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Article: [T cell-mediated immune responses and the recognition of tuberculosis antigens].

Tsujimura, Kunio / Koide, Yukio

2010 Volume 85, Issue 6, Page(s) 509–514

Abstract: T cell-mediated immune responses profoundly contribute to the protection against the re-activation of latently infected Mycobacterium tuberculosis. Th1 cells produce IFN-gamma to activate infected macrophages and promote the formation of granulomas ... ...

Abstract	T cell-mediated immune responses profoundly contribute to the protection against the re-activation of latently infected Mycobacterium tuberculosis. Th1 cells produce IFN-gamma to activate infected macrophages and promote the formation of granulomas around infected macrophages. CD8+, gamma delta and CD1-restricted T cells also produce IFN-gamma and participate the protective responses against bacterial growth. Th17 cells produce IL-17 to promote the mobilization of immunocompetent cells and contribute to the granuloma formation. On the contrary, Th2 cells and Tregs interfere these protective immune responses.
MeSH term(s)	Animals ; Antigens, Bacterial/immunology ; Bacterial Proteins/immunology ; Mice ; Mycobacterium tuberculosis/immunology ; T-Lymphocytes/immunology ; Tuberculosis Vaccines/immunology
Chemical Substances	Antigens, Bacterial ; Bacterial Proteins ; Tuberculosis Vaccines
Language	Japanese
Publishing date	2010-06
Publishing country	Japan
Document type	English Abstract ; Journal Article ; Review
ZDB-ID	131032-x
ISSN	1884-2410 ; 0022-9776
ISSN (online)	1884-2410
ISSN	0022-9776
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Article ; Online: Autophagy adaptor protein p62/SQSTM1 and autophagy-related gene Atg5 mediate autophagosome formation in response to Mycobacterium tuberculosis infection in dendritic cells.

Seto, Shintaro / Tsujimura, Kunio / Horii, Toshinobu / Koide, Yukio

PloS one

2013 Volume 8, Issue 12, Page(s) e86017

Abstract: Mycobacterium tuberculosis is an intracellular pathogen that can survive within phagocytic cells by inhibiting phagolysosome biogenesis. However, host cells can control the intracellular M. tuberculosis burden by the induction of autophagy. The mechanism ...

Abstract	Mycobacterium tuberculosis is an intracellular pathogen that can survive within phagocytic cells by inhibiting phagolysosome biogenesis. However, host cells can control the intracellular M. tuberculosis burden by the induction of autophagy. The mechanism of autophagosome formation to M. tuberculosis has been well studied in macrophages, but remains unclear in dendritic cells. We therefore characterized autophagosome formation in response to M. tuberculosis infection in dendritic cells. Autophagy marker protein LC3, autophagy adaptor protein p62/SQSTM1 (p62) and ubiquitin co-localized to M. tuberculosis in dendritic cells. Mycobacterial autophagosomes fused with lysosomes during infection, and major histcompatibility complex class II molecules (MHC II) also localized to mycobacterial autophagosomes. The proteins p62 and Atg5 function in the initiation and progression of autophagosome formation to M. tuberculosis, respectively; p62 mediates ubiquitination of M. tuberculosis and Atg5 is involved in the trafficking of degradative vesicles and MHC II to mycobacterial autophagosomes. These results imply that the autophagosome formation to M. tuberculosis in dendritic cells promotes the antigen presentation of mycobacterial peptides to CD4(+) T lymphocytes via MHC II.
MeSH term(s)	Adaptor Proteins, Signal Transducing/immunology ; Adaptor Proteins, Signal Transducing/metabolism ; Animals ; Antibodies, Monoclonal ; Autophagy/immunology ; Autophagy-Related Protein 5 ; Dendritic Cells/immunology ; Dendritic Cells/microbiology ; Heat-Shock Proteins/immunology ; Heat-Shock Proteins/metabolism ; Immunoblotting ; Macrophages ; Mice ; Mice, Inbred C57BL ; Microscopy, Electron ; Microscopy, Fluorescence ; Microtubule-Associated Proteins/immunology ; Microtubule-Associated Proteins/metabolism ; Mycobacterium tuberculosis ; Phagosomes/immunology ; RNA Interference ; RNA, Small Interfering/genetics ; Sequestosome-1 Protein ; Tuberculosis/immunology
Chemical Substances	Adaptor Proteins, Signal Transducing ; Antibodies, Monoclonal ; Atg5 protein, mouse ; Autophagy-Related Protein 5 ; Heat-Shock Proteins ; Map1lc3b protein, mouse ; Microtubule-Associated Proteins ; RNA, Small Interfering ; Sequestosome-1 Protein ; Sqstm1 protein, mouse
Language	English
Publishing date	2013-12-23
Publishing country	United States
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ISSN	1932-6203
ISSN (online)	1932-6203
DOI	10.1371/journal.pone.0086017
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Article ; Online: Autophagy adaptor protein p62/SQSTM1 and autophagy-related gene Atg5 mediate autophagosome formation in response to Mycobacterium tuberculosis infection in dendritic cells.

Shintaro Seto / Kunio Tsujimura / Toshinobu Horii / Yukio Koide

PLoS ONE, Vol 8, Iss 12, p e

2013 Volume 86017

Abstract	Mycobacterium tuberculosis is an intracellular pathogen that can survive within phagocytic cells by inhibiting phagolysosome biogenesis. However, host cells can control the intracellular M. tuberculosis burden by the induction of autophagy. The mechanism of autophagosome formation to M. tuberculosis has been well studied in macrophages, but remains unclear in dendritic cells. We therefore characterized autophagosome formation in response to M. tuberculosis infection in dendritic cells. Autophagy marker protein LC3, autophagy adaptor protein p62/SQSTM1 (p62) and ubiquitin co-localized to M. tuberculosis in dendritic cells. Mycobacterial autophagosomes fused with lysosomes during infection, and major histcompatibility complex class II molecules (MHC II) also localized to mycobacterial autophagosomes. The proteins p62 and Atg5 function in the initiation and progression of autophagosome formation to M. tuberculosis, respectively; p62 mediates ubiquitination of M. tuberculosis and Atg5 is involved in the trafficking of degradative vesicles and MHC II to mycobacterial autophagosomes. These results imply that the autophagosome formation to M. tuberculosis in dendritic cells promotes the antigen presentation of mycobacterial peptides to CD4(+) T lymphocytes via MHC II.
Keywords	Medicine ; R ; Science ; Q
Subject code	570 ; 572
Language	English
Publishing date	2013-01-01T00:00:00Z
Publisher	Public Library of Science (PLoS)
Document type	Article ; Online
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Article ; Online: Coronin-1a inhibits autophagosome formation around Mycobacterium tuberculosis-containing phagosomes and assists mycobacterial survival in macrophages.

Seto, Shintaro / Tsujimura, Kunio / Koide, Yukio

Cellular microbiology

2012 Volume 14, Issue 5, Page(s) 710–727

Abstract: Mycobacterium tuberculosis is an intracellular bacterium that can survive within macrophages. Such survival is potentially associated with Coronin-1a (Coro1a). We investigated the mechanism by which Coro1a promotes the survival of M. tuberculosis in ... ...

Abstract	Mycobacterium tuberculosis is an intracellular bacterium that can survive within macrophages. Such survival is potentially associated with Coronin-1a (Coro1a). We investigated the mechanism by which Coro1a promotes the survival of M. tuberculosis in macrophages and found that autophagy was involved in the inhibition of mycobacterial survival in Coro1a knock-down (KD) macrophages. Fluorescence microscopy and immunoblot analyses revealed that LC3, a representative autophagic protein, was recruited to M. tuberculosis-containing phagosomes in Coro1a KD macrophages. Thin-section electron microscopy demonstrated that bacilli were surrounded by the multiple membrane structures in Coro1a KD macrophages. The proportion of LC3-positive mycobacterial phagosomes colocalized with p62/SQSTM1, ubiquitin or LAMP1 increased in Coro1a KD macrophages during infection. These results demonstrate the formation of autophagosomes around M. tuberculosis in Coro1a KD macrophages. Phosphorylation of p38 mitogen-activated protein kinase (MAPK) was induced in response to M. tuberculosis infection in Coro1a KD macrophages, suggesting that Coro1a blocks the activation of the p38 MAPK pathway involved in autophagosome formation. LC3 recruitment to M. tuberculosis-containing phagosomes was also observed in Coro1a KD alveolar or bone marrow-derived macrophages. These results suggest that Coro1a inhibits autophagosome formation in alveolar macrophages, thereby facilitating M. tuberculosis survival within the lung.
MeSH term(s)	Animals ; Cell Line ; Gene Knockdown Techniques ; Host-Pathogen Interactions ; Immunoblotting ; Macrophages/microbiology ; Macrophages/ultrastructure ; Mice ; Microbial Viability ; Microfilament Proteins/genetics ; Microfilament Proteins/metabolism ; Microscopy, Electron ; Microscopy, Fluorescence ; Mycobacterium tuberculosis/pathogenicity ; Mycobacterium tuberculosis/ultrastructure ; Phagosomes/microbiology ; Phagosomes/ultrastructure
Chemical Substances	Microfilament Proteins ; coronin proteins (145420-64-0)
Language	English
Publishing date	2012-05
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/j.1462-5822.2012.01754.x
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Article ; Online: Involvement of IL-33 in the pathogenesis of rheumatoid arthritis: the effect of etanercept on the serum levels of IL-33.

Kageyama, Yasunori / Torikai, Eiji / Tsujimura, Kunio / Kobayashi, Masato

Modern rheumatology

2012 Volume 22, Issue 1, Page(s) 89–93

Abstract: To investigate the role of interleukin (IL)-33 in rheumatoid arthritis (RA) patients, we measured the serum levels of IL-33 in RA patients before and after the administration of etanercept. Twenty-four patients with RA were treated with etanercept. ... ...

Abstract	To investigate the role of interleukin (IL)-33 in rheumatoid arthritis (RA) patients, we measured the serum levels of IL-33 in RA patients before and after the administration of etanercept. Twenty-four patients with RA were treated with etanercept. Clinical and laboratory examinations, including serum levels of C-reactive protein (CRP) and hemoglobin (Hb); white blood cell (WBC) and red blood cell (RBC) counts; and the Disease Activity Score of 28 joints including CRP (DAS28-CRP), were performed at the baseline and at 3 and 6 months after the initial treatment with etanercept. The mean serum IL-33 levels had decreased significantly at 3 and 6 months after the initial treatment with etanercept. Serum IL-33 levels showed a significant correlation with the number of tender joints, CRP, DAS28-CRP, and the WBC count, and an inverse correlation with the RBC count and Hb level. These findings indicated that the decrease of serum IL-33 levels was a novel function of etanercept, shown for the first time in this study. Measurement of serum levels of IL-33 may become a useful control marker for RA treatment.
MeSH term(s)	Antirheumatic Agents/therapeutic use ; Arthritis, Rheumatoid/blood ; Arthritis, Rheumatoid/diagnosis ; Arthritis, Rheumatoid/drug therapy ; Biomarkers/metabolism ; C-Reactive Protein/analysis ; Drug Monitoring ; Etanercept ; Female ; Hematologic Tests ; Humans ; Hyperalgesia/diagnosis ; Hyperalgesia/drug therapy ; Immunoglobulin G/therapeutic use ; Interleukin-33 ; Interleukins/blood ; Joints/pathology ; Male ; Middle Aged ; Receptors, Tumor Necrosis Factor/therapeutic use
Chemical Substances	Antirheumatic Agents ; Biomarkers ; IL33 protein, human ; Immunoglobulin G ; Interleukin-33 ; Interleukins ; Receptors, Tumor Necrosis Factor ; C-Reactive Protein (9007-41-4) ; Etanercept (OP401G7OJC)
Language	English
Publishing date	2012-02
Publishing country	United States
Document type	Clinical Trial ; Journal Article
ZDB-ID	2078157-X
ISSN	1439-7609 ; 1439-7595
ISSN (online)	1439-7609
ISSN	1439-7595
DOI	10.1007/s10165-011-0480-1
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Article: [Mechanism of intracellular parasitism by Mycobacterium tuberculosis].

Seto, Shintaro / Tsujimura, Kunio / Koide, Yukio

Nihon rinsho. Japanese journal of clinical medicine

2011 Volume 69, Issue 8, Page(s) 1373–1377

Abstract: Mycobacterium tuberculosis is an intracellular bacterium that can replicate within infected macrophages. The intracellular parasitism by M. tuberculosis results from arresting phagosome maturation and inhibiting phagolysosome biogenesis in infected ... ...

Abstract	Mycobacterium tuberculosis is an intracellular bacterium that can replicate within infected macrophages. The intracellular parasitism by M. tuberculosis results from arresting phagosome maturation and inhibiting phagolysosome biogenesis in infected macrophages. It has been thought that M. tuberculosis arrests the maturation of its phagosome at the early stage. Several reports attended to the localization of Rab GTPases on mycobacterial phagosomes. Rab GTPases regulate membrane trafficking, but details of how Rab GTPases regulate phagosome maturation and how M. tuberculosis modulates their activities during inhibiting phagolysosome biogenesis remains elusive. Here, we introduce the new findings that M. tuberculosis alters the localization of Rab GTPases regulating phagosome maturation during inhibiting phagolysosome biogenesis.
MeSH term(s)	Macrophages/microbiology ; Mycobacterium tuberculosis/physiology ; Phagosomes/physiology ; rab GTP-Binding Proteins/metabolism
Chemical Substances	rab GTP-Binding Proteins (EC 3.6.5.2)
Language	Japanese
Publishing date	2011-08
Publishing country	Japan
Document type	Journal Article ; Review
ZDB-ID	390903-7
ISSN	0047-1852
ISSN	0047-1852
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Article ; Online: Mobility of late endosomal and lysosomal markers on phagosomes analyzed by fluorescence recovery after photobleaching.

Sugaya, Keiko / Seto, Shintaro / Tsujimura, Kunio / Koide, Yukio

Biochemical and biophysical research communications

2011 Volume 410, Issue 2, Page(s) 371–375

Abstract: During phagosome maturation, the late endosomal marker Rab7 and the lysosomal marker LAMP1 localize to the phagosomes. We investigated the mobility of Rab7 and LAMP1 on the phagosomes in macrophages by fluorescence recovery after photobleaching (FRAP) ... ...

Abstract	During phagosome maturation, the late endosomal marker Rab7 and the lysosomal marker LAMP1 localize to the phagosomes. We investigated the mobility of Rab7 and LAMP1 on the phagosomes in macrophages by fluorescence recovery after photobleaching (FRAP) analysis. Rab7 was mobile between the phagosomal membrane and the cytosol in macrophages that ingested latex beads during phagosome maturation. The addition of interferon-γ (IFN-γ) restricted this mobility, suggesting that Rab7 is forced to bind to the phagosomal membrane by IFN-γ-mediated activation. Immobilization of LAMP1 on the phagosomes was observed irrespective of IFN-γ-activation. We further examined the mobility of Rab7 on the phagosomes containing Mycobacterium bovis BCG by FRAP analysis. The rate of fluorescence recovery for Rab7 on mycobacterial phagosomes was lower than that on the phagosomes containing latex beads, suggesting that mycobacteria impaired the mobility of Rab7 and arrested phagosome maturation.
MeSH term(s)	Animals ; Biomarkers/metabolism ; Cell Line ; Endosomes/metabolism ; Endosomes/microbiology ; Fluorescence Recovery After Photobleaching ; Interferon-gamma/pharmacology ; Lysosomal Membrane Proteins/metabolism ; Lysosomes/metabolism ; Macrophages/metabolism ; Mice ; Microspheres ; Mycobacterium bovis/immunology ; Phagosomes/metabolism ; Phagosomes/microbiology ; rab GTP-Binding Proteins/metabolism ; rab7 GTP-Binding Proteins
Chemical Substances	Biomarkers ; Lamp1 protein, mouse ; Lysosomal Membrane Proteins ; rab7 GTP-Binding Proteins ; rab7 GTP-binding proteins, mouse ; Interferon-gamma (82115-62-6) ; rab GTP-Binding Proteins (EC 3.6.5.2)
Language	English
Publishing date	2011-06-12
Publishing country	United States
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	205723-2
ISSN	1090-2104 ; 0006-291X ; 0006-291X
ISSN (online)	1090-2104 ; 0006-291X
ISSN	0006-291X
DOI	10.1016/j.bbrc.2011.06.023
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Article ; Online: Rab GTPases regulating phagosome maturation are differentially recruited to mycobacterial phagosomes.

Seto, Shintaro / Tsujimura, Kunio / Koide, Yukio

Traffic (Copenhagen, Denmark)

2011 Volume 12, Issue 4, Page(s) 407–420

Abstract: Mycobacterium tuberculosis (M. tb) is an intracellular pathogen that can replicate within infected macrophages. The ability of M. tb to arrest phagosome maturation is believed to facilitate its intracellular multiplication. Rab GTPases regulate membrane ... ...

Abstract	Mycobacterium tuberculosis (M. tb) is an intracellular pathogen that can replicate within infected macrophages. The ability of M. tb to arrest phagosome maturation is believed to facilitate its intracellular multiplication. Rab GTPases regulate membrane trafficking, but details of how Rab GTPases regulate phagosome maturation and how M. tb modulates their localization during inhibiting phagolysosome biogenesis remain elusive. We compared the localization of 42 distinct Rab GTPases to phagosomes containing either Staphylococcus aureus or M. tb. The phagosomes containing S. aureus were associated with 22 Rab GTPases, but only 5 of these showed similar localization kinetics as the phagosomes containing M. tb. The Rab GTPases responsible for phagosome maturation, phagosomal acidification and recruitment of cathepsin D were examined in macrophages expressing the dominant-negative form of each Rab GTPase. LysoTracker staining and immunofluorescence microscopy revealed that Rab7, Rab20 and Rab39 regulated phagosomal acidification and Rab7, Rab20, Rab22b, Rab32, Rab34, Rab38 and Rab43 controlled the recruitment of cathepsin D to the phagosome. These results suggest that phagosome maturation is achieved by a series of interactions between Rab GTPases and phagosomes and that differential recruitment of these Rab GTPases, except for Rab22b and Rab43, to M. tb-containing phagosomes is involved in arresting phagosome maturation and inhibiting phagolysosome biogenesis.
MeSH term(s)	Cathepsin D/metabolism ; Cell Proliferation ; Macrophages/metabolism ; Macrophages/microbiology ; Mycobacterium tuberculosis/metabolism ; Phagosomes/enzymology ; Phagosomes/metabolism ; Phagosomes/microbiology ; Protein Transport ; Staphylococcus aureus/metabolism ; rab GTP-Binding Proteins/metabolism
Chemical Substances	Cathepsin D (EC 3.4.23.5) ; rab GTP-Binding Proteins (EC 3.6.5.2)
Language	English
Publishing date	2011-04
Publishing country	England
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	1483852-7
ISSN	1600-0854 ; 1398-9219
ISSN (online)	1600-0854
ISSN	1398-9219
DOI	10.1111/j.1600-0854.2011.01165.x
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Article: Differential recruitment of CD63 and Rab7-interacting-lysosomal-protein to phagosomes containing Mycobacterium tuberculosis in macrophages.

Seto, Shintaro / Matsumoto, Sohkichi / Tsujimura, Kunio / Koide, Yukio

Microbiology and immunology

2010 Volume 54, Issue 3, Page(s) 170–174

Abstract: M.tb is an intracellular pathogen which survives within the phagosomes of host macrophages by inhibiting their fusion with lysosomes. Here, it has been demonstrated that a lysosomal glycoprotein, CD63, is recruited to the majority of M.tb phagosomes, ... ...

Abstract	M.tb is an intracellular pathogen which survives within the phagosomes of host macrophages by inhibiting their fusion with lysosomes. Here, it has been demonstrated that a lysosomal glycoprotein, CD63, is recruited to the majority of M.tb phagosomes, while RILP shows limited localization. This is consistent with the author's findings that CD63, but not RILP, is recruited to the phagosomes in macrophages expressing the dominant negative form of Rab7. These results suggest that M.tb phagosomes selectively fuse with endosomes and lysosomes to escape killing activity while acquiring nutrients.
MeSH term(s)	Adaptor Proteins, Signal Transducing ; Animals ; Antigens, CD/metabolism ; Carrier Proteins/metabolism ; Cell Line ; Lysosomes/metabolism ; Lysosomes/microbiology ; Macrophages/metabolism ; Macrophages/microbiology ; Mice ; Mycobacterium tuberculosis/physiology ; Phagosomes/metabolism ; Phagosomes/microbiology ; Platelet Membrane Glycoproteins/metabolism ; Protein Binding ; Protein Transport ; Tetraspanin 30 ; Tuberculosis/immunology ; Tuberculosis/metabolism ; Tuberculosis/microbiology ; rab GTP-Binding Proteins/metabolism
Chemical Substances	Adaptor Proteins, Signal Transducing ; Antigens, CD ; Carrier Proteins ; Cd63 protein, mouse ; Platelet Membrane Glycoproteins ; Rilp protein, mouse ; Tetraspanin 30 ; rab7 protein (152989-05-4) ; rab GTP-Binding Proteins (EC 3.6.5.2)
Language	English
Publishing date	2010-03
Publishing country	Australia
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	224792-6
ISSN	1348-0421 ; 0385-5600
ISSN (online)	1348-0421
ISSN	0385-5600
DOI	10.1111/j.1348-0421.2010.00199.x
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Article ; Online: Rab39a interacts with phosphatidylinositol 3-kinase and negatively regulates autophagy induced by lipopolysaccharide stimulation in macrophages.

Seto, Shintaro / Sugaya, Keiko / Tsujimura, Kunio / Nagata, Toshi / Horii, Toshinobu / Koide, Yukio

PloS one

2013 Volume 8, Issue 12, Page(s) e83324

Abstract: Rab39a has pleiotropic functions in phagosome maturation, inflammatory activation and neuritogenesis. Here, we characterized Rab39a function in membrane trafficking of phagocytosis and autophagy induction in macrophages. Rab39a localized to the periphery ...

Abstract	Rab39a has pleiotropic functions in phagosome maturation, inflammatory activation and neuritogenesis. Here, we characterized Rab39a function in membrane trafficking of phagocytosis and autophagy induction in macrophages. Rab39a localized to the periphery of LAMP2-positive vesicles and showed the similar kinetics on the phagosome to that of LAMP1. The depletion of Rab39a did not influence the localization of LAMP2 to the phagosome, but it augments the autophagosome formation and LC3 processing by lipopolysaccharide (LPS) stimulation. The augmentation of autophagosome formation in Rab39a-knockdown macrophages was suppressed by Atg5 depletion or an inhibitor for phosphatidylinostol 3-kinase (PI3K). Immunoprecipitation analysis revealed that Rab39a interacts with PI3K and that the amino acid residues from 34(th) to 41(st) in Rab39a were indispensable for this interaction. These results suggest that Rab39a negatively regulates the LPS-induced autophagy in macrophages.
MeSH term(s)	Animals ; Autophagy/drug effects ; Autophagy/physiology ; Cell Line ; Humans ; Lipopolysaccharides/pharmacology ; Lysosomal Membrane Proteins/genetics ; Lysosomal Membrane Proteins/metabolism ; Macrophages/cytology ; Macrophages/metabolism ; Mice ; Mice, Knockout ; Phosphatidylinositol 3-Kinases/genetics ; Phosphatidylinositol 3-Kinases/metabolism ; Protein Binding/drug effects ; Protein Binding/physiology ; rab GTP-Binding Proteins/genetics ; rab GTP-Binding Proteins/metabolism
Chemical Substances	Lamp1 protein, mouse ; Lipopolysaccharides ; Lysosomal Membrane Proteins ; Phosphatidylinositol 3-Kinases (EC 2.7.1.-) ; Rab39A protein, mouse (EC 3.6.1.-) ; rab GTP-Binding Proteins (EC 3.6.5.2)
Language	English
Publishing date	2013-12-13
Publishing country	United States
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	2267670-3
ISSN	1932-6203 ; 1932-6203
ISSN (online)	1932-6203
ISSN	1932-6203
DOI	10.1371/journal.pone.0083324
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