Search

How host cells induce the release of DNA from cytosolic bacteria is unclear. Broz and colleagues show that the guanylate-binding proteins GBP2 and GBP5 trigger bacteriolysis in infected host cells and thereby allow recognition by the sensor AIM2.

During some types of cell death, cells rupture to release molecules that cause inflammation. This must happen at the right time and place to restore health. How is the protein NINJ1 regulated so that cells break open only when they die?

Neutrophils can release S100A8/S100A9 as an alarmin via gasdermin D pores. Here, the authors untangle the regulatory mechanisms driving this pathway and show that active repair processes make these pores transient, which can prevent the usual lytic cell death.

Rupture of the plasma membrane in different forms of cell death was long thought to be a passive process. The finding that it is an active one, mediated by a specific membrane protein, reveals an unexpected feature shared by dying cells.

Inflammatory caspase proteins help to control pathogen replication by triggering pyroptotic cell death. It now emerges that cleavage of the caspase substrate gasdermin D is sufficient to induce pyroptosis. See Articles p.660 & p.666

By systematically screening viral and bacterial pathogens during co-infection in macrophages, the authors identify and characterize altered host cell entry and suppressed cell death induction as two critical mechanisms that impact infection outcome.

Structural, biochemical and mutagenesis studies indicate that, in dying cells, the membrane protein NINJ1 assembles into filaments, disrupting the cell membrane.

Interferon-inducible GTPases are required for the release of vacuolar Gram-negative bacteria into the cytoplasm and subsequent inflammasome-mediated caspase-11 activation.

Experimental mudflows under Martian surface conditions propagate similarly to terrestrial pahoehoe lava flows, suggesting mud (rather than igneous) volcanism can explain some flow morphologies on Mars.

Detection of LPS derived from Gram-negative bacteria by innate immune receptors is a critical step in the host response. Here Santos and colleagues show human GBP1 binds to LPS resulting in non-canonical inflammasome activation.

Mud flow properties and spatial distribution are greatly influenced by salinity and composition in low pressure extraterrestrial environments such as Mars, according to a comparison of laboratory experiments, thermodynamic calculations, and rheometry measurements

Inflammasomes regulate IL-1β family maturation and pyroptosis. Here the authors show that ASC oligomerization and the formation of ASC specks are needed for IL-1β processing, but are not required for pyroptosis, indicating distinct inflammasome regulatory pathways.

The pathogenicity ofFrancisellaspecies largely depends on their escape from phagosomes in macrophages, mediated by a type VI secretion system (T6SS). Here, the authors show dynamics of T6SS assembly and disassembly and identify the genes essential for phagosome escape and pathogenicity in mice.

Inflammasomes function as immune-signaling platforms that assemble following pathogen detection. Direct binding of a viral protein to NLRP1 and the disruption of a previously unknown autoinhibitory NRLP1 complex drive the activation of the NLRP1 inflammasome independently of the proteasome.

This Review provides a comprehensive overview of very recent progress in our understanding of the role of pattern recognition receptors, including Toll-like receptors, cytosolic nucleic acid receptors and NOD-like receptors that assemble inflammasomes, in the detection of and in the defence against intracellular pathogens.

Activation of the non-canonical, pro-inflammatory caspase-11 by Salmonella typhimurium is shown to contribute to bacterial spread and pathogenesis by the induction of macrophage cell death.

AWP28, an activity-based probe for caspase-1, reveals that caspase-1 is required to bypass apoptosis for pyroptotic cell death during bacterial infection of macrophages.

Dysregulated inflammasome activation is linked to numerous inflammatory disorders and is therefore tightly regulated. In this Review, the authors discuss the latest insights into the activation and assembly mechanisms of inflammasomes, the structure of distinct inflammasome complexes and the mechanisms that regulate inflammasome signalling.

In this Review, Luedde and colleagues describe the complex role of regulated necrosis pathways, including necroptosis, pyroptosis and ferroptosis, in liver disease and cancer development. Potential therapeutic approaches modulating regulated cell death pathways in liver disease are explored.

Gasdermins are a family of proteins that form membrane pores and elicit pyroptosis. This Review discusses recent work highlighting their regulation and emerging biological roles, including in non-lethal pore formation and host defence.

In vitro models mimicking in-patient conditions have the potential to yield exciting opportunities for antibiotic research and revitalize future antibiotic discovery and development.

Gravitational flow deposits on Earth may not be meaningful analogues for those on Mars or other planetary bodies according to laboratory experiments conducted at Mars-like temperatures and pressures where freezing and evaporative cooling play key roles.

The gasdermin family of proteins has the capacity to form pores in the membrane, causing a pro-inflammatory lytic type of cell death called pyroptosis, This Review provides a comprehensive overview of the gasdermin family, the mechanisms that control their activation and their role in inflammatory disorders and cancer.

The non-canonical inflammasome triggers host cell death and inflammation upon recognition of cytosolic LPS. A recent report in Cell now shows that Outer Membrane Vesicles (OMVs) of extracellular Gram-negative bacteria can deliver LPS into the host cell cytosol.

Inflammasomes control host cell death and inflammation in response to sterile or infectious stimuli. Two recent reports published in Science reveal the structural basis for the assembly of NAIP-NLRC4 inflammasomes.