Edwardsiella piscicida employs C3 derivative to mediate internalization and infection via the teleost-specific receptor
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 bi...
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| Format: | Article |
| Language: | English |
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Taylor & Francis Group
2025-12-01
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| Series: | Virulence |
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| Online Access: | https://www.tandfonline.com/doi/10.1080/21505594.2025.2526783 |
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| author | Mo-Fei Li Xiao-Yan Jin Heng Liu Zhe Feng Meng Wu Hong-Qiang Zhang Yu-Ting Du Yuan-Yuan Sun Xue-Peng Li Jin-Sheng Sun |
| author_facet | Mo-Fei Li Xiao-Yan Jin Heng Liu Zhe Feng Meng Wu Hong-Qiang Zhang Yu-Ting Du Yuan-Yuan Sun Xue-Peng Li Jin-Sheng Sun |
| author_sort | Mo-Fei Li |
| collection | DOAJ |
| description | 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. |
| format | Article |
| id | doaj-art-cfc3920033684d6fb64461bc19251065 |
| institution | Kabale University |
| issn | 2150-5594 2150-5608 |
| language | English |
| publishDate | 2025-12-01 |
| publisher | Taylor & Francis Group |
| record_format | Article |
| series | Virulence |
| spelling | doaj-art-cfc3920033684d6fb64461bc192510652025-08-20T03:29:15ZengTaylor & Francis GroupVirulence2150-55942150-56082025-12-0116110.1080/21505594.2025.2526783Edwardsiella piscicida employs C3 derivative to mediate internalization and infection via the teleost-specific receptorMo-Fei Li0Xiao-Yan Jin1Heng Liu2Zhe Feng3Meng Wu4Hong-Qiang Zhang5Yu-Ting Du6Yuan-Yuan Sun7Xue-Peng Li8Jin-Sheng Sun9Tianjin Key Laboratory of Animal and Plant Resistance, College of Life Sciences, Tianjin Normal University, Tianjin, ChinaTianjin Key Laboratory of Animal and Plant Resistance, College of Life Sciences, Tianjin Normal University, Tianjin, ChinaTianjin Key Laboratory of Animal and Plant Resistance, College of Life Sciences, Tianjin Normal University, Tianjin, ChinaTianjin Key Laboratory of Animal and Plant Resistance, College of Life Sciences, Tianjin Normal University, Tianjin, ChinaCAS Key Laboratory of Experimental Marine Biology, CAS Center for Ocean Mega-Science, Institute of Oceanology, Chinese Academy of Sciences, Qingdao, ChinaTianjin Key Laboratory of Animal and Plant Resistance, College of Life Sciences, Tianjin Normal University, Tianjin, ChinaTianjin Key Laboratory of Animal and Plant Resistance, College of Life Sciences, Tianjin Normal University, Tianjin, ChinaCAS Key Laboratory of Experimental Marine Biology, CAS Center for Ocean Mega-Science, Institute of Oceanology, Chinese Academy of Sciences, Qingdao, ChinaSchool of Ocean, Yantai University, Yantai, ChinaTianjin Key Laboratory of Animal and Plant Resistance, College of Life Sciences, Tianjin Normal University, Tianjin, ChinaEdwardsiella 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.https://www.tandfonline.com/doi/10.1080/21505594.2025.2526783Edwardsiella piscicidacomplementC3internalizationinfection |
| spellingShingle | Mo-Fei Li Xiao-Yan Jin Heng Liu Zhe Feng Meng Wu Hong-Qiang Zhang Yu-Ting Du Yuan-Yuan Sun Xue-Peng Li Jin-Sheng Sun Edwardsiella piscicida employs C3 derivative to mediate internalization and infection via the teleost-specific receptor Virulence Edwardsiella piscicida complement C3 internalization infection |
| title | Edwardsiella piscicida employs C3 derivative to mediate internalization and infection via the teleost-specific receptor |
| title_full | Edwardsiella piscicida employs C3 derivative to mediate internalization and infection via the teleost-specific receptor |
| title_fullStr | Edwardsiella piscicida employs C3 derivative to mediate internalization and infection via the teleost-specific receptor |
| title_full_unstemmed | Edwardsiella piscicida employs C3 derivative to mediate internalization and infection via the teleost-specific receptor |
| title_short | Edwardsiella piscicida employs C3 derivative to mediate internalization and infection via the teleost-specific receptor |
| title_sort | edwardsiella piscicida employs c3 derivative to mediate internalization and infection via the teleost specific receptor |
| topic | Edwardsiella piscicida complement C3 internalization infection |
| url | https://www.tandfonline.com/doi/10.1080/21505594.2025.2526783 |
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