Inflammatory corpuscles are a complex group of protein, which participate in stimulating innate immune system. Cryopyrin is a complex component of cytoplasmic inflammatory corpuscles, which can lead to the death of necrotic cells through an inflammatory reaction pathway independent of the formation of inflammatory corpuscles. Recently published in Cellhost &; Microbiology) pointed out that protein cryopyrin (also known as NLRP3, NARP 3 or CIAS 1) is an important host medium for some pathogenic bacteria to induce the death of necrotic cells. Cryopyrin is a member of the nucleotide binding domain (a family rich in leucine repeats) protein family. Cryoprotein is also considered as a receptor or caterpillar protein similar to nucleotide-binding oligomerization domain (NOD). It is a part of cytoplasmic protein complex. Cytosol complex, also known as inflammatory body, not only contains apoptosis-related spot-like protein (ASC), but also undertakes the task of processing caspase- 1 into activated form. In turn, this will lead to the production of mature interleukin-1β. However, do low-temperature proteins in pathogenic bacteria have additional biological functions? There are no macrophages in cryopyran, which is more resistant to some gram-positive bacteria, suggesting that cryopyran can participate in the initial reaction of necrosis, but scientists have not been able to solve the mystery. The mutation of CIAS 1 gene (coding for cryopyrin) is related to the periodic fever syndrome of autoinflammation (characterized by the overproduction of IL- 1β). In this paper, the author confirmed for the first time that the existence of CIAS 1 mutation related to disease led to the necrotic cell death of monocyte strain, and then the mechanism of inducing cell death was discussed. The cells expressing mutant cryopyrin release more and richer IL- 1β than the cells expressing wild-type cryopyrin. However, the occurrence of cell death is proved to be independent of caspase- 1 activity and IL- 1β-mediated signal transmission (so it is independent of the formation of inflammatory bodies). In addition, cell death induced by low-temperature protein mutation was proved to be dependent on ASC, and high-mobility group protein 1 (high-mobility group protein box 1, hmgb1; As a post-inflammatory factor, it is released when cells are necrotic. It was also found that in the face of the challenge of lipopolysaccharide, the monocytes of patients with CIAS 1 mutation related to the disease died excessively through the procedures dependent on ASC and B (cathepsin B), which eventually led to the production of HMGB 1. Because people think that the disease-related cry pyran mutation is a function acquisition (GoF) mutation, the wild-type cry pyran should have similar characteristics to the mutant cry pyran, but the expression level is low or expressed after stimulation. In view of this, the authors speculate whether wild-type cryopyrin plays a role in cell necrosis related to bacterial pathogenicity, especially intracellular bacteria Shigella flexneri (which is thought to induce necrotic cell death). Scholars have found that the induction of macrophage necrosis in mice by Shigella flexneri requires the participation of cryopyrin and ASC, but does not require caspase- 1. In addition, the necrosis process is not dependent on IL- 1β, but related to the release of HMGB 1. Therefore, the cell death induced by Shigella flexneri and the disease-related cell death induced by cryoprotein have the same host cell signal transduction pathway. Therefore, infection with S. flexneri can induce caspase- 1 independent and crypyran-dependent necrotic cells to die, which the author calls focal necrosis, which is the same as the induction of disease-related crypyran. This indicates that patients with functionally activated CIAS 1 mutation can inherit the inflammatory response usually stimulated by pathogenic bacteria. Original search: http://www. Signaling-gateway.org/update/updates/200711/nri2203.html Leucine-rich family: Leucine-rich family; ASC: apoptosis-related spot-like protein (CARD) containing caspase-recruiting domain; Also known as PYCARD, TMS 1 or CARD5；; Interleukin-1β: Interleukin-1β, IL- 1β, a powerful post-inflammatory cytokine (proinflammatory cytokine, which can respond to post-inflammatory stimuli such as bacteria and viruses; Interleukin: Interleukin for short refers to a cytokine that interacts between white blood cells or immune cells, and belongs to the same cytokine as blood cell growth factor. They coordinate and interact with each other, and * * * complete the functions of hematopoiesis and immune regulation. Interleukin plays an important role in transmitting information, activating and regulating immune cells, mediating the activation, proliferation and differentiation of T and B cells and inflammatory reaction.