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Samples were then centrifuged at 15,000 x g for 5 minutes to pellet cellular debris, and the supernatant was collected. Protein concentration was determined by BCA (Thermo Scientific), after which samples were diluted to 1 mg/mL in 5% SDS, 50 mM TEAB. 25 µg of protein from each sample was reduced with dithiothreitol to 2 mM, followed by incubation at 55°C for 60 minutes. Iodoacetamide was added to 10 mM and incubated in the dark at room temperature for 30 minutes to alkylate the proteins. Phosphoric acid was added to 1.2%, followed by six volumes of 90% methanol, 100 mM TEAB. The resulting solution was added to S-Trap micros (Protifi) and centrifuged at 4,000 x g for 1 minute. The S-Traps containing trapped protein were washed twice by centrifuging through 90% methanol, 100 mM TEAB. 1 µg of trypsin was brought up in 20 µL of 100 mM TEAB and added to the S-Trap, followed by an additional 20 µL of TEAB to ensure the sample did not dry out. Samples were incubated at 37°C overnight. The next morning, the S-Trap was centrifuged at 4,000 x g for 1 minute to collect the digested peptides. Sequential additions of 0.1% TFA in acetonitrile and 0.1% TFA in 50% acetonitrile were added to the S-trap, centrifuged, and pooled. Samples were frozen and dried down in a Speed Vac (Labconco), then re-suspended in 0.1% trifluoroacetic acid prior to mass spectrometry analysis. Peptides were injected onto a homemade 30 cm C18 column with 1.8 m beads (Sepax), with an Easy nLC-1200 HPLC (Thermo Fisher), connected to a Fusion Lumos Tribrid mass spectrometer (Thermo Fisher). Solvent A was 0.1% formic acid in water, while solvent B was 0.1% formic acid in 80% acetonitrile. Ions were introduced to the mass spectrometer using a Nanospray Flex source operating at 2 kV. The gradient began at 3% B and held for 2 minutes, increased to 10% B over 5 minutes, increased to 38% B over 68 minutes, then ramped up to 90% B over 3 minutes and was held for 3 minutes, before returning to starting conditions over 2 minutes and re-equilibrating for 7 minutes, for a total run time of 90 minutes.  The Fusion Lumos was operated in data-dependent mode, with MS1 and MS2 scans acquired in the Orbitrap. The cycle time was set to 2 seconds. Monoisotopic Precursor Selection (MIPS) was set to ‘Peptide’. The full scan was performed over a range of 375-1400 m/z, with a resolution of 120,000 at m/z of 200, an AGC target of 4e5, and a maximum injection time of 50 ms. Peptides with a charge state between 2-5 were picked for fragmentation, with minimum and maximum intensity thresholds set to 1e5 and 1e20, respectively. Precursor ions were fragmented by higher energy collision dissociation (HCD) using a collision energy of 30% with an isolation width of 1.1 m/z. The fragment scan was performed with a resolution of 15,000 at m/z of 200, an AGC target of 5e4, and a maximum injection time of 25 ms. Dynamic exclusion was set to 20 seconds with a mass tolerance of 10 ppm."],"repository":["Pride"],"quantification_method":[""],"modification":[""],"data_protocol":["Raw data were searched using the SEQUEST search engine within the Proteome Discoverer software platform, version 2.4 (Thermo Fisher), using the SwissProt human and HCMV databases.  Trypsin was selected as the enzyme, allowing up to 2 missed cleavages, with an MS1 mass tolerance of 10 ppm, and an MS2 mass tolerance of 0.6 Da. Carbamidomethyl was set as a fixed modification, while oxidation of methionine and proline was set as variable modifications.  The Minora node was used to determine relative protein abundance between samples using the default settings. Percolator was used as the FDR calculator, filtering out peptides that had a q-value greater than 0.01."],"omics_type":["Proteomics"],"labhead":["Joshua Munger"],"instrument_platform":[""],"submission_type":["PARTIAL"],"labhead_affiliation":["Biochemistry and Molecular Biology, Munger Lab, University of Rochester, USA"],"species":["Homo Sapiens (human)"],"publication":["42060462 Simpson LA, Dunn DM, Fales W, Moore ZJ, Ciesla JH, Waild NC, Raymonda MH, Harris IS, Munger J. HCMV infection depends on EGLN1-mediated mitochondrial activation to increase dNTP pools for viral DNA replication. Cell Rep. 2026 45(5):117329 10.1016/j.celrep.2026.117329"],"submitter_mail":["lucas_simpson@urmc.rochester.edu"],"submitter_affiliation":["University of Rochester"],"submitter_country":["United States"],"pubmed_abstract":["Human cytomegalovirus (HCMV) is a leading cause of congenital infection and morbidity in immunosuppressed populations. Like all viruses, HCMV is an obligate intracellular parasite that extensively remodels host cell metabolism to support its replication, yet the precise underlying mechanisms and the potentially associated metabolic vulnerabilities remain poorly understood. Using a metabolism-focused screening platform, we identify EGLN prolyl hydroxylase activity as critical for HCMV infection. Our studies reveal that HCMV infection depends on EGLN1, which accumulates in mitochondria during infection. Inhibition of EGLN1 expression blocks HCMV-mediated mitochondrial activation, which in turn prevents the production of the deoxynucleoside triphosphate (dNTP) precursors necessary for dNTP pool expansion and viral DNA replication. Further, pharmacological EGLN inhibition attenuates viral infection in a humanized mouse model. Collectively, these data establish EGLN1 as a critical determinant of mitochondrial metabolic remodeling and virally-induced dNTP generation during HCMV infection, highlighting EGLN1 as a promising antiviral therapeutic target."],"pubmed_title":["HCMV infection depends on EGLN1-mediated mitochondrial activation to increase dNTP pools for viral DNA replication."],"pubmed_authors":["Simpson Lucas A LA, Dunn Diana M DM, Fales Wyatt W, Moore Zachary J ZJ, Ciesla Jessica H JH, Waild Nicole C NC, Raymonda Matthew H MH, Harris Isaac S IS, Munger Joshua J"],"additional_accession":[]},"is_claimable":false,"name":"HCMV infection depends on EGLN1-mediated mitochondrial activation to increase dNTP pools for viral DNA replication","description":"Human cytomegalovirus (HCMV) is a leading cause of congenital infection and morbidity in immunosuppressed populations. Like all viruses, HCMV is an obligate intracellular parasite that extensively remodels host cellular metabolism to support its replication, yet the precise underlying mechanisms and metabolic vulnerabilities remain poorly understood. Using a novel metabolism-focused screening platform, we identified EGLN prolyl hydroxylase activity as critical for HCMV infection. Our studies revealed that HCMV infection depends on EGLN1, which accumulated in mitochondria during infection. Inhibition of EGLN1 expression blocked HCMV-mediated mitochondrial activation, which in turn prevented the production of the dNTP precursors necessary for dNTP pool expansion and viral DNA replication. Further, pharmacological EGLN inhibition attenuated viral infection in a humanized mouse model. Collectively, these data establish EGLN1 as a critical determinant of mitochondrial metabolic remodeling and virally-induced dNTP generation during HCMV infection, highlighting EGLN1 as a promising novel antiviral therapeutic target.","dates":{"publication":"2026-06-01","submission":"2026-02-04"},"accession":"PXD074057","cross_references":{"TAXONOMY":["NEWT:108018","NEWT:377960","NEWT:1131","NEWT:2042546","NEWT:295546","NEWT:258594","NEWT:1126","NEWT:1129","NEWT:309807","NEWT:89184","NEWT:309800","NEWT:1323429","NEWT:876138","NEWT:44271","NEWT:193516","NEWT:2315688","NEWT:592321","NEWT:1073882","NEWT:6819","NEWT:428386","NEWT:1117","NEWT:498257","NEWT:10036","NEWT:32264","NEWT:10034","NEWT:661410","NEWT:224326","NEWT:376619","NEWT:3765","NEWT:3767","NEWT:135622","NEWT:672127","NEWT:656061","NEWT:37965","NEWT:656064","NEWT:3760","NEWT:36630","NEWT:381198","NEWT:418106","NEWT:10029","NEWT:913645","NEWT:2492962","NEWT:641809","NEWT:44250","NEWT:317447","NEWT:5530","NEWT:868565","NEWT:135674","NEWT:1562698","NEWT:12637","NEWT:2164133","NEWT:2767846","NEWT:314344","NEWT:108061","NEWT:224308","NEWT:49928","NEWT:160621","NEWT:110368","NEWT:1916073","NEWT:1310161","NEWT:1230383","NEWT:77133","NEWT:1310165","NEWT:5516","NEWT:498211","NEWT:347256","NEWT:5518","NEWT:398007","NEWT:1527468","NEWT:498217","NEWT:498216","NEWT:11320","NEWT:1310173","NEWT:37919","NEWT:161934","NEWT:156587","NEWT:1148","NEWT:5508","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:3715","NEWT:2065263","NEWT:1549675","NEWT:177437","NEWT:9014","NEWT:10891","NEWT:1616117","NEWT:34865","NEWT:28174","NEWT:284812","NEWT:3702","NEWT:1245466","NEWT:3704","NEWT:1246791","NEWT:9005","NEWT:34871","NEWT:9006","NEWT:33548","NEWT:1883426","NEWT:10886","NEWT:3708","NEWT:536231","NEWT:219813","NEWT:215451","NEWT:460519","NEWT:272844","NEWT:1348799","NEWT:55784","NEWT:485","NEWT:2709072","NEWT:2499525","NEWT:2853422","NEWT:487","NEWT:1679718","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:987059","NEWT:491","NEWT:460523","NEWT:85694","NEWT:85692","NEWT:3750","NEWT:291146","NEWT:29466","NEWT:3745","NEWT:1715989","NCBITaxon:4751","NEWT:3747","NEWT:278161","NEWT:415978","NEWT:410289","NEWT:191701","NEWT:9054","NEWT:472","NEWT:29459","NEWT:1380096","NEWT:28128","NEWT:470","NEWT:41122","NEWT:1328300","NEWT:748693","NCBITaxon:50557","NEWT:29491","NEWT:911022","NEWT:446","NEWT:153481","NEWT:445","NEWT:63366","NEWT:63367","NEWT:29488","NEWT:215402","NEWT:3726","NEWT:30455","NEWT:28141","NEWT:9031","NEWT:3728","NEWT:108931","NEWT:219799","NEWT:219798","NEWT:548","NEWT:150475","NEWT:256737","NEWT:51350","NEWT:8694","NEWT:8692","NEWT:542","NEWT:394503","NEWT:13076","NEWT:219785","NEWT:8673","NEWT:550","NEWT:10804","NEWT:554","NEWT:451516","NEWT:552","NEWT:1325291","NEWT:42410","NEWT:1225786","NEWT:771870","NEWT:51338","NEWT:9995","NEWT:28112","NEWT:49012","NEWT:28110","NEWT:10832","NEWT:507601","NEWT:520","NEWT:64657","NEWT:186441","NEWT:643680","NEWT:214092","NEWT:40697","NEWT:13095","NEWT:162425","NEWT:242124","NEWT:9986","NEWT:8654","NEWT:8658","NEWT:1268063","NEWT:8657","NEWT:9983","NEWT:8655","NEWT:595495","NEWT:80833","NEWT:479096","NEWT:28108","NEWT:28104","NEWT:1114957","NEWT:568703","NEWT:568708","NEWT:52641","NEWT:353152","NEWT:353153","NEWT:227377","NEWT:1774284","NEWT:27689","NEWT:207769","NEWT:40674","NEWT:51329","NCBITaxon:1763","NEWT:443906","NEWT:13037","NEWT:519","NEWT:7394","NEWT:6063","NEWT:404330","NEWT:1328388","NEWT:300641","NEWT:39655","NEWT:38323","NEWT:206411","NEWT:214053","NEWT:80863","NEWT:665890","NEWT:52639","NEWT:52638","NEWT:8697","NEWT:861109","NEWT:8695","NEWT:1196866","NEWT:510516","NEWT:1045775","NEWT:1123869","NCBITaxon:1335626","NEWT:7370","NEWT:83906","NEWT:99488","NEWT:1134506","NEWT:255470","NEWT:27697","NEWT:86185","NEWT:9935","NEWT:287889","NEWT:1028307","NEWT:52603","NEWT:92867","NEWT:92866","NEWT:1344414","NEWT:202950","NEWT:741158","NEWT:1293091","NEWT:202956","NEWT:315750","NEWT:632957","NEWT:9925","NCBITaxon:9606","NEWT:1436183","NEWT:4232","NEWT:9922","NEWT:416348","NEWT:11298","NEWT:4236","NEWT:398031","NEWT:196627","NEWT:523840","NEWT:1076878","NEWT:200308","NEWT:200302","NEWT:9913","NEWT:9915","NEWT:105841","NEWT:2666255","NEWT:999810","NEWT:28995","NEWT:1392998","NEWT:1150621","NEWT:1085791","NEWT:745531","NEWT:226900","NEWT:231490","NEWT:590651","NEWT:449239","NEWT:244704","NEWT:9909","NEWT:9902","NEWT:430615","NEWT:563041","NEWT:36599","NEWT:41949","NEWT:326423","NEWT:326424","NEWT:13013","NEWT:749906","NEWT:418985","NEWT:749907","NEWT:431947","NEWT:142809","NEWT:1095183","NEWT:302409","NEWT:130821","NEWT:2320211","NEWT:27606","NEWT:290610","NEWT:1519788","NEWT:59202","NEWT:9975","NEWT:8643","NEWT:1801631","NEWT:1159899","NEWT:502780","NEWT:860688","NEWT:35231","NEWT:1774208","NEWT:8644","NEWT:1125630","NEWT:28930","NEWT:202914","NEWT:27602","NEWT:502779","NEWT:297246","NEWT:483139","NEWT:101491","NEWT:8639","NEWT:8637","NEWT:1114970","NEWT:285272","NEWT:1922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