CoChat
Sign Up
Cited by 79Tuberculosis Research and EpidemiologyAutophagy in Disease and TherapyImmune responses and vaccinations

Autophagy in Immune Defense Against Mycobacterium tuberculosis

Open access
Vergne, Isabelle, Singh, Sudha, Roberts, Esteban, Kyei, George, Master, Sharon, Harris, James, Haro, Sergio de, Naylor, John +3 more·2006·Autophagy
DOI 10.4161/auto.2830
Open this paper in CoChat — free accountOpen PDF

Abstract

Autophagy is a newly recognized innate and adaptive immunity defense against intracellular pathogens, in keeping with its role as a cytoplasmic maintenance pathway. Induction of autophagy by physiological, pharmacological or immunological means can eliminate intracellular Mycobacterium tuberculosis, providing one of the first examples of the immunological role of autophagy. Under normal circumstances, M. Tuberculosis survives in macrophages by inhibiting phagolysosome biogenesis. Induction of autophagy overcomes the mycobacterial phagosome maturation block, and delivers the tubercle bacilli to degradative compartments where they are eliminated.

The claims and statistics of this paper haven’t been checked yet.

Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.

A few free checks a day · papers already verified open instantly · results are public

Integrity signals

Registry

Crossref · 10.4161/auto.2830

Cites

1 of 1 references verified0 citation errors · 0 not checkable

Statistics

Claims the paper makes

The claims and statistics of this paper haven’t been checked yet.

Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.

A few free checks a day · papers already verified open instantly · results are public

Claims other papers make about this one

Each is checked against this paper’s own text: does it say what the citing paper says it does?

  • The autophagic machinery following pathogen entry into cells can target either bacteria-containing phagosomes or free cytosolic bacteria.

    “The autophagic machinery following the entry of the pathogen into cells can target either bacteria-containing phagosomes, or free cytosolic bacteria [8,9,10,11].”

    From LC3-Associated Phagocytosis (LAP): Connections with Host Autophagy (2012) · cites this paper as [9]

    The IFN-γ–mediated autophagy section proposes that autophagosomes can engulf phagosomes containing mycobacteria, supporting the phagosome part of the claim. The Conclusion raises bacterial escape from isolation membranes as a question, but our copy does not establish that autophagy targets free cytosolic bacteria. (LLM, conf=0.85)

    Experimental — accuracy not yet measured

  • Emerging evidence indicates that LC3 and GABARAP proteins may be involved in recognizing distinct sets of cargoes for selective autophagy.

    “emerging evidence indicates that LC3 and GABARAP proteins may be involved in recognizing distinct sets of cargoes for selective autophagy.”

    From Guidelines for the use and interpretation of assays for monitoring autophagy (3rd edition). (2016) · cites this paper as [125]

    The Conclusion figure caption (page unavailable) identifies LC3 as an autophagy protein, but does not discuss cargo recognition. Searches for GABARAP, distinct cargoes, and selective autophagy found no passage in our copy addressing whether LC3 and GABARAP recognize different cargoes. (LLM, conf=0.76)

    Experimental — accuracy not yet measured

Self-check

Percentages, sums and reported differences re-computed from the paper’s own numbers.

The self-check needs the paper’s full text.

Cites

Flagged first, then by citations

Research works printed but not linked: 39

  1. Vergne I, Chua J, Singh SB, Deretic V. Cell biology of mycobacterium tuberculosis phago- some. Annu Rev Cell Dev Biol 2004; 20:367-94.
  2. Russell DG. Mycobacterium tuberculosis: Here today, and here tomorrow. Nat Rev Mol Cell Biol 2001; 2:569-77.
  3. Ramachandra L, Noss E, Boom WH, Harding CV. Processing of Mycobacterium tuberculosis antigen 85B involves intraphagosomal formation of peptide-major histocompatibility complex II complexes and is inhibited by live bacilli that decrease phagosome maturation. J Exp Med 2001; 194:1421-32.
  4. Via LE, Deretic D, Ulmer RJ, Hibler NS, Huber LA, Deretic V. Arrest of mycobacterial phagosome maturation is caused by a block in vesicle fusion between stages controlled by rab5 and rab7. J Biol Chem 1997; 272:13326-31.
  5. Fratti RA, Backer JM, Gruenberg J, Corvera S, Deretic V. Role of phosphatidylinositol 3-kinase and Rab5 effectors in phagosomal biogenesis and mycobacterial phagosome maturation arrest. J Cell Biol 2001; 154:631-44.
  6. Vieira OV, Harrison RE, Scott CC, Stenmark H, Alexander D, Liu J, Gruenberg J, Schreiber AD, Grinstein S. Acquisition of Hrs, an essential component of phagosomal mat- uration, is impaired by mycobacteria. Mol Cell Biol 2004; 24:4593-604.
  7. Simonsen A, Lippe R, Christoforidis S, Gaullier JM, Brech A, Callaghan J, Toh BH, Murphy C, Zerial M, Stenmark H. EEA1 links PI(3)K function to Rab5 regulation of endosome fusion. Nature 1998; 394:494-8.
  8. Kauppi M, Simonsen A, Bremnes B, Vieira A, Callaghan J, Stenmark H, Olkkonen VM. The small GTPase Rab22 interacts with EEA1 and controls endosomal membrane traf- ficking. J Cell Sci 2002; 115:899-911.
  9. Vieira OV, Botelho RJ, Rameh L, Brachmann SM, Matsuo T, Davidson HW, Schreiber A, Backer JM, Cantley LC, Grinstein S. Distinct roles of class I and class III phosphatidyli- nositol 3-kinases in phagosome formation and maturation. J Cell Biol 2001; 155:19-25.
  10. Stack JH, Emr SD. Vps34p required for yeast vacuolar protein sorting is a multiple specificity kinase that exhibits both protein kinase and phosphatidylinositol-specific PI 3-kinase activities. J Biol Chem 1994; 269:31552-62.
  11. Fratti RA, Chua J, Vergne I, Deretic V. Mycobacterium tuberculosis glycosylated phos- phatidylinositol causes phagosome maturation arrest. Proc Natl Acad Sci USA 2003; 100:5437-42.
  12. Chua J, Deretic V. Mycobacterium tuberculosis reprograms waves of phosphatidylinositol 3-phosphate on phagosomal organelles. J Biol Chem 2004; 279:36982-92.
  13. Vergne I, Chua J, Lee HH, Lucas M, Belisle J, Deretic V. Mechanism of phagolysosome biogenesis block by viable Mycobacterium tuberculosis. Proc Natl Acad Sci USA 2005; 102:4033-38.
  14. Purdy GE, Owens RM, Bennett L, Russell DG, Butcher BA. Kinetics of phosphatidyli- nositol-3-phosphate acquisition differ between IgG bead-containing phagosomes and Mycobacterium tuberculosis-containing phagosomes. Cell Microbiol 2005; 7:1627-34.
  15. Vergne I, Chua J, Deretic V. Tuberculosis toxin blocking phagosome maturation inhibits a novel Ca2+/calmodulin-PI3K hVPS34 cascade. J Exp Med 2003; 198:653-9.
  16. Gutierrez MG, Master SS, Singh SB, Taylor GA, Colombo MI, Deretic V. Autophagy is a defense mechanism inhibiting BCG and Mycobacterium tuberculosis survival in infected macrophages. Cell 2004; 119:753-66.
  17. Dengjel J, Schoor O, Fischer R, Reich M, Kraus M, Muller M, Kreymborg K, Altenberend F, Brandenburg J, Kalbacher H, Brock R, Driessen HG. Autophagy promotes MHC class II presentation of peptides from intracellular source proteins. Proc Natl Acad Sci USA 2005; 102:7922-7.
  18. Scarlatti F, Bauvy C, Ventruti A, Sala G, Cluzeaud F, Vandewalle A, Ghidoni R, Codogno P. Ceramide-mediated macroautophagy involves inhibition of protein kinase B and upreg- ulation of beclin 1. J Biol Chem 2004; 279:18384-91.
  19. Pattingre S, Tassa A, Qu X, Garuti R, Liang XH, Mizushima N, Packer M, Schneider MD, Levine B. Bcl-2 antiapoptotic proteins inhibit Beclin 1-dependent autophagy. Cell 2005; 122:927-39.
  20. Lavieu G, Scarlatti F, Sala G, Carpentier S, Levade T, Ghidoni R, Botti J, Codogno P. Regulation of autophagy by sphingosine kinase 1 and its role in cell survival during nutrient starvation. J Biol Chem 2006; 281:8518-27.
  21. Hoyer-Hansen M, Bastholm L, Mathiasen IS, Elling F, Jaattela M. Vitamin D analog EB1089 triggers dramatic lysosomal changes and Beclin 1-mediated autophagic cell death. Cell Death Differ 2005; 12:1297-309.
  22. Garg SK, Volpe E, Palmieri G, Mattei M, Galati D, Martino A, Piccioni MS, Valente E, Bonanno E, De Vito P, Baldini PM, Spagnoli LG, Colizzi V, Fraziano M. Sphingosine 1-phosphate induces antimicrobial activity both in vitro and in vivo. J Infect Dis 2004; 189:2129-38.
  23. Anes E, Kuhnel MP, Bos E, Moniz-Pereira J, Habermann A, Griffiths G. Selected lipids activate phagosome actin assembly and maturation resulting in killing of pathogenic mycobacteria. Nat Cell Biol 2003; 5:793-802.
  24. Hmama Z, Sendide K, Talal A, Garcia R, Dobos K, Reiner NE. Quantitative analysis of phagolysosome fusion in intact cells: Inhibition by mycobacterial lipoarabinomannan and rescue by an 1alpha,25-dihydroxyvitamin D3-phosphoinositide 3-kinase pathway. J Cell Sci 2004; 117:2131-40.
  25. Liu PT, Stenger S, Li H, Wenzel L, Tan BH, Krutzik SR, Ochoa MT, Schauber J, Wu K, Meinken C, Kamen DL, Wagner M, Bals R, Steinmeyer A, Zugel U, Gallo RL, Eisenberg D, Hewison M, Hollis BW, Adams JS, Bloom BR, Modlin RL. Toll-like receptor triggering of a vitamin D-mediated human antimicrobial response. Science 2006; 311:1770-3.
  26. de Chastellier C, Thilo L. Cholesterol depletion in Mycobacterium avium-infected macrophages overcomes the block in phagosome maturation and leads to the reversible sequestration of viable mycobacteria in phagolysosome-derived autophagic vacuoles. Cell Microbiol 2006; 8:242-56.
  27. Manca C, Reed MB, Freeman S, Mathema B, Kreiswirth B, Barry IIIrd CE, Kaplan G. Differential monocyte activation underlies strain-specific Mycobacterium tuberculosis pathogenesis. Infect Immun 2004; 72:5511-14.
  28. Arico S, Petiot A, Bauvy C, Dubbelhuis PF, Meijer AJ, Codogno P, Ogier-Denis E. The tumor suppressor PTEN positively regulates macroautophagy by inhibiting the phos- phatidylinositol 3-kinase/protein kinase B pathway. J Biol Chem 2001; 276:35243-6.
  29. Inbal B, Bialik S, Sabanay I, Shani G, Kimchi A. DAP kinase and DRP-1 mediate membrane blebbing and the formation of autophagic vesicles during programmed cell death. J Cell Biol 2002; 157:455-68.
  30. Deretic V. Autophagy in innate and adaptive immunity. Trends Immunol 2005; 26:523-8. 2006; Vol. 2 Issue 3
  31. Via LE, Fratti RA, McFalone M, Pagan-Ramos E, Deretic D, Deretic V. Effects of cytokines on mycobacterial phagosome maturation. J Cell Sci 1998; 111:897-905.
  32. Bekpen C, Hunn JP, Rohde C, Parvanova I, Guethlein L, Dunn DM, Glowalla E, Leptin M, Howard JC. The interferon-inducible p47 (IRG) GTPases in vertebrates: Loss of the cell autonomous resistance mechanism in the human lineage. Genome Biol 2005; 6:R92.
  33. MacMicking JD, Taylor GA, McKinney JD. Immune control of tuberculosis by IFN- gamma-inducible LRG-47. Science 2003; 302:654-9.
  34. Ghosh A, Uthaiah R, Howard J, Herrmann C, Wolf E. Crystal structure of IIGP1: A paradigm for interferon-inducible p47 resistance GTPases. Mol Cell 2004; 15:727-39.
  35. Klionsky DJ. The molecular machinery of autophagy: Unanswered questions. J Cell Sci 2005; 118:7-18.
  36. Taylor GA, Stauber R, Rulong S, Hudson E, Pei V, Pavlakis GN, Resau JH, Vande Woude GF. The inducibly expressed GTPase localizes to the endoplasmic reticulum, independently of GTP binding. J Biol Chem 1997; 272:10639-45.
  37. Martens S, Sabel K, Lange R, Uthaiah R, Wolf E, Howard JC. Mechanisms regulating the positioning of mouse p47 resistance GTPases LRG-47 and IIGP1 on cellular membranes: Retargeting to plasma membrane induced by phagocytosis. J Immunol 2004; 173:2594-606.
  38. Kaiser F, Kaufmann SH, Zerrahn J. IIGP, a member of the IFN inducible and microbial defense mediating 47 kDa GTPase family, interacts with the microtubule binding protein hook3. J Cell Sci 2004; 117:1747-56.
  39. Walenta JH, Didier AJ, Liu X, Kramer H. The Golgi-associated hook3 protein is a member of a novel family of microtubule-binding proteins. J Cell Biol 2001; 152:923-34.

Cited by

Sorted by citations

Authors
Vergne, I., Singh, S., Roberts, E., Kyei, G., Master, S., Harris, J., Haro, S. D., Naylor, J., Davis, A., Delgado, M., & Deretic, V.
Affiliations
University of New Mexico (US)
ORCID
Venue
Autophagy
Publisher
Informa UK Limited
Published
2006-07-22
Volume
2
Issue
3
Pages
175-178
ISSN
  • 1554-8627 (ISSN-L)
  • 1554-8635
DOI
10.4161/auto.2830
OpenAlex
W2046282973
Cited by
79
References
1
Citations by year
2025: 1 · 2024: 1 · 2023: 3 · 2022: 2 · 2021: 3 · 2020: 5 · 2019: 4 · 2018: 2 · 2017: 3 · 2016: 8 · 2015: 3 · 2014: 7 · 2013: 4 · 2012: 7
FWCI
0.61
Type
journal article
Language
en
Open access
Locations
  • Autophagy (publishedVersion)
  • PubMed (publishedVersion)
Funders
  • National Institutes of Health
  • National Institute of Allergy and Infectious Diseases (T32AI007538, AI42999, AI 45148, R01AI045148)
Topics
  • Health Sciences › Medicine › Infectious Diseases › Tuberculosis Research and Epidemiology
  • Health Sciences › Medicine › Epidemiology › Autophagy in Disease and Therapy
  • Life Sciences › Immunology and Microbiology › Immunology › Immune responses and vaccinations
Keywords
Mycobacterium tuberculosis, tuberculosis, innate immunity, adaptive immunity, macrophages, phagosome maturation, phagolysosome biogenesis, intracellular pathogen clearance, host-pathogen interaction
MeSH terms
Autophagy, Humans, Interferon-gamma, Lipids, Macrophages, Models, Biological, Mycobacterium tuberculosis, Phagocytosis, Phagosomes, Tuberculosis, Cytokines, Phosphatidylinositol Phosphates, Th2 Cells, GTP Phosphohydrolases, Microbial Viability

About these checks

Registry, retraction, Cites and statistics results are computed, not judged, with one exception: a printed reference that no index lists is read once by a model before it counts as a citation error. Claims are extracted by a model and kept only when their quote appears verbatim in the text; each cited source is then checked, with a model’s help, for whether it says what the claim relies on. Those verdicts can be wrong — read the claim’s quote and the cited source before relying on one.

Statistics and arithmetic are recomputed, not judged.

Confidence bands are shown only for fields calibrated on our annotated test set. None is calibrated yet, so no band is shown.

What counts as a claim ›How we measure confidence ›How we check this ›

Are you an author, or do you see a problem with this page? Request a review