邻近标记技术在弓形虫蛋白质组学研究中的应用进展OA北大核心

Toxoplasma gondii(T.gondii)encodes numerous secretory proteins stored in organelles such as micronemes,rhoptries,and dense granules,which are secreted to different locations before and after the parasite invades host cells and play crucial roles in the infection,parasitism,and pathogenesis processes.The identification and functional studies of these secretory proteins are hotspots and challenges in the research of T.gondii pathogenesis.Traditional proteomic techniques face difficulties in sample purification and low coverage of proteomic information for T.gondii subcellular organelles,and they exhibit lower sensitivity in detecting transient or weak protein interactions.In recent years,the rapidly advancing proximity labeling technology(PL)has overcome these limitations.PL involves fusing bait proteins with specific catalytic enzymes to subsequently add biotin or biotin phenol to label nearby target proteins for biotinylation.This technology integrates the advantages of highly efficient enzyme-catalyzed reactions,enabling efficient labeling of proteins within specific spatial proximity,and can detect weak protein interactions.It has been widely used in biological research in recent years.This paper elaborates on the application of PL catalyzed by biotin ligase(BirA)and ascorbate acid peroxidase(APEX)in T.gondii proteomics research,introduces the contributions of these two labeling methods in the exploration of T.gondii secretory proteins and protein-protein interaction studies,and provides reference for the study of T.gondii pathogenesis and the prevention and control of toxoplasmosis.