Edwardsiella piscicida employs C3 derivative to mediate internalization and infection via the teleost-specific receptor
文献类型：期刊论文
| 作者 | Li, Mo-Fei1,2; Jin, Xiao-Yan2; Liu, Heng2; Feng, Zhe2; Wu, Meng3,4; Zhang, Hong-Qiang2; Du, Yu-Ting2; Sun, Yuan-Yuan3; Li, Xue-Peng5; Sun, Jin-Sheng2 |
| 刊名 | VIRULENCE
 |
| 出版日期 | 2025-12-31 |
| 卷号 | 16期号:1页码:21 |
| 关键词 | |
| ISSN号 | 2150-5594 |
| DOI | 10.1080/21505594.2025.2526783 |
| 通讯作者 | Li, Mo-Fei(murphy210@163.com) ; Sun, Jin-Sheng(skysjs@tjnu.edu.cn) |
| 英文摘要 | Edwardsiella piscicida is a prominent fish pathogen, and spreads the infection to humans and mammals. It can resist serum killing and invade the host phagocytic cells. However, the precise mechanisms underlying E. piscicida infection remain unclear. In this study, we found that E. piscicida could bind to complement factor H and recruit complement factor I from Paralichthys olivaceus (Po) serum, leading to the degradation of complement recognition molecule PoC3b to PoC3dg on the bacterial surface. E. piscicida also bound to peripheral blood leukocytes, depending on the teleost-specific interaction between PoC3dg and the integrin beta VWA (INB) domain of PoCD18, whereby facilitating bacterial internalization and infection. When PoCD18 was knocked down or blocked, bacterial infection and tissue lesions were significantly decreased. Mechanistically, the intracellular domain of PoCD18 subsequently interacted with PoCytohesin and triggered the phosphorylation of the phosphatidylinositol 3-kinase (PI3K)/serine-threonine protein kinase (Akt) signalling pathway. Furthermore, inhibition of the PI3K/Akt pathway impaired the internalization and pathogenicity of E. piscicida. Overall, we demonstrated for the first time that E. piscicida utilized the C3dg-CD18 axis to facilitate internalization, thereby targeting immune evasion and promoting systemic infections. These results provide new insights into the pathogen-host interaction mechanism and a potential target to control edwardsiellosis. |
| WOS关键词 | COMPLEMENT COMPONENT C3 ; CYNOGLOSSUS-SEMILAEVIS ; I-DOMAIN ; ACTIVATION ; TARDA ; PHAGOCYTOSIS ; BINDING ; RECOGNITION ; CYTOHESIN-1 ; INHIBITOR |
| 资助项目 | National Natural Science Foundation of China[42476094] ; Natural Science Foundation of Tianjin[23JCYBJC00240] ; Social Development and Agricultural Science and Technology Project of Tianjin[23YFZCSN00140] ; Young Scholar Program of Tianjin City Distinguished Professor |
| WOS研究方向 | Immunology ; Infectious Diseases ; Microbiology |
| 语种 | 英语 |
| WOS记录号 | WOS:001522132000001 |
| 出版者 | TAYLOR & FRANCIS INC |
| 源URL | [http://ir.qdio.ac.cn/handle/337002/202641]  |
| 专题 | 海洋研究所_实验海洋生物学重点实验室 |
| 通讯作者 | Li, Mo-Fei; Sun, Jin-Sheng |
| 作者单位 | 1.Qingdao Marine Sci & Technol Ctr, Lab Marine Biol & Biotechnol, Qingdao, Peoples R China 2.Tianjin Normal Univ, Coll Life Sci, Tianjin Key Lab Anim & Plant Resistance, Tianjin, Peoples R China 3.Chinese Acad Sci, Inst Oceanol, CAS Ctr Ocean Mega Sci, CAS Key Lab Expt Marine Biol, Qingdao, Peoples R China 4.Univ Chinese Acad Sci, Coll Earth & Planetary Sci, Beijing, Peoples R China 5.Yantai Univ, Sch Ocean, Yantai, Peoples R China |
| 推荐引用方式 GB/T 7714 | Li, Mo-Fei,Jin, Xiao-Yan,Liu, Heng,et al. Edwardsiella piscicida employs C3 derivative to mediate internalization and infection via the teleost-specific receptor[J]. VIRULENCE,2025,16(1):21. |
| APA | Li, Mo-Fei.,Jin, Xiao-Yan.,Liu, Heng.,Feng, Zhe.,Wu, Meng.,...&Sun, Jin-Sheng.(2025).Edwardsiella piscicida employs C3 derivative to mediate internalization and infection via the teleost-specific receptor.VIRULENCE,16(1),21. |
| MLA | Li, Mo-Fei,et al."Edwardsiella piscicida employs C3 derivative to mediate internalization and infection via the teleost-specific receptor".VIRULENCE 16.1(2025):21. |
入库方式： OAI收割
来源：海洋研究所
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