysins/metabolism ; Ubiquitination ; rab GTP-Binding Proteins/metabolism
Chemical Substances	Bacterial Proteins ; Streptolysins ; plY protein, Streptococcus pneumoniae ; Polyubiquitin (120904-94-1) ; Nedd4 Ubiquitin Protein Ligases (EC 2.3.2.26) ; Nedd4 protein, human (EC 2.3.2.26) ; RAB41 protein, human (EC 3.6.1.-) ; rab GTP-Binding Proteins (EC 3.6.5.2)
Language	English
Publishing date	2018-04-22
Publishing country	England
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	1468320-9
ISSN	1462-5822 ; 1462-5814
ISSN (online)	1462-5822
ISSN	1462-5814
DOI	10.1111/cmi.12846
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