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Dissecting S-itaconation at host-pathogen interactions with chemical proteomics tools
被引:0
|作者:
Liu, Zihua
[1
]
Wang, Chu
[1
,2
]
机构:
[1] Peking Univ, Acad Adv Interdisciplinary Studies, Peking Tsinghua Ctr Life Sci, Beijing 100871, Peoples R China
[2] Peking Univ, Coll Chem & Mol Engn, Synthet & Funct Biomol Ctr, Beijing Natl Lab Mol Sci,Key Lab Bioorgan Chem & M, Beijing 100871, Peoples R China
基金:
中国国家自然科学基金;
国家重点研发计划;
关键词:
ISOCITRATE LYASE;
ITACONIC ACID;
MYCOBACTERIUM-TUBERCULOSIS;
SUCCINATE-DEHYDROGENASE;
GENE-EXPRESSION;
DEFENSE PATHWAY;
METABOLISM;
INHIBITION;
GROWTH;
D O I:
10.1016/j.mib.2025.102579
中图分类号:
Q93 [微生物学];
学科分类号:
071005 ;
100705 ;
摘要:
The molecular essence of the battle between host and pathogens lies in the protein-protein or protein-metabolite interactions. Itaconate is one of the most upregulated immunometabolites, regulating immune responses through either noncovalent binding or covalent modification in the host. We herein briefly review recent progresses in the discoveries of physiological and pathological roles of itaconate and applications of chemical proteomic technologies in exploring itaconate modifications on cysteines (S-itaconation) at the interface of host-pathogen interactions. Key challenges are also proposed as future outlook.
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