{"database":"Pride","file_versions":[{"headers":{"Content-Type":["application/json"]},"body":{"files":{"Txt":["ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD071831/checksum.txt"],"Raw":["ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD071831/2025_08_20_PepMap_15cm_2um_direct_60min_DIA_HTERT_Infected_delta27_1.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD071831/2025_08_20_PepMap_15cm_2um_direct_60min_DIA_HTERT_Infected_delta27_3.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD071831/2025_08_20_PepMap_15cm_2um_direct_60min_DIA_Infected_F_1.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD071831/2025_08_20_PepMap_15cm_2um_direct_60min_DIA_SH_Infected_delta27_3.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD071831/2025_08_20_PepMap_15cm_2um_direct_60min_DIA_SH_Infected_delta27_1.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD071831/2025_08_20_PepMap_15cm_2um_direct_60min_DIA_HTERT_NT2.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD071831/2025_08_20_PepMap_15cm_2um_direct_60min_DIA_HTERT_Infetced_F_1.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD071831/2025_08_20_PepMap_15cm_2um_direct_60min_DIA_SH_NT1.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD071831/2025_08_20_PepMap_15cm_2um_direct_60min_DIA_Infected_F_2.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD071831/2025_08_20_PepMap_15cm_2um_direct_60min_DIA_HTERT_Infected_delta27_2.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD071831/2025_08_20_PepMap_15cm_2um_direct_60min_DIA_SH_NT3.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD071831/2025_08_20_PepMap_15cm_2um_direct_60min_DIA_HTERT_Infetced_F_3.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD071831/2025_08_20_PepMap_15cm_2um_direct_60min_DIA_HTERT_NT3.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD071831/2025_08_20_PepMap_15cm_2um_direct_60min_DIA_HTERT_NT1.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD071831/2025_08_20_PepMap_15cm_2um_direct_60min_DIA_HTERT_Infetced_F_2.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD071831/2025_08_20_PepMap_15cm_2um_direct_60min_DIA_Infected_F_3.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD071831/2025_08_20_PepMap_15cm_2um_direct_60min_DIA_SH_Infected_delta27_2.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD071831/2025_08_20_PepMap_15cm_2um_direct_60min_DIA_SH_NT2.raw"],"Other":["ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD071831/20250829_100456_InfectedHerpes.sne"]},"type":"primary"},"statusCode":"OK","statusCodeValue":200}],"scores":null,"additional":{"labhead_mail":["ctnmtn@unife.it"],"submitter":["Davide Barboni"],"technology_type":["Mass Spectrometry","Bottom-up proteomics","Data-independent acquisition"],"disease":["Herpes Simplex"],"software":[""],"submitter_keywords":["Hsv-1","Icp27","Htert rpe-1","Sh-sy5y","Apoptosis"],"full_dataset_link":["https://www.ebi.ac.uk/pride/archive/projects/PXD071831"],"tissue":["Epithelial Cell","Neuroblast Proliferation"],"sample_protocol":["The collected cell pellets were resuspended and lysed (solution containing 5% SDS, 5 mM TCEP, and 20 mM CAA in 100 mM Tris-HCl buffer pH 8.0 at 95°C, 1400 rpm for 10 minutes using a TS-100 thermo shaker (Biosan, Riga, Latvia)), sonicated and clarified by centrifugation at 5000 rpm for 10 minutes using a Fresco-17 Centrifuge (Thermo Fisher Scientific, Waltham, MA, USA).  Total protein concentration was quantified using the BCA Protein Assay Kit (Thermo Fisher Scientific Italia, Segrate, Italy). Protein purification was performed using MagReSyn® Hydroxyl magnetic beads (ReSyn Biosciences, Edenvale, South Africa), following the protocol of Koenig et al. (2023) with slight modifications. The protein samples were mixed with ACN, water, and magnetic beads to obtain a final ACN concentration of 70% and a protein-to-bead ratio of 1:2. After incubation for 2.5 minutes on a rocking platform at medium speed, the beads were retained with a DynaMag magnetic rack (Thermo Fisher Scientific Italia, Segrate, Italy) and washed repeatedly with 95% ACN and 70% ethanol, with shaking and magnetic separation at each step.  Bead digestion was performed in 100 mM Tris-HCl (pH 8.0) with trypsin (enzyme-to-protein ratio 1:50) at 37°C, 1200 rpm for 16 hours. Proteolysis was quenched by adjusting the pH to 2 with 1% TFA. The peptides were purified using an Oasis HLB 96-well Plate (3 mg sorbent; Waters, Milford, MA, USA); cartridges were conditioned with ACN and equilibrated twice with 0.1% TFA.  After sample loading, the columns were washed twice with 200 µL of 0.1% TFA, and peptides were eluted in two aliquots of 50 µL each containing 50% ACN and 0.1% TFA. Eluates were dried in a Concentrator Plus SpeedVac (Eppendorf, Hamburg, Germany) and reconstituted in 50 µL of 0.1% FA prior to liquid chromatography-tandem mass spectrometry (LC-MS/MS) analysis. Tryptic peptides were analyzed using a Vanquish Neo nano-HPLC system coupled online to an Orbitrap Exploris 240 mass spectrometer equipped with a nano-ESI Easy-Spray ion source (Thermo Fisher Scientific, Waltham, MA, USA). Mobile phase A was 0.1% FA in water, and mobile phase B was 80:20 ACN:water with 0.1% FA. Direct injection was performed onto an EASY-Spray PepMap Neo RP-C18 column (150 mm × 75 µm, 2 µm; Thermo Fisher Scientific, Waltham, MA, USA) at a flow rate of 500 nL/min, with the column temperature maintained at 35 °C. The total runtime was 60 min. The gradient elution was programmed as follows: 1% B for 1.5 min, linear increase to 31% B over 45 min, to 50% in 3.75 min, then to 95% in another 3.75 min. The 95% B phase was maintained for 6 min, followed by a rapid re-equilibration to initial conditions for the next injection. Peptides were ionized with a spray voltage of +1.9 kV and a capillary temperature of 280 °C. MS full-scan parameters: scan range 350-1100 Th, RF lens at 70%, Orbitrap resolution of 60,000 (FWHM at m/z 200), automatic maximum injection time, and AGC target of 100%.  MS/MS acquisition was performed in data independent acquisition (DIA) mode. The precursor mass range was 361-1033 Th, segmented into 56 isolation windows (12 Th each, with 1 Th overlap). The normalized HCD collision energy was set to 28%. Orbitrap resolution for MS2 was 15,000 (FWHM at m/z 200), with auto injection time and AGC target of 1000%. Instrument performance was monitored by blank injections after each batch of samples; a HeLa protein digest (Thermo Fisher Scientific, Waltham, MA, USA) was also injected as a quality control sample at regular intervals"],"repository":["Pride"],"quantification_method":[""],"modification":[""],"data_protocol":["All raw files were analyzed using Spectronaut v20, searching against a library automatically generated by combining Homo sapiens and Human herpesvirus 1 (strain 17) Swiss-Prot proteome database (https://www.uniprot.org/, last access 21/08/2025), supplemented with common contaminants and using default settings All experiments were executed in triplicate and independently repeated three times. MTT assay, LDH assay, qPCR, western blot, Caspase-Glo 3/7 activity assay, and flow cytometry data were analyzed using either one-way or two-way analysis of variance (ANOVA), followed by Dunnett’s post hoc test or Šídák’s multiple comparisons test, respectively. Data analyses were performed with GraphPad Prism software, version 9.0.0 for macOS (GraphPad Software, San Diego, CA, USA). Differences were considered statistically significant at p ≤ 0.05. For proteomic experiments, downstream analysis was performed using Perseus Software v.2.1.5 (285). Contaminants and proteins with Q-value > 0.05 were excluded from label-free quantification (LFQ) intensities, which were log2-transformed. Proteins lacking at least 3 out of 3 valid values in at least one of the experimental groups were filtered out. Missing values were imputed using a normal distribution with a downshift of 1.8 and a width of 0.3. Datasets were thus subsetted by cell line for independent analysis. Within each subset, an analysis of variance (ANOVA) with Benjamini-Hochberg false discovery rate (FDR) correction was conducted. Proteins with an adjusted Q-value ≤ 0.05 were considered significantly differentially expressed. After filtering out non-significant proteins, their log2-transformed LFQ intensities were Z-score normalized and subjected to unsupervised hierarchical clustering analysis. Additionally, differential expression analysis was performed within each subset using two-tailed t-tests with Benjamini-Hochberg FDR correction, testing all pairwise comparisons between the experimental conditions. Proteins with a Q-value ≤ 0.05 were considered statistically significant. Protein-protein interaction networks of differentially expressed proteins (DEPs) were generated using STRING database and imported into Cytoscape for visualization and clustering. Functional modules were identified by Markov Cluster Algorithm (MCL) with an inflation parameter set to 3."],"omics_type":["Proteomics"],"labhead":["Martina Catani"],"instrument_platform":[""],"labhead_affiliation":["Dipartimento di Scienze Chimiche, Farmaceutiche ed Agrarie, Università degli Studi di Ferrara"],"submission_type":["PARTIAL"],"species":["Homo Sapiens (human)"],"submitter_mail":["brbdvd1@unife.it"],"publication":["10.3389/FMICB.2026.1849379"],"submitter_affiliation":["Università degli Studi di Ferrara"],"submitter_country":["Italy"],"additional_accession":[]},"is_claimable":false,"name":"Life-Death Trade-offs: HSV-1 ICP27 as a Cellular Context-Dependent Regulator of Intrinsic Apoptosis","description":"Herpes simplex virus type 1 (HSV-1) infection represents an established model for studying virus-host interactions, given its ability to modulate cell fate and achieve long-term persistence. Among the immediate early genes, the multifunctional regulatory protein ICP27, encoded by the UL54 gene, plays a pivotal role in coordinating viral gene expression and remodeling host signaling pathways. This study investigates the role of ICP27 in modulating the intrinsic apoptotic pathway in two cell models representative of different stages of infection: hTert RPE-1 epithelial cells, modeling the lytic replication, and SH-SY5Y neuroblastoma cells, mimicking a neuron-like microenvironment.  To evaluate the specific function of HSV-1 ICP27 in this field, cells infected with wild-type HSV-1 (HSV-1 w.t.) were compared with a viral vector lacking ICP27 (HSV-1ΔICP27). Analyses were conducted using RT-qPCR for gene quantification, western blotting for protein evaluation, enzymatic assays to measure caspase activity, flow cytometry to determine reactive oxygen species (ROS) production and mitochondrial functionality, and quantitative proteomic approaches for the global characterization of infection-induced protein changes. ICP27 exerts cell type-dependent effects on apoptosis. In epithelial cells, ICP27 promotes programmed cell death by activating caspase-9 and effector caspases (3/7), increasing reactive oxygen species (ROS) generation, altering mitochondrial function, and elevating the Bax/Bcl-2 ratio, indicative of mitochondrial pathway activation. Conversely, in neuron-like cells, ICP27 suppresses apoptotic signaling by reducing caspase activity, limiting oxidative stress, and preserving mitochondrial integrity. These findings position ICP27 as a cellular context-dependent regulator of apoptosis, driving lytic apoptosis in epithelial cells while favoring host cell survival in neuronal environments. This dual behavior underscores HSV-1 adaptability across microenvironments, with implications for viral pathogenesis and therapeutic targeting.","dates":{"publication":"2026-06-16","submission":"2025-12-10"},"accession":"PXD071831","cross_references":{"TAXONOMY":["NEWT:108018","NEWT:377960","NEWT:1131","NEWT:190486","NEWT:2737160","NEWT:2042546","NEWT:148942","NEWT:295546","NEWT:258594","NEWT:1126","NEWT:1129","NEWT:89187","NEWT:309807","NEWT:89184","NEWT:309800","NEWT:156563","NEWT:1323429","NEWT:876138","NEWT:44271","NEWT:193516","NEWT:2315688","NEWT:44270","NEWT:592321","NEWT:1073882","NEWT:6819","NEWT:93217","NEWT:428386","NEWT:1117","NEWT:498257","NEWT:10036","NEWT:32264","NEWT:10034","NEWT:661410","NEWT:488003","NEWT:224326","NEWT:376619","NEWT:3765","NEWT:2433","NEWT:3767","NEWT:433727","NEWT:135622","NEWT:672127","NEWT:656061","NEWT:37965","NEWT:656064","NEWT:3760","NEWT:36630","NEWT:381198","NEWT:1176302","NEWT:418106","NEWT:10029","NEWT:913645","NEWT:2492962","NEWT:641809","NEWT:44250","NEWT:77151","NEWT:317447","NEWT:698761","NEWT:5530","NEWT:868565","NEWT:135674","NEWT:1562698","NEWT:1177","NEWT:11308","NEWT:12637","NEWT:2164133","NEWT:1180","NEWT:2767846","NEWT:1343074","NEWT:314344","NEWT:108061","NEWT:224308","NEWT:3134131","NEWT:49928","NEWT:160621","NEWT:110368","NEWT:1916073","NEWT:1310161","NEWT:1230383","NEWT:77133","NEWT:160620","NEWT:1310165","NEWT:114727","NEWT:5516","NEWT:498211","NEWT:347256","NEWT:5518","NEWT:398007","NEWT:1527468","NEWT:498217","NEWT:498216","NEWT:11320","NEWT:1410384","NEWT:1310173","NEWT:1072569","NEWT:1072568","NEWT:161934","NEWT:156587","NEWT:1148","NEWT:5508","NEWT:135666","NEWT:419481","NEWT:5507","NEWT:1140","NCBITaxon:2157","NEWT:2066563","NEWT:1143","NEWT:1462472","NEWT:1336795","NEWT:644042","NEWT:709964","NEWT:3712","NEWT:3711","NEWT:3714","NEWT:65121","NEWT:3716","NEWT:3715","NEWT:2065263","NEWT:1549675","NEWT:177437","NEWT:9014","NEWT:10891","NEWT:118221","NEWT:34869","NEWT:226126","NEWT:1616117","NEWT:34865","NEWT:28174","NEWT:550537","NEWT:284812","NEWT:284811","NEWT:2902907","NEWT:3701","NEWT:3702","NEWT:1245466","NEWT:3704","NEWT:1246791","NEWT:34875","NEWT:1431297","NEWT:9005","NEWT:34871","NEWT:9006","NEWT:33548","NEWT:1883426","NEWT:657321","NEWT:1423687","NEWT:657322","NEWT:10886","NEWT:3708","NEWT:536231","NEWT:219813","NEWT:1301262","NEWT:319224","NEWT:2305479","NEWT:215451","NEWT:460519","NEWT:272843","NEWT:272844","NEWT:1348799","NEWT:55784","NEWT:485","NEWT:2499525","NEWT:467144","NEWT:142786","NEWT:28196","NEWT:2853422","NEWT:487","NEWT:1679718","NEWT:387344","NEWT:657318","NEWT:480","NEWT:67767","NEWT:46835","NEWT:216778","NEWT:376686","NEWT:237610","EFO:0001352","NEWT:219809","NEWT:219808","NEWT:119562","NEWT:1883446","NEWT:1233435","NEWT:118223","NEWT:141469","NEWT:272831","NEWT:987059","NEWT:491","NEWT:422203","NEWT:460523","NEWT:2423","NEWT:85694","NEWT:85692","NEWT:911045","NEWT:3750","NEWT:123606","NEWT:85698","NEWT:291146","NEWT:233271","NEWT:3745","NEWT:1715989","NCBITaxon:4751","NEWT:3747","NEWT:278161","NEWT:415978","NEWT:410289","NEWT:191701","NEWT:9054","NEWT:472","NEWT:29459","NEWT:34839","NEWT:476","NEWT:1380096","NEWT:28128","NEWT:470","NEWT:41122","NEWT:1328300","NEWT:748693","NCBITaxon:50557","NEWT:63363","NEWT:3735","NEWT:29491","NEWT:911022","NEWT:446","NEWT:153481","NEWT:714485","NEWT:445","NEWT:2003758","NEWT:29486","NEWT:63366","NEWT:64697","NEWT:63367","NEWT:29488","NEWT:215402","NEWT:3726","NEWT:30455","NEWT:28141","NEWT:9030","NEWT:9031","NEWT:3728","NEWT:108931","NEWT:219799","NEWT:1325292","NEWT:219798","NEWT:548","NEWT:150475","NEWT:546","NEWT:1431340","NEWT:256737","NEWT:51350","NEWT:8694","NEWT:8692","NEWT:542","NEWT:394503","NEWT:13076","NEWT:219785","NEWT:451515","NEWT:8673","NEWT:550","NEWT:10804","NEWT:554","NEWT:451516","NEWT:552","NEWT:1325291","NEWT:42410","NEWT:40686","NEWT:1225786","NEWT:771870","NEWT:8665","NEWT:51338","NEWT:377142","NEWT:9995","NEWT:28112","NEWT:49012","NEWT:28110","NEWT:10832","NEWT:311339","NEWT:507601","NEWT:520","NEWT:64657","NEWT:186441","NEWT:2585209","NEWT:643680","NEWT:214092","NEWT:40697","NEWT:13095","NEWT:162425","NEWT:242124","NEWT:9986","NEWT:8654","NEWT:536","NEWT:8658","NEWT:1268063","NEWT:8657","NEWT:9983","NEWT:8655","NEWT:80833","NEWT:479096","NEWT:28108","NEWT:28104","NEWT:1114957","NEWT:568703","NEWT:568708","NEWT:51315","NEWT:52641","NEWT:353152","NEWT:116597","NEWT:353153","NEWT:116598","NEWT:227377","NEWT:1774284","NEWT:27689","NEWT:207769","NEWT:40674","NEWT:51329","NCBITaxon:1763","NEWT:443906","NEWT:6055","NEWT:13037","NEWT:519","NEWT:941638","NEWT:511","NEWT:7394","NEWT:6063","NEWT:404330","NEWT:1328388","NEWT:13064","NEWT:529120","NEWT:7375","NEWT:300641","NEWT:39655","NEWT:38323","NEWT:206411","NEWT:80869","NEWT:214053","NEWT:80863","NEWT:665890","NEWT:52639","NEWT:52638","NEWT:8697","NEWT:861109","NEWT:8695","NEWT:1196866","NEWT:6039","NEWT:37003","NEWT:1045775","NEWT:1123869","NCBITaxon:1335626","NEWT:7370","NEWT:280406","NEWT:83906","NEWT:99488","NEWT:99487","NEWT:1134506","NEWT:255470","NEWT:762903","NEWT:27697","NEWT:86185","NEWT:9935","NEWT:266940","NEWT:287889","NEWT:9938","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