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Cultures were then divided and incubated at 37 °C for 1 h 30 min under either neutral (pH 7) or acidic (pH 5) conditions. Cells were harvested, frozen in liquid nitrogen, and lyophilised. Total proteins were extracted using lysis buffer containing 50 mM Tris-Cl (pH 7.5), 1% sodium deoxycholate, 1% Triton X-100, phosphatase inhibitors, and protease inhibitors. For affinity purification, lysates from Wcp1-mCherry strains were incubated with RFP-Trap agarose beads, and lysates from Wcp1-4×FLAG strains were incubated with anti-FLAG antibody followed by Protein G agarose beads. After incubation, beads were washed three times with lysis buffer, and bound proteins were eluted using SDS sample buffer. Eluted proteins were separated by SDS–PAGE and subjected to in-gel trypsin digestion prior to LC–MS/MS analysis."],"repository":["Pride"],"modification":[""],"quantification_method":[""],"data_protocol":["Peptide samples were analysed using an Orbitrap Exploris 240 mass spectrometer coupled to a nanoLC system in data-dependent acquisition mode. Raw MS data were processed using Proteome Discoverer (version 2.5, Thermo Scientific) and searched against the Cryptococcus neoformans H99 reference proteome database using the Sequest HT search engine. Trypsin was specified as the digestion enzyme, allowing up to two missed cleavages. Carbamidomethylation of cysteine was set as a fixed modification, while oxidation of methionine and protein N-terminal acetylation were set as variable modifications. Peptide-spectrum matches and protein identifications were filtered using a false discovery rate (FDR) threshold of <1% based on a target–decoy strategy. Protein groups were assembled for downstream analysis. Comparative analyses were performed to identify Wcp1-associated proteins enriched under pH 5 or pH 7 conditions."],"omics_type":["Proteomics"],"labhead":["Yong-Sun Bahn"],"instrument_platform":[""],"submission_type":["COMPLETE"],"labhead_affiliation":["Department of Biotechnology, College of Life Science and Biotechnology, Yonsei University, Seoul 03722, Korea"],"species":["Fungi","Cryptococcus Neoformans H99-ypd_1"],"publication":["Not available"],"submitter_mail":["chsami2@naver.com"],"submitter_affiliation":["Department of Biotechnology, College of Life Science and Biotechnology, Yonsei University, Seoul 03722, Korea"],"submitter_country":["South Korea"],"doi":["10.6019/PXD077146"],"additional_accession":[]},"is_claimable":false,"name":"Cryptococcus Wcp1-mCherry Wcp1-FLAG AP–MS","description":"This study aims to identify Wcp1-interacting proteins in Cryptococcus neoformans under different pH conditions. Wcp1 is a WD40–cyclophilin fusion protein implicated in adaptation to host-associated stresses, including CO2, temperature, and acidic pH.   Affinity purification coupled with liquid chromatography–tandem mass spectrometry (AP–LC–MS/MS) was performed using Wcp1-mCherry and Wcp1-4×FLAG tagged strains to define the Wcp1 interactome under neutral (pH 7) and acidic (pH 5) 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