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. 2022 Aug 10;13:4701. doi: 10.1038/s41467-022-32384-z

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© The Author(s) 2022

Open Access This article is licensed under a Creative Commons Attribution 4.0 International License, which permits use, sharing, adaptation, distribution and reproduction in any medium or format, as long as you give appropriate credit to the original author(s) and the source, provide a link to the Creative Commons license, and indicate if changes were made. The images or other third party material in this article are included in the article’s Creative Commons license, unless indicated otherwise in a credit line to the material. If material is not included in the article’s Creative Commons license and your intended use is not permitted by statutory regulation or exceeds the permitted use, you will need to obtain permission directly from the copyright holder. To view a copy of this license, visit http://creativecommons.org/licenses/by/4.0/.

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Fig. 4 — a The size of the Nd-reconstituted PLC remains unchanged after peptide binding and GluII trimming as demonstrated by SEC. Peptide loading and glycan trimming by GluII does not change the overall composition and stoichiometry of the PLC. b, c The PLC remains fully assembled after MHC I loading with high-affinity peptide epitope (CSN) and GluII-catalyzed deglucosylation of MHC I, as demonstrated by SDS-PAGE (b) and immunoblotting (c) of SEC fractions corresponding to the PLC and GluII peak. The data are representative of two biological replicas. Source data are provided as a Source Data file.