Tom Holland would like to act in a Jak & Daxter film
Tom Holland, an actor best known for playing Spider-Man and the upcoming Uncharted movie, has revealed which film adaptation of a video game he would like to participate in: Jak & Dexter. But his proposal is a bit strange.Speaking with GameSpot, Tom Holland said: "I would like to make a Jak & Dexter film and I would play Jak, but I would have A24 make it, so as to make it very strange and dark. I would like to make some sort of absurd live-action version of Jak & Daxter. "
Jak and Daxter Holland really specify that he wants a live-action film, not an animated product. Obviously this is a far-fetched idea, which we do not really believe can ever be realized, but for sure the actor's idea is original.
In case you don't know it, let's specify that A24 is an American independent film distribution and production house that has worked on Midsommar, Sir Gawain and the Green Knight, and the new adaptation of Macbeth.
We should also remember that Jak & Daxter has not been in the videogame scene for many years and its return is by no means easy, as Naughty Dog also explains.
Source Have you noticed any errors?
Bacterial manipulation of innate immunity to promote infection
Alexopoulou, L. & Kontoyiannis, D. Contribution of microbial-associated molecules in innate mucosal responses. Cell. Mol. Life Sci. 62, 1349–1358 (2005).
Hibino, T. et al. The immune gene repertoire encoded in the purple sea urchin genome. Dev. Biol. 300, 349–365 (2006).
Akashi-Takamura, S. & Miyake, K. TLR accessory molecules. Curr. Opin. Immunol. 20, 420–425 (2008).
Kumar, Y. & Valdivia, R. H. Leading a sheltered life: intracellular pathogens and maintenance of vacuolar compartments. Cell Host Microbe 5, 593–601 (2009). This review concentrates on the strategies used by vacuole-bound pathogens to invade and establish a replicative vacuole and also on what are the mechanisms involved in pathogenic vacuole maintenance and disruption.
Neyrolles, O. et al. Is adipose tissue a place for Mycobacterium tuberculosis persistence? PLoS One 1, e43 (2006).
Tailleux, L., Maeda, N., Nigou, J., Gicquel, B. & Neyrolles, O. How is the phagocyte lectin keyboard played? Master class lesson by Mycobacterium tuberculosis. Trends Microbiol. 11, 259–263 (2003).
Yadav, M. & Schorey, J. S. The β-glucan receptor dectin-1 functions together with TLR2 to mediate macrophage activation by mycobacteria. Blood 108, 3168–3175 (2006).
Korbel, D. S., Schneider, B. E. & Schaible, U. E. Innate immunity in tuberculosis: myths and truth. Microbes Infect. 10, 995–1004 (2008).
Flannagan, R. S., Cosio, G. & Grinstein, S. Antimicrobial mechanisms of phagocytes and bacterial evasion strategies. Nature Rev. Microbiol. 7, 355–366 (2009).
Cooper, A. M. Cell-mediated immune responses in tuberculosis. Annu. Rev. Immunol. 27, 393–422 (2009).
Bonazzi, M., Lecuit, M. & Cossart, P. Listeria monocytogenes internalin and E-cadherin: from structure to pathogenesis. Cell. Microbiol. 11, 693–702 (2009).
Dehio, C. Bartonella interactions with endothelial cells and erythrocytes. Trends Microbiol. 9, 279–285 (2001).
Kubori, T. et al. Supramolecular structure of the Salmonella typhimurium type III protein secretion system. Science 280, 602–605 (1998).
Unsworth, K. E., Way, M., McNiven, M., Machesky, L. & Holden, D. W. Analysis of the mechanisms of Salmonella-induced actin assembly during invasion of host cells and intracellular replication. Cell. Microbiol. 6, 1041–1055 (2004).
Patel, J. C. & Galan, J. E. Manipulation of the host actin cytoskeleton by Salmonella — all in the name of entry. Curr. Opin. Microbiol. 8, 10–15 (2005).
Patel, J. C., Rossanese, O. W. & Galan, J. E. The functional interface between Salmonella and its host cell: opportunities for therapeutic intervention. Trends Pharmacol. Sci. 26, 564–570 (2005).
Patel, J. C. & Galan, J. E. Differential activation and function of Rho GTPases during Salmonella-host cell interactions. J. Cell Biol. 175, 453–463 (2006).
Kaniga, K., Uralil, J., Bliska, J. B. & Galan, J. E. A secreted protein tyrosine phosphatase with modular effector domains in the bacterial pathogen Salmonella typhimurium. Mol. Microbiol. 21, 633–641 (1996).
Li, G. & Zhang, X. C. GTP hydrolysis mechanism of Ras-like GTPases. J. Mol. Biol. 340, 921–932 (2004).
Fu, Y. & Galan, J. E. A salmonella protein antagonizes Rac-1 and Cdc42 to mediate host-cell recovery after bacterial invasion. Nature 401, 293–297 (1999). This article shows that the S . Typhimurium effector protein SptP delivered to the host cell cytosol by the T3SS acts as a GAP for RAC1 and CDC42, leading to the reversal of the actin cytoskeletal changes induced on bacterium entry.
Murli, S., Watson, R. O. & Galan, J. E. Role of tyrosine kinases and the tyrosine phosphatase SptP in the interaction of Salmonella with host cells. Cell. Microbiol. 3, 795–810 (2001).
Haraga, A. & Miller, S. I. A Salmonella enterica serovar typhimurium translocated leucine-rich repeat effector protein inhibits NF-κ B-dependent gene expression. Infect. Immun. 71, 4052–4058 (2003).
Collier-Hyams, L. S. et al. Cutting edge: Salmonella AvrA effector inhibits the key proinflammatory, anti-apoptotic NF-κ B pathway. J. Immunol. 169, 2846–2850 (2002).
Nhieu, G. T. & Sansonetti, P. J. Mechanism of Shigella entry into epithelial cells. Curr. Opin. Microbiol. 2, 51–55 (1999).
Lafont, F., Tran Van Nhieu, G., Hanada, K., Sansonetti, P. & van der Goot, F. G. Initial steps of Shigella infection depend on the cholesterol/sphingolipid raft-mediated CD44-IpaB interaction. EMBO J. 21, 4449–4457 (2002).
Niebuhr, K. et al. Conversion of PtdIns(4, 5)P2 into PtdIns(5)P by the S.flexneri effector IpgD reorganizes host cell morphology. EMBO J. 21, 5069–5078 (2002).
Salcedo, S. P. et al. Brucella control of dendritic cell maturation is dependent on the TIR-containing protein Btp1. PLoS Pathog. 4, e21 (2008). This article describes for the first time the Brucella spp. TIR-interacting protein Btp1, which interferes with TLR2 signalling and induces an arrest in the DC maturation process.
Newman, R. M., Salunkhe, P., Godzik, A. & Reed, J. C. Identification and characterization of a novel bacterial virulence factor that shares homology with mammalian Toll/interleukin-1 receptor family proteins. Infect. Immun. 74, 594–601 (2006).
Cirl, C. et al. Subversion of Toll-like receptor signalling by a unique family of bacterial Toll/interleukin-1 receptor domain-containing proteins. Nature Med. 14, 399–406 (2008). The authors characterize TIR domain-containing proteins in pathogenic bacteria. E. coli TcpC promotes bacterial survival and kidney pathology in vivo and inhibits TLR- and MYD88-specific signalling.
Radhakrishnan, G. K., Yu, Q., Harms, J. S. & Splitter, G. A. Brucella TIR domain-containing protein mimics properties of the toll-like receptor adaptor protein TIRAP. J. Biol. Chem. 284, 9892–9898 (2009).
Lapaque, N., Moriyon, I., Moreno, E. & Gorvel, J. P. Brucella lipopolysaccharide acts as a virulence factor. Curr. Opin. Microbiol. 8, 60–66 (2005).
Fugier, E., Pappas, G. & Gorvel, J. P. Virulence factors in brucellosis: implications for aetiopathogenesis and treatment. Expert Rev. Mol. Med. 9, 1–10 (2007).
Ganguly, N. et al. Mycobacterium tuberculosis secretory proteins CFP-10, ESAT-6 and the CFP10:ESAT6 complex inhibit lipopolysaccharide-induced NF-κB transactivation by downregulation of reactive oxidative species (ROS) production. Immunol. Cell Biol. 86, 98–106 (2008).
Ganguly, N. et al. Mycobacterium tuberculosis 6-kDa early secreted antigenic target (ESAT-6) protein downregulates lipopolysaccharide induced c-myc expression by modulating the extracellular signal regulated kinases 1/2. BMC Immunol. 8, 24 (2007).
High, N., Mounier, J., Prevost, M. C. & Sansonetti, P. J. IpaB of Shigella flexneri causes entry into epithelial cells and escape from the phagocytic vacuole. EMBO J. 11, 1991–1999 (1992).
Pizarro-Cerda, J. & Cossart, P. Subversion of cellular functions by Listeria monocytogenes. J. Pathol. 208, 215–223 (2006).
Corr, S. C. & O'Neill, L. A. Listeria monocytogenes infection in the face of innate immunity. Cell. Microbiol. 11, 703–709 (2009).
Goldberg, M. B. Actin-based motility of intracellular microbial pathogens. Microbiol. Mol. Biol. Rev. 65, 595–626 (2001).
Perrin, A. J., Jiang, X., Birmingham, C. L., So, N. S. & Brumell, J. H. Recognition of bacteria in the cytosol of mammalian cells by the ubiquitin system. Curr. Biol. 14, 806–811 (2004).
de Chastellier, C., Forquet, F., Gordon, A. & Thilo, L. Mycobacterium requires an all-around closely apposing phagosome membrane to maintain the maturation block and this apposition is re-established when it rescues itself from phagolysosomes. Cell. Microbiol. 11, 1190–1207 (2009).
Fratti, R. A., Backer, J. M., 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. 154, 631–644 (2001).
Philips, J. A. Mycobacterial manipulation of vacuolar sorting. Cell. Microbiol. 10, 2408–2415 (2008).
Vergne, I. et al. Mechanism of phagolysosome biogenesis block by viable Mycobacterium tuberculosis. Proc. Natl Acad. Sci. USA 102, 4033–4038 (2005).
Shabaana, A. K. et al. Mycobacterial lipoarabinomannans modulate cytokine production in human T helper cells by interfering with raft/microdomain signalling. Cell. Mol. Life Sci. 62, 179–187 (2005).
Welin, A. et al. Incorporation of Mycobacterium tuberculosis lipoarabinomannan into macrophage membrane rafts is a prerequisite for the phagosomal maturation block. Infect. Immun. 76, 2882–2887 (2008).
Robinson, N. et al. Mycobacterial phenolic glycolipid inhibits phagosome maturation and subverts the pro-inflammatory cytokine response. Traffic 9, 1936–1947 (2008). In this paper the authors characterize a glycolipid of M. marinum , phenolphthiocerol diester, which promotes the arrest of phagosome maturation and abrogates pro-inflammatory cytokine production in human monocyte-derived macrophages.
Axelrod, S. et al. Delay of phagosome maturation by a mycobacterial lipid is reversed by nitric oxide. Cell. Microbiol. 10, 1530–1545 (2008).
Vergne, I., Chua, J. & Deretic, V. Mycobacterium tuberculosis phagosome maturation arrest: selective targeting of PI3P-dependent membrane trafficking. Traffic 4, 600–6 (2003).
Meresse, S., Steele-Mortimer, O., Finlay, B. B. & Gorvel, J. P. The rab7 GTPase controls the maturation of Salmonella typhimurium-containing vacuoles in HeLa cells. EMBO J. 18, 4394–4403 (1999).
Knodler, L. A. & Steele-Mortimer, O. Taking possession: biogenesis of the Salmonella-containing vacuole. Traffic 4, 587–599 (2003).
Galan, J. E. Interaction of Salmonella with host cells through the centisome 63 type III secretion system. Curr. Opin. Microbiol. 2, 46–50 (1999).
Mukherjee, K., Parashuraman, S., Raje, M. & Mukhopadhyay, A. SopE acts as an Rab5-specific nucleotide exchange factor and recruits non-prenylated Rab5 on Salmonella-containing phagosomes to promote fusion with early endosomes. J. Biol. Chem. 276, 23607–23615 (2001).
Cirillo, D. M., Valdivia, R. H., Monack, D. M. & Falkow, S. Macrophage-dependent induction of the Salmonella pathogenicity island 2 type III secretion system and its role in intracellular survival. Mol. Microbiol. 30, 175–188 (1998).
Hensel, M. et al. Genes encoding putative effector proteins of the type III secretion system of Salmonella pathogenicity island 2 are required for bacterial virulence and proliferation in macrophages. Mol. Microbiol. 30, 163–174 (1998).
Uchiya, K. et al. A Salmonella virulence protein that inhibits cellular trafficking. EMBO J. 18, 3924–3933 (1999).
Lee, A. H., Zareei, M. P. & Daefler, S. Identification of a NIPSNAP homologue as host cell target for Salmonella virulence protein SpiC. Cell. Microbiol. 4, 739–750 (2002).
Garcia-del Portillo, F., Zwick, M. B., Leung, K. Y. & Finlay, B. B. Salmonella induces the formation of filamentous structures containing lysosomal membrane glycoproteins in epithelial cells. Proc. Natl Acad. Sci. USA 90, 10544–10548 (1993).
Brumell, J. H., Goosney, D. L. & Finlay, B. B. SifA, a type III secreted effector of Salmonella typhimurium, directs Salmonella-induced filament (Sif) formation along microtubules. Traffic 3, 407–415 (2002).
Stein, M. A., Leung, K. Y., Zwick, M., Garcia-del Portillo, F. & Finlay, B. B. Identification of a Salmonella virulence gene required for formation of filamentous structures containing lysosomal membrane glycoproteins within epithelial cells. Mol. Microbiol. 20, 151–164 (1996).
Beuzon, C. R. et al. Salmonella maintains the integrity of its intracellular vacuole through the action of SifA. EMBO J. 19, 3235–3249 (2000).
Brumell, J. H., Tang, P., Mills, S. D. & Finlay, B. B. Characterization of Salmonella-induced filaments (Sifs) reveals a delayed interaction between Salmonella-containing vacuoles and late endocytic compartments. Traffic 2, 643–653 (2001).
Salcedo, S. P., Noursadeghi, M., Cohen, J. & Holden, D. W. Intracellular replication of Salmonella typhimurium strains in specific subsets of splenic macrophages in vivo. Cell. Microbiol. 3, 587–597 (2001).
Arellano-Reynoso, B. et al. Cyclic β-1, 2-glucan is a Brucella virulence factor required for intracellular survival. Nature Immunol. 6, 618–625 (2005). This study shows that the cyclic β-1, 2-glucans synthesized by Brucella spp. act in lipid rafts found on host cell membranes to prevent phagosome–lysosome fusion and to allow bacterial replication.
Fugier, E. et al. The glyceraldehyde-3-phosphate dehydrogenase and the small GTPase Rab 2 are crucial for Brucella replication. PLoS Pathog. 5, e1000487 (2009).
Roy, C. R., Salcedo, S. P. & Gorvel, J. P. Pathogen-endoplasmic-reticulum interactions: in through the out door. Nature Rev. Immunol. 6, 136–147 (2006).
Ninio, S. & Roy, C. R. Effector proteins translocated by Legionella pneumophila: strength in numbers. Trends Microbiol. 15, 372–380 (2007).
Wyrick, P. B. Intracellular survival by Chlamydia. Cell. Microbiol. 2, 275–282 (2000).
Heuer, D. et al. Chlamydia causes fragmentation of the Golgi compartment to ensure reproduction. Nature 457, 731–735 (2009). This is a landmark paper showing that Chlamydia spp. infection in human epithelial cells induces Golgi fragmentation to generate Golgi ministacks surrounding the bacterial inclusion, facilitating lipid acquisition and intracellular pathogen growth. Ministack formation is triggered by the proteolytic cleavage of golgin 84.
Radtke, A. L. & O'Riordan, M. X. Intracellular innate resistance to bacterial pathogens. Cell. Microbiol. 8, 1720–1729 (2006). The authors provide excellent general review of the mechanisms of innate immune intracellular resistance encountered by bacterial pathogens and how some bacteria can evade destruction by the innate immune system.
Nauseef, W. M. Assembly of the phagocyte NADPH oxidase. Histochem. Cell. Biol. 122, 277–291 (2004).
MacMicking, J., Xie, Q. W. & Nathan, C. Nitric oxide and macrophage function. Annu. Rev. Immunol. 15, 323–350 (1997).
Bogdan, C. Nitric oxide and the immune response. Nature Immunol. 2, 907–916 (2001).
Lowenstein, C. J. & Padalko, E. iNOS (NOS2) at a glance. J. Cell Sci. 117, 2865–2867 (2004).
Chakravortty, D. & Hensel, M. Inducible nitric oxide synthase and control of intracellular bacterial pathogens. Microbes Infect. 5, 621–627 (2003).
Fang, F. C. Antimicrobial reactive oxygen and nitrogen species: concepts and controversies. Nature Rev. Microbiol. 2, 820–832 (2004).
De Groote, M. A. et al. Periplasmic superoxide dismutase protects Salmonella from products of phagocyte NADPH-oxidase and nitric oxide synthase. Proc. Natl Acad. Sci. USA 94, 13997–14001 (1997).
Farrant, J. L. et al. Bacterial copper- and zinc-cofactored superoxide dismutase contributes to the pathogenesis of systemic salmonellosis. Mol. Microbiol. 25, 785–796 (1997).
Fang, F. C. et al. Virulent Salmonella typhimurium has two periplasmic Cu, Zn-superoxide dismutases. Proc. Natl Acad. Sci. USA 96, 7502–7507 (1999).
Linehan, S. A. & Holden, D. W. The interplay between Salmonella typhimurium and its macrophage host—what can it teach us about innate immunity? Immunol. Lett. 85, 183–192 (2003). This is an excellent review on host–pathogen interactions during S . Typhimurium infection. The authors focus on different facets to the cell biology of macrophages and their innate immune functions.
Lundberg, B. E., Wolf, R. E. Jr, Dinauer, M. C., Xu, Y. & Fang, F. C. Glucose 6-phosphate dehydrogenase is required for Salmonella typhimurium virulence and resistance to reactive oxygen and nitrogen intermediates. Infect. Immun. 67, 436–438 (1999).
van der Straaten, T. et al. Novel Salmonella enterica serovar Typhimurium protein that is indispensable for virulence and intracellular replication. Infect. Immun. 69, 7413–7418 (2001).
van Diepen, A., van der Straaten, T., Holland, S. M., Janssen, R. & van Dissel, J. T. A superoxide-hypersusceptible Salmonella enterica serovar Typhimurium mutant is attenuated but regains virulence in p47(phox−/−) mice. Infect. Immun. 70, 2614–2621 (2002).
Bryk, R., Griffin, P. & Nathan, C. Peroxynitrite reductase activity of bacterial peroxiredoxins. Nature 407, 211–215 (2000).
Chen, L., Xie, Q. W. & Nathan, C. Alkyl hydroperoxide reductase subunit C (AhpC) protects bacterial and human cells against reactive nitrogen intermediates. Mol. Cell 1, 795–805 (1998).
Husain, M. et al. Nitric oxide evokes an adaptive response to oxidative stress by arresting respiration. J. Biol. Chem. 283, 7682–7689 (2008).
Jaeger, T. et al. Multiple thioredoxin-mediated routes to detoxify hydroperoxides in Mycobacterium tuberculosis. Arch. Biochem. Biophys. 423, 182–191 (2004).
Jaeger, T. Peroxiredoxin systems in mycobacteria. Subcell. Biochem. 44, 207–217 (2007).
Sherman, D. R. et al. Compensatory ahpC gene expression in isoniazid-resistant Mycobacterium tuberculosis. Science 272, 1641–1643 (1996).
Fischer, K. et al. Mycobacterial lysocardiolipin is exported from phagosomes upon cleavage of cardiolipin by a macrophage-derived lysosomal phospholipase A2. J. Immunol. 167, 2187–2192 (2001). This paper shows that lysocardiolipin is released from the mycobacterial cell wall in the phagosome of infected macrophages and transported out of this compartment into intracellular vesicles. Lysocardiolipin was generated through cleavage of mycobacterial cardiolipin by a calcium-independent phospholipase A2 present in the lysosomes of macrophages.
Bang, I. S. et al. Maintenance of nitric oxide and redox homeostasis by the Salmonella flavohemoglobin hmp. J. Biol. Chem. 281, 28039–28047 (2006).
Darwin, K. H. & Nathan, C. F. Role for nucleotide excision repair in virulence of Mycobacterium tuberculosis. Infect. Immun. 73, 4581–4587 (2005).
Cowley, S. C., Myltseva, S. V. & Nano, F. E. Phase variation in Francisella tularensis affecting intracellular growth, lipopolysaccharide antigenicity and nitric oxide production. Mol. Microbiol. 20, 867–874 (1996).
Eriksson, S. et al. Salmonella typhimurium mutants that downregulate phagocyte nitric oxide production. Cell. Microbiol. 2, 239–250 (2000).
Vazquez-Torres, A. et al. Salmonella pathogenicity island 2-dependent evasion of the phagocyte NADPH oxidase. Science 287, 1655–1658 (2000).
Shiloh, M. U. et al. Phenotype of mice and macrophages deficient in both phagocyte oxidase and inducible nitric oxide synthase. Immunity 10, 29–38 (1999).
Gallois, A., Klein, J. R., Allen, L. A., Jones, B. D. & Nauseef, W. M. Salmonella pathogenicity island 2-encoded type III secretion system mediates exclusion of NADPH oxidase assembly from the phagosomal membrane. J. Immunol. 166, 5741–5748 (2001).
Vazquez-Torres, A., Fantuzzi, G., Edwards, C. K. 3rd, Dinarello, C. A. & Fang, F. C. Defective localization of the NADPH phagocyte oxidase to Salmonella-containing phagosomes in tumour necrosis factor p55 receptor-deficient macrophages. Proc. Natl Acad. Sci. USA 98, 2561–2565 (2001).
Cherayil, B. J., McCormick, B. A. & Bosley, J. Salmonella enterica serovar typhimurium-dependent regulation of inducible nitric oxide synthase expression in macrophages by invasins SipB, SipC, and SipD and effector SopE2. Infect. Immun. 68, 5567–5574 (2000).
Bjur, E., Eriksson-Ygberg, S. & Rhen, M. The O-antigen affects replication of Salmonella enterica serovar Typhimurium in murine macrophage-like J774-A.1 cells through modulation of host cell nitric oxide production. Microbes Infect. 8, 1826–1838 (2006).
Chakravortty, D., Hansen-Wester, I. & Hensel, M. Salmonella pathogenicity island 2 mediates protection of intracellular Salmonella from reactive nitrogen intermediates. J. Exp. Med. 195, 1155–1166 (2002). In this paper the authors use immunofluorescence microscopy to show efficient colocalization of NOS2 with bacteria deficient in SPI2 but not wild-type S . Typhimurium, suggesting that the SPI2 system interferes with the localization of NOS2 in S . Typhimurium and that avoidance of colocalization with RNI is important for a pathogen to adapt to an intracellular lifestyle.
Miller, B. H. et al. Mycobacteria inhibit nitric oxide synthase recruitment to phagosomes during macrophage infection. Infect. Immun. 72, 2872–2878 (2004).
Davis, A. S. et al. Mechanism of inducible nitric oxide synthase exclusion from mycobacterial phagosomes. PLoS Pathog. 3, e186 (2007).
Forbes, J. R. & Gros, P. Iron, manganese, and cobalt transport by Nramp1 (Slc11a1) and Nramp2 (Slc11a2) expressed at the plasma membrane. Blood 102, 1884–1892 (2003).
Chlosta, S. et al. The iron efflux protein ferroportin regulates the intracellular growth of Salmonella enterica. Infect. Immun. 74, 3065–3067 (2006).
De Voss, J. J. et al. The salicylate-derived mycobactin siderophores of Mycobacterium tuberculosis are essential for growth in macrophages. Proc. Natl Acad. Sci. USA 97, 1252–1257 (2000).
Parent, M. A. et al. Brucella abortus siderophore 2, 3-dihydroxybenzoic acid (DHBA) facilitates intracellular survival of the bacteria. Microb. Pathog. 32, 239–248 (2002).
Fischbach, M. A., Lin, H., Liu, D. R. & Walsh, C. T. How pathogenic bacteria evade mammalian sabotage in the battle for iron. Nature Chem. Biol. 2, 132–138 (2006).
Chatterjee, S. S. et al. Intracellular gene expression profile of Listeria monocytogenes. Infect. Immun. 74, 1323–1338 (2006).
Jansen, A. & Yu, J. Differential gene expression of pathogens inside infected hosts. Curr. Opin. Microbiol. 9, 138–142 (2006).
Levine, B. & Deretic, V. Unveiling the roles of autophagy in innate and adaptive immunity. Nature Rev. Immunol. 7, 767–777 (2007).
Schmid, D. & Munz, C. Innate and adaptive immunity through autophagy. Immunity 27, 11–21 (2007).
Orvedahl, A. & Levine, B. Eating the enemy within: autophagy in infectious diseases. Cell Death Differ. 16, 57–69 (2009).
Dorn, B. R., Dunn, W. A. Jr & Progulske-Fox, A. Porphyromonas gingivalis traffics to autophagosomes in human coronary artery endothelial cells. Infect. Immun. 69, 5698–5708 (2001).
Gutierrez, M. G. et al. Autophagy induction favours the generation and maturation of the Coxiella-replicative vacuoles. Cell. Microbiol. 7, 981–993 (2005).
Birmingham, C. L. et al. Listeriolysin O allows Listeria monocytogenes replication in macrophage vacuoles. Nature 451, 350–354 (2008). The authors reveal a role for listeriolysin O in promoting L. monocytogenes replication in vacuoles in infected macrophages.
Swanson, M. S. & Molofsky, A. B. Autophagy and inflammatory cell death, partners of innate immunity. Autophagy 1, 174–176 (2005).
Suzuki, T. et al. Differential regulation of caspase-1 activation, pyroptosis, and autophagy via Ipaf and ASC in Shigella-infected macrophages. PLoS Pathog. 3, e111 (2007).
Schroeder, G. N. & Hilbi, H. Cholesterol is required to trigger caspase-1 activation and macrophage apoptosis after phagosomal escape of Shigella. Cell. Microbiol. 9, 265–278 (2007).
Suzuki, T. & Nunez, G. A role for Nod-like receptors in autophagy induced by Shigella infection. Autophagy 4, 73–75 (2008).
Ogawa, M. et al. Escape of intracellular Shigella from autophagy. Science 307, 727–731 (2005). This is a landmark paper showing that S. flexneri can escape autophagy by secreting IcsB. S. flexneri VirG, which is required for intracellular actin-based motility, induces autophagy by binding to ATG5. IcsB does not directly inhibit autophagy and instead its role is to camouflage its own bacterial target molecule (VirG) from the autophagic host defence system.
Akira, S., Uematsu, S. & Takeuchi, O. Pathogen recognition and innate immunity. Cell 124, 783–801 (2006).
Meylan, E., Tschopp, J. & Karin, M. Intracellular pattern recognition receptors in the host response. Nature 442, 39–44 (2006).
Ting, J. P. et al. The NLR gene family: a standard nomenclature. Immunity 28, 285–287 (2008).
Martinon, F., Burns, K. & Tschopp, J. The inflammasome: a molecular platform triggering activation of inflammatory caspases and processing of proIL-β. Mol. Cell 10, 417–426 (2002).
Kanneganti, T. D., Lamkanfi, M. & Nunez, G. Intracellular NOD-like receptors in host defense and disease. Immunity 27, 549–559 (2007).
Mariathasan, S. & Monack, D. M. Inflammasome adaptors and sensors: intracellular regulators of infection and inflammation. Nature Rev. Immunol. 7, 31–40 (2007).
Martinon, F. & Tschopp, J. Inflammatory caspases and inflammasomes: master switches of inflammation. Cell Death Differ. 14, 10–22 (2007).
Fernandes-Alnemri, T. et al. The pyroptosome: a supramolecular assembly of ASC dimers mediating inflammatory cell death via caspase-1 activation. Cell Death Differ. 14, 1590–1604 (2007).
Yu, H. B. & Finlay, B. B. The caspase-1 inflammasome: a pilot of innate immune responses. Cell Host Microbe 4, 198–208 (2008).
Martinon, F. & Tschopp, J. Inflammatory caspases: linking an intracellular innate immune system to autoinflammatory diseases. Cell 117, 561–574 (2004).
Keller, M., Ruegg, A., Werner, S. & Beer, H. D. Active caspase-1 is a regulator of unconventional protein secretion. Cell 132, 818–831 (2008).
Shao, W., Yeretssian, G., Doiron, K., Hussain, S. N. & Saleh, M. The caspase-1 digestome identifies the glycolysis pathway as a target during infection and septic shock. J. Biol. Chem. 282, 36321–36329 (2007).
Kanneganti, T. D. et al. Bacterial RNA and small antiviral compounds activate caspase-1 through cryopyrin/Nalp3. Nature 440, 233–236 (2006).
Mariathasan, S. et al. Cryopyrin activates the inflammasome in response to toxins and ATP. Nature 440, 228–232 (2006). This paper shows that cryopyrin-deficient macrophages cannot activate caspase 1 in response to TLR agonists and ATP. Cryopyrin is essential for inflammasome activation in response to signalling pathways that are triggered specifically by ATP, nigericin, maitotoxin, Staphylococcus aureus or L. monocytogenes.
Faustin, B. et al. Reconstituted NALP1 inflammasome reveals two-step mechanism of caspase-1 activation. Mol. Cell 25, 713–724 (2007).
Martinon, F., Agostini, L., Meylan, E. & Tschopp, J. Identification of bacterial muramyl dipeptide as activator of the NALP3/cryopyrin inflammasome. Curr. Biol. 14, 1929–1934 (2004).
Pan, Q. et al. MDP-induced interleukin-1β processing requires Nod2 and CIAS1/NALP3. J. Leukoc. Biol. 82, 177–183 (2007).
Hsu, L. C. et al. A NOD2-NALP1 complex mediates caspase-1-dependent IL-1β secretion in response to Bacillus anthracis infection and muramyl dipeptide. Proc. Natl Acad. Sci. USA 105, 7803–7808 (2008).
Franchi, L. et al. Cytosolic flagellin requires Ipaf for activation of caspase-1 and interleukin 1β in salmonella-infected macrophages. Nature Immunol. 7, 576–582 (2006).
Miao, E. A. et al. Cytoplasmic flagellin activates caspase-1 and secretion of interleukin 1β via Ipaf. Nature Immunol. 7, 569–575 (2006).
Kanneganti, T. D. et al. Critical role for Cryopyrin/Nalp3 in activation of caspase-1 in response to viral infection and double-stranded RNA. J. Biol. Chem. 281, 36560–36568 (2006).
Kanneganti, T. D. et al. Pannexin-1-mediated recognition of bacterial molecules activates the cryopyrin inflammasome independent of Toll-like receptor signalling. Immunity 26, 433–443 (2007).
Piccini, A. et al. ATP is released by monocytes stimulated with pathogen-sensing receptor ligands and induces IL-1β and IL-18 secretion in an autocrine way. Proc. Natl Acad. Sci. USA 105, 8067–8072 (2008).
Weiss, D. S. et al. In vivo negative selection screen identifies genes required for Francisella virulence. Proc. Natl Acad. Sci. USA 104, 6037–6042 (2007).
Master, S. S. et al. Mycobacterium tuberculosis prevents inflammasome activation. Cell Host Microbe 3, 224–232 (2008).
Ruckdeschel, K. et al. Yersinia enterocolitica impairs activation of transcription factor NF-κB: involvement in the induction of programmed cell death and in the suppression of the macrophage tumour necrosis factor α production. J. Exp. Med. 187, 1069–1079 (1998).
Schesser, K. et al. The yopJ locus is required for Yersinia-mediated inhibition of NF-κB activation and cytokine expression: YopJ contains a eukaryotic SH2-like domain that is essential for its repressive activity. Mol. Microbiol. 28, 1067–1079 (1998).
Schotte, P. et al. Targeting Rac1 by the Yersinia effector protein YopE inhibits caspase-1-mediated maturation and release of interleukin-1β. J. Biol. Chem. 279, 25134–25142 (2004).
Dukuzumuremyi, J. M. et al. The Yersinia protein kinase A is a host factor inducible RhoA/Rac-binding virulence factor. J. Biol. Chem. 275, 35281–35290 (2000).
Bergsbaken, T. & Cookson, B. T. Macrophage activation redirects yersinia-infected host cell death from apoptosis to caspase-1-dependent pyroptosis. PLoS Pathog. 3, e161 (2007).