{"database":"Pride","file_versions":[{"headers":{"Content-Type":["application/json"]},"body":{"files":{"Xlsx":["ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/07/PXD079401/Peptide_110_119_SCfab_Bimodal_Quantitation_V39.xlsx","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/07/PXD079401/Peptide_110_119_LCfab_Bimodal_Quantitation_V39.xlsx","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/07/PXD079401/Peptide_110_119_Apo_Bimodal_Quantitation_V39.xlsx","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/07/PXD079401/Peptide_110_135_VLP_BimodalDecon.xlsx","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/07/PXD079401/Peptide_110_119_C1P_Bimodal_Quantitation_V39.xlsx"],"Txt":["ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/07/PXD079401/checksum.txt"],"Csv":["ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/07/PXD079401/240530_Mprot_Und_0sec_01_IA_final_peptide.csv","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/07/PXD079401/130624_Omicron_VLP_Und_2_IA_final_peptide.csv","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/07/PXD079401/100124_D614G_VLP_Und_1_IA_final_peptide.csv","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/07/PXD079401/110124_D614G_VLP_Und_2_IA_final_peptide.csv","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/07/PXD079401/100124_D614G_VLP_Und_2_IA_final_peptide.csv","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/07/PXD079401/130624_Omicron_VLP_Und_1_IA_final_peptide.csv","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/07/PXD079401/110124_D614G_VLP_Und_1_IA_final_peptide.csv","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/07/PXD079401/130624_Omicron_VLP_Und_3_IA_final_peptide.csv","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/07/PXD079401/240520_MProteinscFab_neppep_0sec_02_IA_final_peptide.csv","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/07/PXD079401/240530_Mprot_Und_0sec_02_IA_final_peptide.csv"],"Other":["ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/07/PXD079401/M_apo.zip","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/07/PXD079401/250119_VLP_Mprot_D614G.DnX","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/07/PXD079401/M_C1P.zip","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/07/PXD079401/M_apo_VLPbuffer.zip","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/07/PXD079401/250119_MDimer_VLPBuffer_SMB.DnX","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/07/PXD079401/250119_MDimer_Apo_scFab_lcFab_C1P_SMB.DnX","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/07/PXD079401/M_scFab.zip","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/07/PXD079401/SolubleM_Undeuterated.zip","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/07/PXD079401/VLPembedded_M.zip","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/07/PXD079401/M_lcFab.zip"]},"type":"primary"},"statusCode":"OK","statusCodeValue":200}],"scores":null,"additional":{"labhead_mail":["gsa5089@psu.edu"],"submitter":["Sean Braet"],"technology_type":["Mass Spectrometry","Bottom-up proteomics"],"software":["Not available"],"submitter_keywords":["Sars-cov-2","Lipid interaction","Hdxms"],"full_dataset_link":["https://www.ebi.ac.uk/pride/archive/projects/PXD079401"],"sample_protocol":["Labeling buffer was prepared by diluting 10x HEPES buffer in D2O (99.9%) (1x buffer: 20 mM HEPES, 150 mM KCl, 1 mM EDTA, pH 8.0). Deuterium labelling was carried out for M protein in detergent as well as M protein mixed with scFab, lcFab, and C1P for 1, 10, and 100 min labelling at 20°C using a PAL-RTC (Leap) autosampler. M protein was mixed with scFab or lcFab in a 1:1 ratio for a final concentration of 15 μM M dimer for 60 minutes on ice prior to labelling. M protein (15 μM dimer) was mixed with excess (100 μM) C1P for 30 min on ice prior to labelling. 3 μL of M protein or M protein complex were mixed with 57 μL of labelling buffer for a final D2O concentration of 85.4%. After labeling, an equivalent volume of prechilled quench solution (1.5 M guanidine hydrochloride, 0.25 M TCEP, 2.4 mM DDM) were added to the labelling reaction to bring the pH to 2.5.    Deuterium labelling was also carried out on M protein embedded in VLPs. Labelling buffer was prepared by diluting 20x TNE (20 mM Tris, 100 mM NaCl, 1 mM EDTA) buffer in D2O (99.9%). 20 μL of VLP sample was mixed with 40 μL of labelling buffer prior to quenching. After labelling, 3 volumes of labelling reaction were mixed with 1 volume of prechilled quench solution (4 M guanidine hydrochloride, 0.4 M TCEP, 2.4 mM DDM). For comparison, apo M protein in detergent was also labelled after diluting 3 μL of sample (15 μM dimer) with 17 uL of 1x TNE buffer prior to mixing with 40 uL of labelling buffer to match the final D2O concentration of 63.3% in labelled VLPs.   Undeuterated reference samples for VLPs and M protein were prepared by mixing equivalent sample with 1x buffer in H2O prior to quenching. All reference states and labelling timepoints were collected in triplicate.    Approximately 15-20 pmol of soluble M were digested online using a nepenthesin-2/pepsin mixed bed column (2.1 x 20 mm) (Affipro, AP-PC-006) at 15 °C. Peptides were trapped for 3 min in a C18 trap column (ACQUITY BEH C18 VanGuard Pre-column, 1.7 µM, Waters, Milford, MA) at a flow rate of 100 μL/min. Peptides were subsequently eluted in an acetonitrile gradient (5-35%) over 7 minutes in 0.1% formic acid on a reverse phase C18 column (AQUITY UPLC BEH C18 Column, Waters, Milford, MA) at 40 μL/min. All fluidics were controlled by nanoACQUITY Binary Solvent Manager (Waters, Milford, MA). Electrospray ionization mode was utilized, and ionized peptides were sprayed onto an SYNAPT XS mass spectrometer (Waters, Milford, MA) acquired in HDMSE Mode. Spectra were recorded over a range of 50-2000 m/z with the following settings: capillary voltage: 2.8 kV; trap collision energy: 6 V; sampling cone: 30 V; transfer CE ramp 20-45 V; source temperature: 80 °C; and desolvation temperature: 175 °C. Ion mobility settings of 600 m/s wave velocity and 197 m/s, transfer wave velocity were used with collision energies of 4 and 2 V for trap and transfer, respectively. 100 fmol/μL of [Glu1]-fibrinopeptide B ([Glu1]-Fib) with a flow rate of 5 µL/min was used to inject as lockspray reference mass. VLP samples containing M, E, N, and S proteins were digested online at 15 °C using an AffiPro pepsin column (AffiPro, AP-PC-001). All chromatographic components were housed in the UPLC system's cooling chamber, maintained at 0.0 ± 0.1 °C throughout the measurements. Peptides were trapped and desalted on a VanGuard Pre-Column trap (2.1 mm × 5 mm, ACQUITY UPLC BEH C18, 1.7 μm (Waters, Milford, MA)) for 3 minutes at a flow rate of 100 μL/min. Elution was achieved using a 5%–35% acetonitrile gradient over 10 minutes at 100 μL/min, with separation on an ACQUITY UPLC HSS T3 column (1.8 μm, 1.0 mm × 50 mm (Waters, Milford, MA)). The system operated at an average back pressure of ~12,950 psi under initial conditions (5% acetonitrile, 95% water, 0.1% formic acid) at 0 °C. Deuterium level determination had an error margin of ± 0.25 Da in this experimental setup. To avoid peptide carryover, a wash solution (1.5 M guanidinium chloride, 0.8% formic acid, and 4% acetonitrile) was injected over the pepsin column after each analytical run.  Mass spectra were acquired on a Waters SELECT SERIES Cyclic IMS instrument coupled with a UPLC I-Class system and HDX manager. Spectra were recorded over an m/z range of 50–2000 with the following settings: capillary voltage, 3.0 kV; trap collision energy, 4 V; sampling cone, 40 V; transfer CE ramp, 15–50 V; source temperature, 80 °C; and desolvation temperature, 450 °C. Ion mobility separation was performed with a single pass using a sequence of 10 ms injection, 3 ms separation, and 34 ms ejection/acquisition. For post-acquisition mass accuracy correction, ([Glu1]-Fib (Sigma, Burlington, MA) was infused at 250 fmol/μL at 5 μL/min as a lock mass."],"repository":["Pride"],"quantification_method":["Not available"],"modification":[""],"data_protocol":["Peptides corresponding to M protein were identified from mass spectra corresponding to undeuterated controls through searches against an M protein database using PROTEIN LYNX GLOBAL SERVER (PLGS) version 3.0 (Waters, Milford, MA) software in HDMSE mode for non-specific protease cleavage. PLGS search parameters were changed to include no fixed or variable modifier reagents and no N-linked glycosylation.   Deuterium exchange was quantitated using DynamX v3.0 (Waters, Milford, MA) with cutoff filters of: minimum intensity = 1500; minimum peptide length = 4; maximum peptide length = 30; minimum products per amino acid = 0.11; minimum consecutive products = 1; and precursor ion error tolerance <10 ppm. Only peptides that fulfilled the above-described criteria in 2 of the 3 undeuterated samples were included in the final peptide list.  To analyze cyclic IMS data, PLGS and DynamX were modified as described by Griffiths et al.  Peptides were manually analyzed for quality across technical replicates using DynamX v3.0 (Waters, Milford, MA). The average number of deuterons exchanged in each peptide was calculated by subtracting the centroid mass of the undeuterated reference spectra from each deuterated spectrum. Mass spectral envelopes were acquired from DynamX v3.0 and plotted in MATLAB 2023b, (The MathWorks Inc, Natick, MA, USA). Spectra showing bimodal hydrogen deuterium exchange kinetics were quantitated using HX-express3 v39 92 with iterative fitting applied93."],"omics_type":["Proteomics"],"labhead":["Dr. Ganesh S. Anand"],"instrument_platform":[""],"submission_type":["PARTIAL"],"labhead_affiliation":["Pennsylvania State University, Department of Chemistry"],"species":["Homo Sapiens (human)","Severe Acute Respiratory Syndrome Coronavirus 2"],"submitter_mail":["smb6745@psu.edu"],"publication":["Not available"],"submitter_affiliation":["Penn State"],"submitter_country":["United States"],"additional_accession":[]},"is_claimable":false,"name":"Direct lipid interactions control SARS-CoV-2 M protein conformational dynamics and virus assembly","description":"M is the most abundant structural membrane protein in coronaviruses and is essential for the formation of infectious virus particles. SARS-CoV-2 M adopts two conformations, Mshort and Mlong, and regulated transition between states is hypothesized to coordinate viral assembly and budding. However, the factors that regulate M conformation and roles for each state are unknown. Here, we discover a direct M-sphingolipid interaction that controls M conformational dynamics, interaction with other structural proteins, and virus assembly. We show M binds Golgi-enriched anionic lipids including ceramide-1-phosphate (C1P). Molecular dynamics simulations show C1P interaction promotes a long to short transition and energetically stabilizes Mshort. Cryo-EM structures show C1P specifically binds Mshort at a conserved site bridging transmembrane and cytoplasmic regions. Hydrogen-deuterium exchange mass spectrometry confirms that C1P binds primarily to a condensed Mshort conformation and shows a switching from Mshort to Mlong in virus-like particles.  Disrupting Mshort-C1P interaction alters M subcellular localization, reduces colocalization with Spike and E, and reduces virus-like particle formation and cell entry. Together, these results show endogenous signaling lipids regulate M structure and support a model in which Mshort is stabilized in the early endomembrane system to organize other structural proteins prior to viral budding.","dates":{"publication":"2026-07-09","submission":"2026-06-08"},"accession":"PXD079401","cross_references":{"TAXONOMY":["NEWT:330879","NEWT:377960","NEWT:1131","NEWT:2042546","NEWT:259447","NEWT:295546","NCBITaxon:2719036","NEWT:1334565","NEWT:625351","NEWT:258594","NCBITaxon:1280","NEWT:112503","NEWT:1129","NEWT:309807","NEWT:59753","NEWT:89184","NEWT:309800","NEWT:281395","NEWT:1211601","NEWT:876138","NEWT:44271","NEWT:193516","NEWT:1073882","NEWT:6819","NEWT:475174","NEWT:111205","NEWT:1117","NEWT:498257","NEWT:10036","NEWT:1590","NEWT:10034","NEWT:33114","NEWT:661410","NEWT:638632","NEWT:224326","NEWT:376619","NCBITaxon:79857","NEWT:1096976","NEWT:3765","NEWT:3767","NEWT:1589","NEWT:135622","NEWT:35786","NEWT:1580","NEWT:399784","NEWT:96731","NEWT:656064","NEWT:1582","NEWT:1584","NEWT:36630","NEWT:383379","NEWT:418106","NCBITaxon:12721","NEWT:10029","NEWT:913645","NEWT:2492962","NEWT:641809","NEWT:1392488","NEWT:38815","NEWT:317447","NEWT:4688","NEWT:111225","NEWT:7719","NEWT:868565","NEWT:135674","NEWT:79329","NEWT:30069","NEWT:12637","NEWT:59729","NEWT:2164133","NEWT:295105","NEWT:108061","NEWT:60711","NEWT:224308","NEWT:3347","NEWT:160621","NEWT:212790","NEWT:110368","NEWT:55350","NEWT:1310161","NEWT:77133","NEWT:145481","NEWT:1310165","NEWT:29058","NCBITaxon:79824","NEWT:1912919","NEWT:410658","NEWT:5516","NEWT:44688","NEWT:44689","NEWT:498211","NEWT:347256","NEWT:5518","NEWT:398007","NEWT:1527468","NEWT:498217","NEWT:498216","NEWT:11320","NEWT:246196","NEWT:246197","NEWT:145458","NEWT:1310173","NEWT:44685","NEWT:161934","NEWT:156587","NEWT:1148","NEWT:5508","NEWT:3329","NEWT:419481","NEWT:5507","NEWT:410661","NEWT:1140","NCBITaxon:2157","NEWT:1143","NEWT:1287689","NEWT:1094343","NEWT:1462472","NEWT:1336795","NEWT:644042","NEWT:150808","NEWT:1182590","NEWT:3712","NEWT:3711","NEWT:3714","NCBITaxon:37162","NEWT:270643","NEWT:2065263","NEWT:177437","NEWT:10418","NEWT:118698","NEWT:1616117","NEWT:118696","NEWT:34865","NEWT:52283","NEWT:28174","NEWT:284812","NEWT:8175","NEWT:43330","NEWT:1603293","NEWT:44664","NEWT:43346","NEWT:3702","NEWT:1245466","NEWT:3704","NEWT:244366","NEWT:1246791","NEWT:176597","NEWT:118694","NEWT:2850","NEWT:118691","NEWT:34871","NEWT:33548","NEWT:52299","NEWT:8165","NEWT:96794","NEWT:3708","NEWT:332648","NEWT:44670","NEWT:926571","NEWT:536231","NEWT:376219","NEWT:219813","NEWT:1510","NEWT:460519","NEWT:1515","NEWT:572307","NEWT:1432138","NEWT:1424507","NEWT:1194599","NEWT:272844","NEWT:1348799","NEWT:33995","NEWT:55784","NEWT:1303443","NEWT:9483","NEWT:485","NEWT:56636","NEWT:2709072","NEWT:2499525","NEWT:2853422","NEWT:487","NEWT:1538553","NEWT:1679718","NEWT:480","NEWT:67767","NEWT:46835","NEWT:109757","NEWT:582580","NEWT:1185650","NEWT:216778","NEWT:294607","NEWT:1502","NEWT:128017","NEWT:376686","NEWT:237610","NEWT:95486","NEWT:1883446","NEWT:1233435","NEWT:118223","NEWT:11757","NEWT:987059","NEWT:109760","NEWT:29031","NEWT:317047","NEWT:491","NEWT:460523","NEWT:45954","NEWT:235443","NEWT:1757312","NEWT:85694","NEWT:109786","NEWT:108458","NEWT:5936","NEWT:320637","NEWT:1078283","NEWT:3750","NEWT:983964","NEWT:11706","NEWT:32644","NEWT:527796","NEWT:499175","NEWT:109779","NEWT:3745","NEWT:1715989","NCBITaxon:4751","NEWT:3747","NEWT:1116234","NEWT:1255228","NEWT:410289","NEWT:373153","NEWT:1640278","NEWT:472","NEWT:940825","NEWT:529507","NEWT:1071661","NEWT:28128","NEWT:470","NEWT:5911","NEWT:748693","NCBITaxon:50557","NEWT:39251","NEWT:29491","NEWT:101841","NEWT:446","NEWT:153481","NEWT:2014887","NEWT:33952","NEWT:445","NEWT:153009","NEWT:261756","NEWT:166313","NEWT:63366","NEWT:63367","NEWT:215402","NEWT:1547","NEWT:1290454","NEWT:906914","NEWT:28141","NEWT:9031","NEWT:27292","NEWT:1050722","NEWT:3728","NEWT:108931","NEWT:1293497","NEWT:1055524","NEWT:150475","NEWT:267872","NEWT:381666","NEWT:172269","NEWT:9534","NEWT:5180","NEWT:256737","NEWT:9541","NEWT:8694","NEWT:33936","NEWT:8692","NEWT:2903","NEWT:185579","NEWT:13076","NEWT:207340","NEWT:1006581","NEWT:8673","NEWT:33940","NEWT:550","NEWT:554","NEWT:451516","NEWT:552","NEWT:1325291","NEWT:42410","NEWT:36185","NEWT:1054211","NEWT:1225786","NEWT:771870","NEWT:51338","NEWT:575412","NEWT:28112","NEWT:49012","NEWT:6493","NEWT:10832","NEWT:6494","NEWT:6491","NEWT:507601","NEWT:520","NEWT:186441","NEWT:643680","NEWT:214092","NCBITaxon:6157","NEWT:13095","NEWT:162425","NEWT:104105","NEWT:216257","NEWT:9986","NEWT:8654","NEWT:8658","NEWT:1268063","NEWT:8657","NEWT:9983","NEWT:8655","NEWT:5147","NEWT:595495","NEWT:28108","NEWT:28104","NEWT:407821","NEWT:568703","NCBITaxon:2","NEWT:568708","NEWT:1613","NEWT:986","NEWT:52641","NEWT:28532","NEWT:353152","NEWT:298176","NEWT:353153","NEWT:227377","NEWT:1774284","NEWT:40674","NEWT:1194669","NEWT:51329","NEWT:443906","NEWT:13037","NEWT:519","NEWT:2510939","NEWT:7394","NEWT:6063","NEWT:1328388","NEWT:105487","NEWT:1548728","NEWT:667127","NEWT:9557","NEWT:377586","NEWT:300641","NEWT:39655","NEWT:9554","NEWT:38323","NEWT:475932","NEWT:256318","NEWT:206411","NCBITaxon:6191","NEWT: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