{"database":"Pride","file_versions":[{"headers":{"Content-Type":["application/json"]},"body":{"files":{"Txt":["ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/07/PXD070575/checksum.txt"],"Csv":["ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/07/PXD070575/proteins.csv","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/07/PXD070575/protein-peptides.csv"],"Mzxml":["ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/07/PXD070575/SaraZaldivar_sol472-1-22_WT-1_DDA-PASEF_0.5sec_3-9-2022_Slot1-28_1_505.mzxml","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/07/PXD070575/SaraZaldivar_sol472-1-22_ORF7a-1_DDA-PASEF_0.5sec_3-9-2022_Slot1-31_1_511.mzxml","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/07/PXD070575/SaraZaldivar_sol472-1-22_ORF7a-2_DDA-PASEF_0.5sec_3-9-2022_Slot1-31_1_513.mzxml","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/07/PXD070575/SaraZaldivar_sol472-1-22_WT-2_DDA-PASEF_0.5sec_3-9-2022_Slot1-29_1_507.mzxml","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/07/PXD070575/SaraZaldivar_sol472-1-22_WT-3_DDA-PASEF_0.5sec_3-9-2022_Slot1-30_1_509.mzxml","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/07/PXD070575/SaraZaldivar_sol472-1-22_ORF7a-3_DDA-PASEF_0.5sec_3-9-2022_Slot1-31_1_515.mzxml"],"Mzid":["ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/07/PXD070575/peptides_1_1_0.mzid"],"Mgf":["ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/07/PXD070575/SaraZaldivar_sol472-1-22_WT-3_DDA-PASEF_0.5sec_3-9-2022_Slot1-30_1_509.mgf","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/07/PXD070575/SaraZaldivar_sol472-1-22_ORF7a-2_DDA-PASEF_0.5sec_3-9-2022_Slot1-31_1_513.mgf","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/07/PXD070575/SaraZaldivar_sol472-1-22_WT-2_DDA-PASEF_0.5sec_3-9-2022_Slot1-29_1_507.mgf","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/07/PXD070575/SaraZaldivar_sol472-1-22_ORF7a-1_DDA-PASEF_0.5sec_3-9-2022_Slot1-31_1_511.mgf","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/07/PXD070575/SaraZaldivar_sol472-1-22_ORF7a-3_DDA-PASEF_0.5sec_3-9-2022_Slot1-31_1_515.mgf","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/07/PXD070575/SaraZaldivar_sol472-1-22_WT-1_DDA-PASEF_0.5sec_3-9-2022_Slot1-28_1_505.mgf"]},"type":"primary"},"statusCode":"OK","statusCodeValue":200}],"scores":null,"additional":{"labhead_mail":["b52gagat@uco.es"],"submitter":["Raúl Fernández Rodríguez"],"technology_type":["Data-dependent acquisition","Mass Spectrometry","Gel-based experiment","Bottom-up proteomics"],"software":[""],"submitter_keywords":["Sars-cov-2","Sars-cov-2; accessory proteins; orf7a; covid-19","accessory proteins","covid-19","orf7a"],"full_dataset_link":["https://www.ebi.ac.uk/pride/archive/projects/PXD070575"],"tissue":["Lung","Epithelial Cell"],"sample_protocol":["Protein extracts underwent clean-up in one dimensional sodium dodecyl sulfate-polyacrylamide gel electrophoresis with 10% polyacrylamide. After electrophoresis at 100 V, gel was stained with Coomassie Blue and protein bands were cut out and stored in water until digestion. Protein bands were first destained in 200 mM ammonium bicarbonate (AB)/50% acetonitrile, then in 100% acetonitrile, reduced with 20 mM dithiothreitol and incubated in 25 mM AB at 55 °C. After cooling to room temperature, free thiols were alkylated with 40 mM iodoacetamide. Following two AB washes, proteins were digested with trypsin (Promega, Madison, WI, USA) and incubated overnight at 37 °C. Digestion was stopped by adding trifluoroacetic acid to a final concentration of 1%. Digested samples were dried and resuspended in 0.1% formic acid (FA). Nano liquid chromatography (LC) was performed on a Dionex Ultimate 3000 nano ultra performance LC (Thermo Scientific Inc., Waltham, MA, USA) with a C18 75 µm × 50 Acclaim Pepmap column (Thermo Scientific Inc., Waltham, MA, USA). Peptides were loaded onto a 300 µm × 5 mm Acclaim Pepmap precolumn (Thermo Scientific Inc., Waltham, MA, USA) in 2% acetonitrile/0.05% trifluoroacetic acid, then separated at 40 °C with a gradient of buffer A (water with 0.1% FA) and buffer B (20% acetonitrile with 0.1% FA) over 85 min of chromatography. Peptide cations were ionized and analyzed on a Thermo Orbitrap Fusion (Q-OT-qIT, Thermo Scientific Inc., Waltham, MA, USA), operated in positive mode with survey scans at 120K resolution. Tandem mass spectrometry (MS/MS) involved quadrupole isolation, collision-induced dissociation fragmentation, and rapid scan MS analysis, sampling only precursors with charge states 2–5. The instrument operated in top speed mode with 3 s MS2 cycles, excluding precursors dynamically."],"repository":["Pride"],"quantification_method":[""],"modification":[""],"data_protocol":["MS2 spectra were analyzed using MaxQuant software v. 1.6.17.0, with the Andromeda search engine set against a Uniprot_proteome_Homo-sapiens_database. Peptides were generated through tryptic digestion with up to one missed cleavage, fixed carbamidomethylation of cysteines, and variable oxidation of methionine. The mass tolerance was 10 ppm, and product ions were searched with 0.6 Da tolerance. Peptide matches were filtered to a 1% false discovery rate (FDR). Quantification was conducted using the MaxLFQ label-free method, using retention time alignment and match-between-runs protocol."],"omics_type":["Proteomics"],"labhead":["Tránsito García García"],"instrument_platform":[""],"labhead_affiliation":["Department of Genetics, Immunogenomics and Molecular Pathogenesis Group, UIC Zoonoses and Emergent Diseases ENZOEM, University of Córdoba, Córdoba, Spain"],"submission_type":["COMPLETE"],"species":["Homo Sapiens (human)"],"submitter_mail":["b42feror@uco.es"],"publication":["Not available"],"submitter_affiliation":["Department of Genetics, Immunogenomics and Molecular Pathogenesis Group, UIC Zoonoses and Emergent Diseases ENZOEM, University of Córdoba, Córdoba, Spain."],"submitter_country":["Spain"],"doi":["10.6019/PXD070575"],"additional_accession":[]},"is_claimable":false,"name":"Proteomics of A549 and A549 cells transducted with ORF7a SARS-CoV-2 accessory protein","description":"SARS-CoV-2 reprograms host metabolism to facilitate immune evasion and viral replication. While infection is known to impair mitochondrial function and enhance glycolysis, the role of viral accessory proteins in these alterations remains unclear. Here, we investigate the metabolic impact of the accessory protein ORF7a. Using lentiviral transduction, we expressed ORF7a in human lung epithelial (A549) and monocytic (THP1) cells. Integrated transcriptomic, proteomic, and metabolomic analyses in A549 cells revealed profound dysregulation of glucose and lipid metabolism. ORF7a impaired oxidative phosphorylation, as shown by reduced basal and maximal respiration, mitochondrial depolarization, and elevated reactive oxygen species. ORF7a induced upregulation of pyruvate dehydrogenase kinase 4 (PDK4) and increased phosphorylation of the pyruvate dehydrogenase complex (PDHC), leading to impaired pyruvate oxidation. However, pharmacological inhibition of PDK4 with dichloroacetate failed to rescue mitochondrial respiration, suggesting additional dysfunction. Enzymatic assays confirmed reduced complex I activity, pointing to direct impairment of the electron transport chain. Our findings demonstrate that ORF7a orchestrates a multifaceted metabolic reprogramming involving PDK4-dependent PDHC inhibition and complex I dysfunction. These results highlight ORF7a as a key modulator of host metabolism and underscore mitochondrial pathways as potential therapeutic targets in 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