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Calreticulin S-Domain Binds to Human Complement C1q to Interfere With C1q-Mediated Immune Functions

Front Immunol. 2020-11; 
Shuai Shao, Chunyue Hao, Bin Zhan, Qinghui Zhuang, Limei Zhao, Yi Chen, Jingjing Huang, Xinping Zhu
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Recombinant Antibody Expression … contaminating the purified recombinant proteins was removed using Pierce High Capacity Endotoxin Removal Resin (Invitrogen, Carlsbad, CA, USA), and endotoxin removal was confirmed using the ToxinSensor Endotoxin Detection System (GenScript, Nanjing, China) … Get A Quote

摘要

Helminths develop strategies to escape host immune responses that facilitate their survival in the hostile host immune environment. , a tissue-dwelling nematode, has developed a sophisticated strategy to escape complement attack. Our previous study demonstrated that secretes calreticulin (CRT) to inhibit host classical complement activation through binding to C1q; however, the C1q binding site in CRT and the specific mechanism involved with complement-related immune evasion remains unknown. Using molecular docking modeling and fragment expression, we determined that CRT-S, a 153-aa domain of CRT, is responsible for C1q binding. Recombinant CRT-S protein expressed in had the same capacity to bind and inhibit h... More

关键词

Trichinella spiralis, binding site, calreticulin S-domain, classical complement activation, complement C1q, immune evasion, neutrophil, neutrophil extracellular traps