丁璟珒

中国科学院生物物理研究所

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  • 丁璟珒
  • 研究员

丁璟珒 博士 研究员

国家“优秀青年基金”获得者

中国科学院生物物理研究所,生物大分子国家重点实验室,研究组长

研究方向:病原菌感染和宿主天然免疫防御的分子机理

电子邮件(E-mail) jding(AT)ibp.ac.cn

电话(Tel) 010-64888548

传真(Fax) 010-64888548

邮政编码 100101

英文版个人网页

简历 & 研究工作摘要

1999.09-2003.07 武汉大学生命科学学院,理学学士

2003.09-2008.07 中国科学院生物物理研究所,理学博士

2008.10-2010.11中国科学院生物物理研究所,博士后

2010.11-2011.12 中国科学院生物物理研究所,助理研究员

2012.01-2016.12 中国科学院生物物理研究所,副研究员

2017.01-2017.12 中国科学院生物物理研究所,项目研究员

2013.04-2017.12 北京生命科学研究所,访问学者

2018.01-至今 中国科学院生物物理研究所 研究员

研究方向

病原细菌的感染是人类生命活动的重要威胁,利用独特的效应蛋白破坏机体的正常信号转导或表达专门的耐药基因拮抗抗菌药物的杀灭,是许多病原菌感染致病的关键分子机制;天然免疫系统是机体抵御病原菌感染的第一道防线,通过特异识别、精确激活和高效应答清除病原菌的感染,保护机体健康。病原菌感染和宿主天然免疫防御是病原菌与宿主相互作用的重要体现,关键的科学问题是破解病原菌感染与免疫识别应答的分子机理。本课题组围绕天然免疫防御和病原菌感染与耐药这一主题开展了系统的研究工作,取得了重要的研究成果,包括破解宿主天然免疫应答中细胞焦亡的关键分子机制(Nature 2016),揭示病原菌通过新颖的精氨酸糖基化修饰阻断宿主死亡受体信号通路的完整分子机理(Mol Cell 2019),揭示超级细菌金属β内酰胺酶NDM-1水解头孢类抗生素的催化机制(JACS 2014)。现阶段课题组将继续聚焦病原菌与宿主天然免疫通路的直接对话,深入研究病原菌效应蛋白拮抗宿主天然免疫防御通路的精确分子机制,揭示新型天然免疫受体识别病原相关分子模式激活免疫应答的工作原理,为抗菌感染、免疫调节和抗炎治疗药物的研发提供坚实的理论基础。

代表性论文(*Corresponding Authors, # First Authors)

1. Ding, J.*, Pan X, Du L, Yao Q, Xue J, Yao H, Wang DC, Li S*, Shao F*. (2019). Structural and functional insights into host death domains Inactivation by the Bacterial Arginine GlcNAcyltransferase Effector. Mol Cell. 74, 922-35.

2. Ding, J.* & Shao F*. (2018). Growing a gasdermin pore in membranes of pyroptotic cells. EMBO J. 37, e100067.

3. Ding, J. & Shao, F. (2017). SnapShot: The Noncanonical Inflammasome. Cell. 168, 544-4.

4. Ding, J., Wang, K., Liu, W., She, Y., Sun, Q., Shi, J., Sun, H., Wang, D. C.*& Shao, F.* (2016). Pore-forming activity and structural autoinhibition of the gasdermin family. Nature. 535, 111-6.

5. Wang, X., Hou, Y., Deng, K., Zhang, Y., Wang, D. C.* & Ding, J.* (2015). Structural Insights into the Molecular Recognition between Cerebral Cavernous Malformation 2 and Mitogen-Activated Protein Kinase Kinase Kinase 3. Structure. 23, 1087-96.

6. Feng, H.#, Ding, J.#, Zhu, D.#, Liu, X., Xu, X., Zhang, Y., Zang, S., Wang, D. C.*& Liu, W.* (2014). Structural and mechanistic insights into NDM-1 catalyzed hydrolysis of cephalosporins. J Am Chem Soc. 136, 14694-7.

7. Wang, W.#, Ding, J.#, Zhang, Y., Hu, Y.*& Wang, D. C.* (2014). Structural insights into the unique single-stranded DNA-binding mode of Helicobacter pylori DprA. Nucleic Acids Res. 42, 3478-91.

8. Guo, L.#, Ding, J.#, Guo, R., Hou, Y., Wang, D. C.*& Huang, L.* (2014). Biochemical and structural insights into RNA binding by Ssh10b, a member of the highly conserved Sac10b protein family in Archaea. J Biol Chem. 289, 1478-90.

9. Xu, X., Wang, X., Zhang, Y., Wang, D. C.* & Ding, J.* (2013). Structural basis for the unique heterodimeric assembly between cerebral cavernous malformation 3 and germinal center kinase III. Structure. 21, 1059-66.

10. Wang, T.#, Ding, J.#, Zhang, Y., Wang, D. C.* & Liu, W.* (2013). Complex structure of type VI peptidoglycan muramidase effector and a cognate immunity protein. Acta Crystallogr D Biol Crystallogr. 69, 1889-900.

11. Ding, J.#, Wang, W.#, Feng, H., Zhang, Y. & Wang, D. C. (2012). Structural insights into the Pseudomonas aeruginosa type VI virulence effector Tse1 bacteriolysis and self-protection mechanisms. J Biol Chem. 287, 26911-20.

12.Gong, Y.#, Zhu, D.#, Ding, J.#, Dou, C. N., Ren, X., Gu, L., Jiang, T. * & Wang, D. C.*(2011). Crystal structures of aprataxin ortholog Hnt3 reveal the mechanism for reversal of 5'-adenylated DNA. Nat Struct Mol Biol. 18, 1297-9.

13. Ding, J., Wang, X., Li, D. F., Hu, Y., Zhang, Y. & Wang, D. C. (2010). Crystal structure of human programmed cell death 10 complexed with inositol-(1,3,4,5)-tetrakisphosphate: a novel adaptor protein involved in human cerebral cavernous malformation. Biochem Biophys Res Commun. 399, 587-92.

14. Ding, J., Bao, J., Zhu, D., Zhang, Y. & Wang, D. C. (2010). Crystal structures of a novel anti-HIV mannose-binding lectin from Polygonatum cyrtonema Hua with unique ligand-binding property and super-structure. J Struct Biol. 171, 309-17.

资料来源:丁璟珒研究员,2019-10-16