Host-derived, pore-forming toxin-like protein and trefoil factor complex protects the host against microbial infection
文献类型：期刊论文
| 作者 | Xiang Y1; Yan C1,2; Guo XL1,2; Zhou KF1,2; Li SA1; Gao Q1; Wang X1,2; Zhao F1,2; Liu J1,2; Lee WH1 |
| 刊名 | PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA
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| 出版日期 | 2014 |
| 卷号 | 111期号:18页码:6702-6707 |
| 关键词 | innate immunity infectious disease interleukin-1beta |
| 通讯作者 | zhangy@mail.kiz.ac.cn |
| 合作状况 | 其它 |
| 英文摘要 | Aerolysins are virulence factors belonging to the bacterial beta-pore-forming toxin superfamily. Surprisingly, numerous aerolysin-like proteins exist in vertebrates, but their biological functions are unknown. beta gamma-CAT, a complex of an aerolysin-like protein subunit (two beta gamma-crystallin domains followed by an aerolysin pore-forming domain) and two trefoil factor subunits, has been identified in frogs (Bombina maxima) skin secretions. Here, we report the rich expression of this protein, in the frog blood and immune-related tissues, and the induction of its presence in peritoneal lavage by bacterial challenge. This phenomena raises the possibility of its involvement in antimicrobial infection. When beta gamma-CAT was administrated in a peritoneal infection model, it greatly accelerated bacterial clearance and increased the survival rate of both frogs and mice. Meanwhile, accelerated Interleukin-1 beta release and enhanced local leukocyte recruitments were determined, which may partially explain the robust and effective antimicrobial responses observed. The release of interleukin-1 beta was potently triggered by beta gamma-CAT from the frog peritoneal cells and murine macrophages in vitro. beta gamma-CAT was rapidly endocytosed and translocated to lysosomes, where it formed high molecular mass SDS-stable oligomers (>170 kDa). Lysosomal destabilization and cathepsin B release were detected, which may explain the activation of caspase-1 inflammasome and subsequent interleukin-1 beta maturation and release. To our knowledge, these results provide the first functional evidence of the ability of a host-derived aerolysin-like protein to counter microbial infection by eliciting rapid and effective host innate immune responses. The findings will also largely help to elucidate the possible involvement and action mechanisms of aerolysin-like proteins and/or trefoil factors widely existing in vertebrates in the host defense against pathogens. |
| 资助信息 | This work was sup- ported by Chinese 973 Program Grant 2010CB529800, Natural Science Foundation of China (NSFC)-Yunnan joint Grant U1132601, NSFC Grants 31270835 and 31301884, and Chinese Academy of Sciences Grant KJZD- EW-L03. |
| 语种 | 英语 |
| WOS记录号 | WOS:000335477300051 |
| 公开日期 | 2014-06-03 |
| 源URL | [http://159.226.149.42:8088/handle/152453/7849]  |
| 专题 | 昆明动物研究所_动物活性蛋白多肽组学 昆明动物研究所_动物模型与人类重大疾病机理重点实验室 |
| 作者单位 | 1.Key Laboratory of Animal Models and Human Disease Mechanisms, The Chinese Academy of Sciences and Yunnan Province, Kunming Institute of Zoology, Chinese Academy of Sciences, Kunming, Yunnan 650223, China 2.Kunming College of Life Science, University of Chinese Academy of Sciences, Beijing 100049, China |
| 推荐引用方式 GB/T 7714 | Xiang Y,Yan C,Guo XL,et al. Host-derived, pore-forming toxin-like protein and trefoil factor complex protects the host against microbial infection[J]. PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA,2014,111(18):6702-6707. |
| APA | Xiang Y.,Yan C.,Guo XL.,Zhou KF.,Li SA.,...&Zhang Y[*].(2014).Host-derived, pore-forming toxin-like protein and trefoil factor complex protects the host against microbial infection.PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA,111(18),6702-6707. |
| MLA | Xiang Y,et al."Host-derived, pore-forming toxin-like protein and trefoil factor complex protects the host against microbial infection".PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA 111.18(2014):6702-6707. |
入库方式： OAI收割
来源：昆明动物研究所
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