Prideapplication/xmlftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/05/PXD077483/ppmfixerOutput_alphalytic.txtftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/05/PXD077483/checksum.txtftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/05/PXD077483/ppmfixerOutput_trypgluc.txtftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/05/PXD077483/Ag85b_alphalytic.rawftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/05/PXD077483/Ag85b_trypgluc.rawprimaryOK200favci@emory.eduTrevor AdamsData-dependent acquisitionGlycoproteomicsMass SpectrometryBottom-up proteomicsNot availableGlycoproteomicsMtbAg85bhttps://www.ebi.ac.uk/pride/archive/projects/PXD077483Cell Suspension CultureEarly Embryonic CellAg85B was transiently transfected and expressed in Expi293 cells and secreted into the supernatant. Supernatant was harvested and protein was purified with Ni-NTA affinity chromatography followed by size exclusion chromatography. Intact glycopeptides were generated utilizing purified Ag85B. Fifty microgram of purified glycoprotein was reduced for 1 h at 56 °C in 10 mM DTT. Ag85B cysteines were alkylated using 25 mM iodoacetamide in the dark at room temperature for 45 min. Alkylation was quenched with an additional 10 mM DTT. Glycoprotein was then digested with one of two separate protease conditions: (1) α-lytic protease (NEB, Part #: P8113S) or (2) trypsin/LysC mix (Promega, Part #: V5071) followed by GluC (Promega, Part #: V1651). All protease digestions were carried out at 37 °C overnight (∼16–18 h) at a 1:20 μg:μg protease:protein ratio (e.g., protease condition 2 required two overnight digests). After each digest, the protease was heat-inactivated at 95 °C for 5 min.Glycopeptides were desalted via reverse-phase cleanup using a BioPureSPN MINI C18 column (The Nest Group, Part #: HUM S18V). Desalted peptides were dried down with a vacuum centrifuge and then resuspended in a solution of 95.9% water, 4% acetonitrile, and 0.1% formic acid. Resuspended peptides were filtered through a conditioned 0.2 μm filter (PALL, Cat. #: ODM02C34) before transferring to autosampler vials. For intact glycopeptide analysis, 1 μg of Ag85B glycopeptides was injected onto a 75μmx15cm Acclaim PepMap 100 C18 nanoViper column (Thermo Fisher Scientific, Part #: 164,940) and eluted into the nanospray source of an Orbitrap Eclipse Tribrid mass spectrometer with a field asymmetric ion mobility spectrometry frontend interface (Thermo Fisher Scientific). Glycopeptides were separated with a two-buffer LC gradient using water with 0.1% formic acid as buffer A and 80% acetonitrile with 0.1% formic acid as buffer B utilizing a Vanquish liquid chromatography system (Thermo Fisher Scientific) with a flow rate of 0.4 μl/min. The 90-min buffer gradient proceeded: 0 to 6 min 2.5% B, 6 to 76 min 2.5 to 32.5% B, 76 to 88 min 32.5% to 100% B, followed by a 1 min column wash with 100% B at 1 μl/min. The spray voltage was set to 2.35 kV, and the ion transfer tube was heated to 305 °C. Field asymmetric ion mobility spectrometry compensation voltages were set to cycle through −35 V, −40 V, and −50 V. Full MS scans were acquired from m/z 200 to 2000 at 60,000 resolution in the Orbitrap. MS/MS scans were triggered with an intensity threshold of 2 × 104 and a mass tolerance of 20 ppm. MS/MS scans were acquired at a resolution of 15,000 in the Orbitrap via stepped higher collisional dissociation, with HCD collision energies of 15%, 25%, and 35% and an isolation window of 1.6 m/z.PrideNot availableFor intact glycopeptide analysis, the resulting RAW files were searched for glycopeptide spectral matches (GPSMs) using the search engine pGlyco3 (79). RAW files were searched against a FASTA database containing Ag85B and common contaminants and a custom glycan database derived from released glycan compositions identified in glycomics experiments (see above). Search was conducted with a precursor tolerance of 10 ppm, fragment tolerance of 20 ppm, and glycopeptide FDR set to 0.01. Resulting GPSMs were manually inspected to ensure accuracy. GPSMs were processed by the ppmFixer script (80) to adjust for common errors due to monoisotopic peak misidentification, and site-specific glycan compositions were relatively quantified using spectral counts (81).ProteomicsFikri AvciPARTIALEmory University, Department of BiochemistryHomo Sapiens (human)41935836 Cinar MS, Adams TM, Nawaz Z, Demir ES, Demirturk ME, Keelaghan AP, Nazaar SM, Roberts BR, Ozdilek A, Avci FY. Molecular mechanisms of immune evasion by host protein glycosylation of a bacterial immunogen used in nucleic acid vaccines. J Biol Chem. 2026:111423 10.1016/j.jbc.2026.111423trevor.adams@emory.eduEmory UniversityUnited StatesNucleic acid vaccines (DNA and mRNA) induce immunity by driving in situ antigen expression in host cells. For nonviral pathogens, however, host expression can impose post-translational modifications absent from the native microbial antigen. Tuberculosis remains a leading cause of infectious mortality, and nucleic acid vaccines targeting the Mycobacterium tuberculosis antigen 85 (Ag85) complex did not confer protective efficacy in clinical trials. We hypothesized that host-derived N-glycosylation of Ag85 immunogens expressed in mammalian cells compromises immune recognition. Here, we define structural, biochemical, and immunological mechanisms by which host-imposed N-glycosylation remodels a bacterial antigen expressed in mammalian cells. We show that Ag85B expressed in human Expi293 cells is microheterogeneously N-glycosylated at four canonical sequons (N52, N224, N234, and N280) with predominantly complex, highly fucosylated, and frequently sialylated glycans. Molecular dynamics simulations indicate that these glycans occupy substantial conformational space and reduce solvent and antibody-accessible surface area, occluding multiple established B-cell and T-cell epitope regions. Consistent with glycan-mediated shielding, mammalian-expressed Ag85B shows markedly reduced binding to an Ag85-complex monoclonal antibody by competitive ELISA and biolayer interferometry, and sialylated glycans enable Siglec-9 binding that is abrogated by sialidase treatment. Together, these findings define the structural and biochemical mechanisms by which host glycosylation can remodel bacterial vaccine antigens, supporting glycosylation-aware immunogen engineering as a design principle for nucleic acid vaccines targeting nonviral pathogens.Molecular mechanisms of immune evasion by host protein glycosylation of a bacterial immunogen used in nucleic acid vaccines.Cinar Mukaddes Sena MS, Adams Trevor M TM, Nawaz Fathima Zahra FZ, Demir Elif S ES, Erol Demirturk Mariye M, Keelaghan Aidan P AP, Nazaar Shaima M SM, Roberts Blaine R BR, Ozdilek Ahmet A, Avci Fikri Y FYfalseRecombinant Ag85B GlycoproteomicsA bacterial antigen (Ag85B) was recombinantly expressed in Expi293 cells in which non-native N-glycosylation occured. We used glycoproteomics to characterize site-specific glycosylation across the surface of Ag85B as informed by glycomics data.2026-05-252026-04-22PXD077483NEWT:3555NEWT:71647NEWT:330879NEWT:35554NEWT:32046NEWT:544496NEWT:2042546NEWT:32049NEWT:1392696NEWT:259447NEWT:295546NEWT:45351NEWT:445974NEWT:43179NEWT:180454NEWT:5722NCBITaxon:1280NEWT:1129NEWT:309807NEWT:55153NEWT:309800NEWT:281395NEWT:1211601NEWT:876138NEWT:44271NEWT:10036NEWT:1590NEWT:498019NEWT:1351NEWT:1438992NEWT:1352NEWT:2649997NEWT:1147161NEWT:638632NEWT:263737NEWT:224326NEWT:1333499NCBITaxon:79857NEWT:1096976NEWT:5702NEWT:95648NEWT:1589NEWT:135622NEWT:1349NEWT:96731NEWT:383379NEWT:10029NEWT:913645NEWT:44491NEWT:556484NEWT:317447NEWT:4688NEWT:7955NEWT:7959NEWT:2261NEWT:31156NEWT:3112NEWT:4442NEWT:192875NEWT:1214915NEWT:12637NEWT:59729NEWT:2164133NEWT:108061NEWT:1316931NEWT:224308NEWT:3347NEWT:511145NEWT:931281NEWT:4432NEWT:658457NEWT:1310161NEWT:77133NEWT:295358NEWT:145481NCBITaxon:79824NEWT:2246NCBITaxon:4563NEWT:5755NEWT:44689NEWT:44447NEWT:752555NEWT:498211NEWT:5759NEWT:1736231NEWT:5518NEWT:398007NEWT:1392NEWT:498217NEWT:498216NEWT:2242NEWT:11320NEWT:286NEWT:391619NEWT:246196NEWT:287NEWT:246197NEWT:633149NEWT:10239NEWT:44685NEWT:161934NEWT:4897NEWT:1148NEWT:5508NEWT:5507NEWT:410661NEWT:55571NEWT:35500NEWT:1140NCBITaxon:2157NEWT:1143NEWT:4896NEWT:1287689NEWT:1390NEWT:11557NEWT:1094343NEWT:1336795NEWT:644042NEWT:294NEWT:1773NEWT:1182590NEWT:3712NEWT:82380NEWT:3711NEWT:935293NEWT:375146NEWT:2065263NEWT:118698NEWT:1616117NEWT:263NEWT:118696NEWT:52283NEWT:284812NEWT:8175NEWT:43330NEWT:1603293NEWT:408169NEWT:44664NEWT:47946NEWT:3702NEWT:243277NEWT:7067NEWT:118694NEWT:2850NEWT:118691NEWT:33548NEWT:274NEWT:408172NEWT:408170NEWT:96794NEWT:3708NEWT:332648NEWT:44670NEWT:536231NEWT:376219NEWT:1436733NEWT:460519NEWT:1247411NEWT:572307NEWT:1432138NEWT:1424507NEWT:1194599NEWT:272844NEWT:9483NEWT:333760NEWT:1513458NEWT:1233681NCBITaxon:40559NEWT:506599NEWT:84588NEWT:1679718NEWT:480NEWT:67767NEWT:46835NEWT:109757NEWT:582580NEWT:300852NEWT:1502NEWT:376686NEWT:95486NEWT:508771NEWT:1883446NEWT:253NCBITaxon:2759NEWT:1233435NEWT:93061NEWT:93062NCBITaxon:4932NEWT:644223NEWT:235443NEWT:108458NEWT:272623NEWT:272624NEWT:320637NEWT:983964NEWT:118499NEWT:11706NEWT:32644NEWT:527796NEWT:499175NEWT:109779NEWT:3745NEWT:1715989NCBITaxon:4751NEWT:476272NEWT:3747NEWT:195051NEWT:3988NEWT:1255228NEWT:649908NEWT:410289NEWT:373153NEWT:3983NEWT:352472NEWT:1071661NEWT:360094NEWT:470NEWT:41364NEWT:1313NEWT:39491NCBITaxon:5811NEWT:29491NEWT:2014887NEWT:33952NEWT:261756NEWT:571256NEWT:40483NEWT:63366NEWT:63367NEWT:215402NEWT:272634NEWT:9031NEWT:1872122NEWT:7091NEWT:141262NEWT:108931NEWT:1055524NEWT:4087NEWT:9778NEWT:306NEWT:150475NEWT:303NEWT:267872NEWT:7111NEWT:347515NEWT:9534NEWT:5180NEWT:256737NEWT:4090NEWT:4092NEWT:9541NEWT:8694NEWT:4093NEWT:4096NEWT:8692NEWT:185579NEWT:941442NEWT:13076NEWT:1226408NEWT:7108NEWT:40479NEWT:43989NEWT:4076NEWT:317NEWT:1006581NEWT:885318NEWT:39488NEWT:550NEWT:4081NEWT:273068NEWT:554NEWT:98334NEWT:451516NEWT:4084NEWT:63577NEWT:36185NEWT:1225786NEWT:7574NEWT:1715256NEWT:30640NEWT:575412NEWT:929793NEWT:29204NEWT:28112NEWT:114155NEWT:6494NEWT:6491NEWT:507601NEWT:186441NEWT:643680NEWT:214092NCBITaxon:6157NEWT:6239NEWT:162425NEWT:216257NEWT:102169NEWT:9986NEWT:4054NEWT:8654NEWT:8658NEWT:1268063NEWT:8655NEWT:1263854NEWT:118503NEWT:2059687NEWT:160488NEWT:28104NEWT:207559NEWT:407821NCBITaxon:2NEWT:985076NEWT:1215323NEWT:986NEWT:52641NEWT:7159NEWT:28532NEWT:353152NEWT:8496NEWT:27448NEWT:40674NEWT:1194669NEWT:243230NEWT:1080772NEWT:519NEWT:8479NEWT:8485NEWT:6063NEWT:49240NEWT:104395NEWT:6289NEWT:6287NEWT:300641NEWT:727NEWT:9796NEWT:725NEWT:469008NEWT:256318NEWT:9321NEWT:206411NCBITaxon:6191NEWT:596153NEWT:229533NEWT:1836NEWT:214053NEWT:80863NEWT:105231NEWT:74649NEWT:52638NEWT:57075NEWT:4097NEWT:8697NEWT:8695NEWT:884204NEWT:9785NEWT:6279NEWT:1123869NEWT:9544NEWT:7370NEWT:83906NCBITaxon:780NCBITaxon:1502NEWT:6282NEWT:1134506NEWT:38783NEWT:4006NEWT:6426NCBITaxon:5476NEWT:6669NEWT:9935NEWT:89453NEWT:287889NEWT:1114301NEWT:51515NEWT:588596NEWT:51511NEWT:8845NEWT:92867NEWT:92866NEWT:5334NEWT:51750NEWT:202950NEWT:382352NEWT:413071NCBITaxon:714NEWT:295027NEWT:632957NEWT:9925NEWT:89462NCBITaxon:9606NEWT:8839NEWT:90690NEWT:1436183NEWT:4232NEWT:2758385NEWT:11298NEWT:171101NEWT:714NEWT:5322NEWT:421932NEWT:312017NEWT:196627NEWT:200308NEWT:553470NEWT:200302NEWT:870435NEWT:284593NEWT:100392NEWT:5315NEWT:9913NEWT:265872NEWT:105841NEWT:337330NEWT:2666255NEWT:2285NEWT:999810NCBITaxon:5693NEWT:1392998NEWT:380394NEWT:981087NEWT:180066NEWT:226900NEWT:231490NEWT:7725NEWT:430615NEWT:326423NEWT:452467NEWT:198822NEWT:36111NEWT:326424NEWT:1416333NEWT:35024NEWT:135461NEWT:1678078NEWT:749906NEWT:418985NEWT:1817808NEWT:749907NEWT:145263NEWT:69014NEWT:142809NEWT:694569NEWT:27606NEWT:9739NEWT:59202NEWT:9975NEWT:8643NEWT:51953NEWT:3197NEWT:860688NEWT:13443NEWT:8644NEWT:36329NEWT:62615NCBITaxon:3044782NEWT:1333550NEWT:160235NEWT:72407NEWT:8639NEWT:8637NEWT:349741NEWT:409859NEWT:157295NEWT:2096NEWT:509169NEWT:192222NEWT:9721NEWT:137221NEWT:9963NEWT:1617910NEWT:565050NEWT:409860NEWT:2785785NEWT:411901NEWT:8626NEWT:10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