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. 2022 May 17;10(5):e003733. doi: 10.1136/jitc-2021-003733

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© Author(s) (or their employer(s)) 2022. Re-use permitted under CC BY-NC. No commercial re-use. See rights and permissions. Published by BMJ.

This is an open access article distributed in accordance with the Creative Commons Attribution Non Commercial (CC BY-NC 4.0) license, which permits others to distribute, remix, adapt, build upon this work non-commercially, and license their derivative works on different terms, provided the original work is properly cited, appropriate credit is given, any changes made indicated, and the use is non-commercial. See http://creativecommons.org/licenses/by-nc/4.0/.

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Experimental design. Pleural effusions were collected from cancer and non-cancer patients, cells were separated and cultures were grown, when possible. HLA-peptide complexes were immunoaffinity-purified, peptides were separeted and analyzed by mass spectrometer. Peptides were considered HLA ligands after filtration of known contaminants, and if they were 8–14 amino-acids-long and matched the HLA allele consensus motifs of each patient, based on their tissue typing and online analysis with the NetMHCpan V.4.1 server http://www.cbs.dtu.dk/services/NetMHCpan/. Tumor antigens were identified from the peptides lists and candidates were tested for an immunogenic response. The figure was created using BioRender (https://biorender.com/). HLA, human leucocyte antigen; LC-MS/MS, liquid chromatography and tandem mass spectrometry.