2026-08-05T15:04:45Zhttps://repisalud.isciii.es/rest/oai/request

oai:repisalud.isciii.es:20.500.12105/72452025-03-27T10:05:59Zcom_20.500.12105_2052com_20.500.12105_2051col_20.500.12105_19609

00925njm 22002777a 4500 dc Putri, Rindia M. author Allende-Ballestero, Carolina author Luque, Daniel author Klem, Robin author Rousou, Katerina-Asteria author Liu, Aijie author Traulsen, Christoph H.-H. author Rurup, W. Frederik author Koay, Melissa S. T. author Castón, José R author Cornelissen, Jeroen J. L. M. author 2017-11-22 Recent years have witnessed the emergence of bacterial semiorganelle encapsulins as promising platforms for bio-nanotechnology. To advance the development of encapsulins as nanoplatforms, a functional and structural basis of these assemblies is required. Encapsulin from Brevibacterium linens is known to be a protein-based vessel for an enzyme cargo in its cavity, which could be replaced with a foreign cargo, resulting in a modified encapsulin. Here, we characterize the native structure of B. linens encapsulins with both native and foreign cargo using cryo-electron microscopy (cryo-EM). Furthermore, by harnessing the confined enzyme (i.e., a peroxidase), we demonstrate the functionality of the encapsulin for an in vitro surface-immobilized catalysis in a cascade pathway with an additional enzyme, glucose oxidase. We also demonstrate the in vivo functionality of the encapsulin for cellular uptake using mammalian macrophages. Unraveling both the structure and functionality of the encapsulins allows transforming biological nanocompartments into functional systems. ACS Nano. 2017;26;11(12):12796-12804. 10.1021/acsnano.7b07669 1936-086X 1936-0851 ACS Nano 29166561 http://hdl.handle.net/20.500.12105/7245 Bacterial compartments Cryo-electron microscopy Encapsulin Nanoplatforms Nanoreactors Structural Characterization of Native and Modified Encapsulins as Nanoplatforms for in Vitro Catalysis and Cellular Uptake