Pathogen-induced apoptosis of macrophages: a common end for different pathogenic strategies. Microreview

Navarre, William Wiley; Zychlinsky, Arturo

doi:10.1046/j.1462-5822.2000.00056.x

Cited by 187 publications

(165 citation statements)

References 67 publications

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“…Indeed, the morphological features of infected wild-type or the caspase-1-deficient macrophages are indistinguishable with extensive membrane blebbing and membrane integrity. The same was true of BMDCs and peritoneal macrophages from wild-type and caspase-1-deficient mice, 2 and necrotic cell death was also observed in J774A.1 macrophages (Fig. 3), mouse RAW264.7 macrophages, or human monocyte-derived macrophages infected with Shigella.…”

Section: Discussionsupporting

confidence: 56%

“…Once they reach the underlying M cells, Shigella invade the resident macrophages, and the infecting bacteria escape from the phagosome into the cytosol. Shigella multiply in the cytoplasm and induce cell death through activation of caspase-1 mediated by IpaB protein secreted via the type III secretion system (TTSS), 1 in turn leading to the maturation and release of IL-1␤ (2,3). Shigella released from the killed macrophages enter the surrounding enterocytes through their basolateral surface by inducing membrane ruffling and macro-pinocytosis (4).…”

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confidence: 99%

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A Novel Caspase-1/Toll-like Receptor 4-independent Pathway of Cell Death Induced by Cytosolic Shigella in Infected Macrophages

Suzuki

Nakanishi

Tsutsui

et al. 2005

Journal of Biological Chemistry

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Shigella-induced macrophage cell death is an important step in the induction of acute inflammatory responses that ultimately lead to bacillary dysentery. Cell death was previously reported to be dependent upon the activation of caspase-1 via interaction with IpaB secreted by intracellular Shigella, but in this study, we show that Shigella infection of macrophages can also induce cell death independent of caspase-1 or IpaB activity. Time-lapse imaging and electron microscopic analyses indicated that caspase-1-dependent and -independent cell death is morphologically indistinguishable and that both resemble necrosis. Analyses of Shigella mutants or Escherichia coli using co-infection with Listeria suggested that a component common to Gram-negative bacteria is involved in inducing caspase-1-independent cell death. Further studies revealed that translocation of bacterial lipid A into the cytosol of macrophages potentially mediates cell death. Notably, cell death induced by cytosolic bacteria was TLR4-independent. These results identify a novel cell death pathway induced by intracellular Gram-negative bacteria that may play a role in microbial-host interactions and inflammatory responses.

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Section: Discussionsupporting

confidence: 56%

mentioning

confidence: 99%

A Novel Caspase-1/Toll-like Receptor 4-independent Pathway of Cell Death Induced by Cytosolic Shigella in Infected Macrophages

Suzuki

Nakanishi

Tsutsui

et al. 2005

Journal of Biological Chemistry

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“…However, whether the level of N-WASP expression in haematopoietic cells would be the same or not as that in other epithelial or fibroblastic cells has never been seriously investigated yet. As macrophages and polymorphonuclear leucocytes (PMNs) have been indicated to play significant roles in mucosal infection of Shigella including the inflammatory responses (Navarre and Zychlinsky, 2000;Philpott et al, 2000;Kuwae et al, 2001), we investigated macrophages and PMNs for the expression of N-WASP and WASP. Human monocyte-derived macrophages (HMDMs), PMNs and platelets were examined for the expression of N-WASP or WASP by Western blotting using N-WASPspecific or WASP-specific antibodies.…”

Section: Human Macrophages Do Not Support Actin-based Motility Of Intmentioning

confidence: 99%

Neural Wiskott-Aldrich syndrome protein (N-WASP) is the specific ligand for Shigella VirG among the WASP family and determines the host cell type allowing actin-based spreading

et al. 2002

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SummaryShigella, the causative agent of bacillary dysentery, is capable of directing its movement within host cells by forming an actin comet tail. The VirG (IcsA) protein expressed at one pole of the bacterium recruits neural Wiskott-Aldrich syndrome protein (N-WASP), a member of the WASP family, which in turn stimulates actin-related protein (Arp) 2/3 complex-mediated actin polymerization. As all the WASP family proteins induce actin polymerization by recruiting Arp2/3 complex, we investigated their involvement in Shigella motility. Here, we show that VirG binds to N-WASP but not to the other WASP family proteins. Using a series of chimeras obtained by swapping N-WASP and WASP domains, we demonstrated that the specificity of VirG to interact with N-WASP lies in the N-terminal region containing the pleckstrin homology (PH) domain and calmodulin-binding IQ motif of N-WASP. A conformational change in N-WASP was important for the VirG-N-WASP interaction, as elimination of the C-terminal acidic region, which is responsible for the intramolecular interaction with the central basic region of N-WASP, affected the specific binding to VirG. We observed that, in haematopoietic cells such as macrophages, polymorphonuclear leucocytes (PMNs) and platelets, WASP was predominantly expressed, whereas the expression of N-WASP was greatly suppressed. Indeed, unlike Listeria, Shigella was unable to move in macrophages at all, (V) domain, a domain (C) with homology to the actindepolymerizing protein cofilin and, finally, a C-terminal acidic (A) segment (Miki et al., 1996). The C-terminal VCA domain interacts with the actin-related protein (Arp) 2/3 complex after the stimulation of actin polymerization by the complex (Rohatgi et al., 1999). N-WASP exists in two conformations: an inactive form in which the VCA domain is masked, and an active form in which it is exposed to promote actin polymerization by interaction with the Arp2/3 complex. The activation of N-WASP requires Cdc42 or PtdIns(4,5)P2 bound to N-WASP (Miki et al., 1998b;Rohatgi et al., 1999;2000;Prehoda et al., 2000). It has been reported that N-WASP is required for generating the actin tail from motile S. flexneri (Suzuki et al., 1998;Egile et al., 1999). Arp2/3 complex is also required for actin-based motility of Shigella, in which N-WASP stimulates the actin nucleation activity of the Arp2/3 complex in vitro (Egile et al., 1999).In mammalian cells, five WASP family members, N-WASP, WASP and WAVE1-3, have been identified and characterized to date (Suetsugu et al., 1999); however, none of them except N-WASP has been elucidated for involvement in the actin-based motility of Shigella in infected cells. It has been shown that human platelet extracts supported Shigella actin-based motility as added N-WASP in vitro (Egile et al., 1999). Recent reports using N-WASP-deficient mouse embryonic fibroblasts (Lommel et al., 2001;Snapper et al., 2001) confirmed our previous work indicating that N-WASP is required for Shigella motility in mammalian cells (Suzuki et al., 1998). However...

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“…The pathogenic outcomes of these four pathways are distinct, whereby cell death by an apoptotic or autophagy pathway occurs without significant tissue disruption and inflammation, while host cell death by oncosis and pyroptosis leads to secretion of inflammatory cytokines, such as interleukin (IL)-1b and IL-8, and subsequent recruitment of activated neutrophils to the site of infection (Navarre & Zychlinsky, 2000). Interestingly, the same species of bacteria may use more than one mechanism to induce the death of epithelial cells and macrophages.…”

Section: Introductionmentioning

confidence: 99%

“…For example, Listeria monocytogenes and Legionella pneumophila reside intracellularly in the macrophage, thereby avoiding an antimicrobial environment and promoting their dissemination throughout the host without being exposed to antibodies (Duclos & Desjardins, 2000;Pizarro-Cerda & Cossart, 2006;Swanson & Fernandez-Moreira, 2002). In contrast, Salmonella and Shigella can survive within macrophages as well as kill macrophages, depending on the physiological state of the macrophage (Navarre & Zychlinsky, 2000). Finally, Yersinia is also known to induce macrophage death (Hersh et al, 1999;Mills et al, 1997;Palmer et al, 1999).…”

Section: Introductionmentioning

confidence: 99%

Type III secretion system 1 of Vibrio parahaemolyticus induces oncosis in both epithelial and monocytic cell lines

2009

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The Vibrio parahaemolyticus type III secretion system 1 (T3SS1) induces cytotoxicity in mammalian epithelial cells. We characterized the cell death phenotype in both epithelial (HeLa) and monocytic (U937) cell lines following infection with V. parahaemolyticus. Using a combination of the wild-type strain and gene knockouts, we confirmed that V. parahaemolyticus strain NY-4 was able to induce cell death in both cell lines via a T3SS1-dependent mechanism. Bacterial contact, but not internalization, was required for T3SS1-induced cytotoxicity. The mechanism of cell death involves formation of a pore structure on the surface of infected HeLa and U937 cells, as demonstrated by cellular swelling, uptake of cell membrane-impermeable dye and protection of cytotoxicity by osmoprotectant (PEG3350). Western blot analysis showed that poly ADP ribose polymerase (PARP) was not cleaved and remained in its full-length active form. This result was evident for seven different V. parahaemolyticus strains. V. parahaemolyticus-induced cytotoxicity was not inhibited by addition of the pan-caspase inhibitor carbobenzoxy-valyl-alanyl-aspartyl-[O-methyl]-fluoromethylketone (Z-VAD-FMK) or the caspase-1 inhibitor N-acetyl-tyrosyl-valylalanyl-aspartyl-aldehyde (Ac-YVAD-CHO); thus, caspases were not involved in T3SS1-induced cytotoxicity. DNA fragmentation was not evident following infection and autophagic vacuoles were not observed after monodansylcadaverine staining. We conclude that T3SS1 of V. parahaemolyticus strain NY-4 induces a host cell death primarily via oncosis rather than apoptosis, pyroptosis or autophagy. INTRODUCTIONVibrio parahaemolyticus is a Gram-negative food-borne pathogen that is commonly associated with consumption of raw or undercooked seafood (Joseph et al., 1982). Symptoms of infection include diarrhoea, nausea, vomiting, headache, fever and chills. In addition to typical gastrointestinal infections, approximately 5 % of V. parahaemolyticus infections advance to septicaemia (Hlady & Klontz, 1996) and these infections may be fatal, especially in immunocompromised patients or those with a preexisting medical condition such as liver disease or diabetes (Yeung & Boor, 2004).Thermostable direct haemolysin (TDH) is considered the primary virulence factor in V. parahaemolyticus. In addition to its ability to form pores in red blood cells, TDH causes increased short circuit current, increased Cl 2 secretion in human colonic epithelial cells, and enhanced Ca 2+ entry from the extracellular medium (Takahashi et al., 2001). An early study of a tdh deletion mutant demonstrated significantly reduced ability to cause fluid accumulation in ileal loops of a rabbit model (Nishibuchi et al., 1992). In contrast, Park et al. (2004) showed that a tdh deletion mutant has the ability to cause fluid accumulation in the ligated intestine of rabbits. Furthermore, both TDH-positive and -negative strains of V. parahaemolyticus can disrupt the epithelial tight junction, a precursor to dissemination of bacteria into the circulation (Lynch et a...

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Pathogen-induced apoptosis of macrophages: a common end for different pathogenic strategies. Microreview

Cited by 187 publications

References 67 publications

A Novel Caspase-1/Toll-like Receptor 4-independent Pathway of Cell Death Induced by Cytosolic Shigella in Infected Macrophages

A Novel Caspase-1/Toll-like Receptor 4-independent Pathway of Cell Death Induced by Cytosolic Shigella in Infected Macrophages

Neural Wiskott-Aldrich syndrome protein (N-WASP) is the specific ligand for Shigella VirG among the WASP family and determines the host cell type allowing actin-based spreading

Type III secretion system 1 of Vibrio parahaemolyticus induces oncosis in both epithelial and monocytic cell lines

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