{"database":"Pride","file_versions":[{"headers":{"Content-Type":["application/json"]},"body":{"files":{"Txt":["ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/04/PXD067198/proteinGroups.txt"],"Raw":["ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/04/PXD067198/VL_0007219_DIEGO_21_2.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/04/PXD067198/VL_0007218_DIEGO_21_1.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/04/PXD067198/VL_0007215_DIEGO_20_2_200313110204.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/04/PXD067198/VL_0007206_DIEGO_18_1_200313024537.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/04/PXD067198/VL_0007207_DIEGO_18_2.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/04/PXD067198/VL_0007203_DIEGO_17_2.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/04/PXD067198/VL_0007204_DIEGO_17_3.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/04/PXD067198/VL_0007202_DIEGO_17_1.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/04/PXD067198/VL_0007222_DIEGO_22_1.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/04/PXD067198/VL_0007223_DIEGO_22_2.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/04/PXD067198/VL_0007211_DIEGO_19_2.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/04/PXD067198/VL_0007210_DIEGO_19_1.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/04/PXD067198/VL_0007214_DIEGO_20_1_200313083815.raw"],"Fasta":["ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/04/PXD067198/uniprotkb_taxonomy_id_237561_2025_01_15canonical.fasta"]},"type":"primary"},"statusCode":"OK","statusCodeValue":200}],"scores":null,"additional":{"labhead_mail":["allanguimaraes@id.uff.br"],"submitter":["Allan Guimaraes"],"technology_type":["Data-dependent acquisition","Mass Spectrometry"],"disease":["Candidiasis"],"software":[""],"submitter_keywords":["Candida albicans. lectin-fc","Antifungal effects"],"full_dataset_link":["https://www.ebi.ac.uk/pride/archive/projects/PXD067198"],"tissue":["Permanent Cell Line Cell"],"sample_protocol":["Yeasts pellets were resuspended in a solution containing 7 M Urea, 2 M Thiourea, and 100 mM HEPES. Subsequently, dithiothreitol was added to achieve a final concentration of 10 mM, and samples were incubated for 1 h at 30°C. Iodoacetamide was added to a final concentration of 40 mM, and the samples were incubated for an additional 30 min in the dark. Following this, 175 μL of ultrapure water (TEDIA) was added, and the samples were trypsinized overnight at 37°C by adding trypsin (0.1 μg/μL in 0.1 M acetic acid) to achieve a final concentration of 16 ng/μL). Then, 2 μL of 10% trifluoroacetic acid (TFA) was added to achieve a final concentration of 0.1%, and peptides were purified using UltraMicroSpin™columns (Harvard Apparatus), before drying in a speed vac (ThermoScientific). The tryptic peptides were solubilized in 10 μL of 0.1% TFA and approximately 4 μL of the mixture were loaded onto an in‐house packed column (15 cm × 75μm) filled with 3 μm ReproSil C18 resin (Dr. Maisch GmbH) using the Nano LC-Ultra nano liquid chromatography system (Eksigent Technologies)."],"repository":["Pride"],"quantification_method":[""],"modification":[""],"data_protocol":["Mass spectra were acquired in positive mode Data-Dependent Acquisition (DDA) method. The MS1 scan was acquired in an Orbitrap analyzer (ThermoScientific) set for a 350-1800 m/z range, 60000 resolution (at m/z 400), with a 10000 minimal signal required and 2.0 isolation width. The most intense ions were fragmented by collision-induced dissociation at 30 Collision Energy, with a dynamic exclusion of 30 s. The acquired spectra were processed and analyzed using the MaxQuant 2.4.4.0 software (Max Plank Institute of Biochemistry) for peptide identification against the UniProt Candida albicans (strain SC5314 / ATCC MYA-2876) database (as of June 2023). The considered parent mass error and fragment mass error  tolerance were respectively set to 0.6 Da and 0.5 Da, with a monoisotopic.precursor mass search type. Two maximum missed tryptic cleavage were allowed, along with one non‐specific cleavage. Carbamidomethylation (MW = 57.02 Da) was set as a fixed modification, while methionine oxidation (MW = 15.99 Da) as the variable modification. Gene ontology analysis on identified proteins was performed using the DAVID functional annotation tool (DAVID Bioinformatics Resources, NIAID/NIH). Protein interaction networks were mapped using the String database (https://string-db.org/)."],"omics_type":["Proteomics"],"labhead":["Allan Jefferson Guimaraes"],"instrument_platform":[""],"labhead_affiliation":["Fluminense Federal Unibersity"],"submission_type":["PARTIAL"],"species":["Candida Albicans (yeast)"],"submitter_mail":["allanguimaraes@id.uff.br"],"publication":["Not available"],"submitter_affiliation":["Federal Flumunense University"],"submitter_country":["Brazil"],"additional_accession":[]},"is_claimable":false,"name":"Lectin-Fc(IgG2a) fusion proteins binding to the cell wall of C. albicans cause structural, metabolic, oxidative, and other pleiotropic effects","description":"Candida albicans, an opportunist fungal pathogen ranked top among those causing hospital-acquired infections, exhibits diverse virulence factors aiding its survival within the human body. The rise of multidrug resistance (MDR) in C. albicans requires urgent development of new alternative antifungal therapies. Through genetic engineering gene fusion technologies, our group developed Lectin- Fc(IgG2a) proteins (WGA-Fc(IgG) and Dectin-1-Fc(IgG)) exhibiting antifungal effects against various endemic mycosis and consisting of promising options to combat fungal infections. This study explores the direct impact of Lectin-Fc treatments on C. albicans, shedding light on potential mechanisms disrupting fungal survival and growth. Our results revealed Lectin-Fc(IgG2a) proteins' ability to reduce key polysaccharides on the fungal cell wall. Co-incubations also resulted in oxidative stress in the fungus and alterations in the yeast micronutrient content and lipid reserves. Furthermore, Lectin-Fc(IgG2a) impacted fungal secretion and impeded the release of extracellular vesicles (EVs). The proteomic analysis demonstrated differential protein expression in both the whole C. albicans yeast and EVs post-Lectin-Fc(IgG2a). Notably, these antibody-like structures are slowly degraded by secreted aspartyl proteases (Saps) in vitro, as sap mutants are more prone to growth inhibition. Finally, Lectin-Fc(IgG2a) opsonization enhanced the activation of dendritic cells, contributing to fungal killing. These findings affirm Lectin-Fc(IgG2a) proteins as viable alternatives for therapeutic interventions against fungal infections. Beyond their antibodies-like functions, they induce fungal morphological alterations, and oxidative and metabolic stress, increasing the susceptibility of their cell wall to host immune recognition and 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