2024
Glycoproteomics: Charting new territory in mass spectrometry and glycobiology
Malaker S. Glycoproteomics: Charting new territory in mass spectrometry and glycobiology. Journal Of Mass Spectrometry 2024, 59: e5034. PMID: 38726698, DOI: 10.1002/jms.5034.Peer-Reviewed Original Research
2022
Cell-specific bioorthogonal tagging of glycoproteins
Cioce A, Calle B, Rizou T, Lowery SC, Bridgeman VL, Mahoney KE, Marchesi A, Bineva-Todd G, Flynn H, Li Z, Tastan OY, Roustan C, Soro-Barrio P, Rafiee MR, Garza-Garcia A, Antonopoulos A, Wood TM, Keenan T, Both P, Huang K, Parmeggian F, Snijders AP, Skehel M, Kjær S, Fascione MA, Bertozzi CR, Haslam SM, Flitsch SL, Malaker SA, Malanchi I, Schumann B. Cell-specific bioorthogonal tagging of glycoproteins. Nature Communications 2022, 13: 6237. PMID: 36284108, PMCID: PMC9596482, DOI: 10.1038/s41467-022-33854-0.Peer-Reviewed Original ResearchConceptsMass spectrometry glycoproteomicsArtificial biosynthetic pathwayTumor-derived cell linesCellular model systemNon-transfected cellsCellular functionsProtein glycosylationBiosynthetic pathwayProteome analysisGlycosylation sitesBioorthogonal tagsCancer developmentCell linesModel systemImportant modulatorIntricate interactionsCo-culture modelGlycoproteinCellsGlycoprotein expressionMouse modelGlycoproteomeGlycosylationTaggingMonocultureMucus sialylation determines intestinal host-commensal homeostasis
Yao Y, Kim G, Shafer S, Chen Z, Kubo S, Ji Y, Luo J, Yang W, Perner SP, Kanellopoulou C, Park AY, Jiang P, Li J, Baris S, Aydiner EK, Ertem D, Mulder DJ, Warner N, Griffiths AM, Topf-Olivestone C, Kori M, Werner L, Ouahed J, Field M, Liu C, Schwarz B, Bosio CM, Ganesan S, Song J, Urlaub H, Oellerich T, Malaker SA, Zheng L, Bertozzi CR, Zhang Y, Matthews H, Montgomery W, Shih HY, Jiang J, Jones M, Baras A, Shuldiner A, Gonzaga-Jauregui C, Snapper SB, Muise AM, Shouval DS, Ozen A, Pan KT, Wu C, Lenardo MJ. Mucus sialylation determines intestinal host-commensal homeostasis. Cell 2022, 185: 1172-1188.e28. PMID: 35303419, PMCID: PMC9088855, DOI: 10.1016/j.cell.2022.02.013.Peer-Reviewed Original ResearchConceptsInflammatory bowel diseaseMicrobial pathogen-associated molecular patternsPathogen-associated molecular patternsMicrobial symbiosisRegulatory networksIntestinal mucusGlycoproteomic profilingMolecular patternsTerminal sialylationMucus proteinsProteolytic degradationBiochemical analysisBacterial invasionBowel diseaseIntestinal inflammationMucus integrityMutationsSialylationST6GALNAC1Barrier integrityGoblet cellsMucus barrierFirst lineSymbiosisCommensalism
2021
Novel Antibodies for the Simple and Efficient Enrichment of Native O-GlcNAc Modified Peptides
Burt RA, Dejanovic B, Peckham HJ, Lee KA, Li X, Ounadjela JR, Rao A, Malaker SA, Carr SA, Myers SA. Novel Antibodies for the Simple and Efficient Enrichment of Native O-GlcNAc Modified Peptides. Molecular & Cellular Proteomics 2021, 20: 100167. PMID: 34678516, PMCID: PMC8605273, DOI: 10.1016/j.mcpro.2021.100167.Peer-Reviewed Original ResearchConceptsO-GlcNAc-modified peptidesPosttranslational modificationsNumerous biological processesUbiquitin remnantsMouse brain tissue samplesGlcNAc signalingThreonine residuesLysine acetylationGlcNAc transferaseO-GlcNAcylationGlcNAc antibodiesBiological processesO-GalNAcExtended glycansN-acetylglucosamineEnrichment strategyFundamental roleDisease statesPeptidesInstrument timeModified peptidePhosphotyrosineNovel antibodyBrain tissue samplesImmunoprecipitationMucinomics as the Next Frontier of Mass Spectrometry
Rangel-Angarita V, Malaker SA. Mucinomics as the Next Frontier of Mass Spectrometry. ACS Chemical Biology 2021, 16: 1866-1883. PMID: 34319686, DOI: 10.1021/acschembio.1c00384.Peer-Reviewed Original ResearchOn-tissue spatially resolved glycoproteomics guided by N-glycan imaging reveal global dysregulation of canine glioma glycoproteomic landscape
Malaker SA, Quanico J, Raffo-Romero A, Kobeissy F, Aboulouard S, Tierny D, Bertozzi CR, Fournier I, Salzet M. On-tissue spatially resolved glycoproteomics guided by N-glycan imaging reveal global dysregulation of canine glioma glycoproteomic landscape. Cell Chemical Biology 2021, 29: 30-42.e4. PMID: 34102146, PMCID: PMC8617081, DOI: 10.1016/j.chembiol.2021.05.007.Peer-Reviewed Original ResearchSmall RNAs are modified with N-glycans and displayed on the surface of living cells
Flynn RA, Pedram K, Malaker SA, Batista PJ, Smith BAH, Johnson AG, George BM, Majzoub K, Villalta PW, Carette JE, Bertozzi CR. Small RNAs are modified with N-glycans and displayed on the surface of living cells. Cell 2021, 184: 3109-3124.e22. PMID: 34004145, PMCID: PMC9097497, DOI: 10.1016/j.cell.2021.04.023.Peer-Reviewed Original ResearchConceptsLiving cellsGlycan biosynthetic machineryDomains of lifeMultiple cell typesRNA biologySmall RNAsExtracellular biologyBiosynthetic machineryBiochemical approachesMammalian speciesBattery of chemicalAnti-dsRNA antibodiesN-glycansCell typesReceptor familyCultured cellsCell surfaceRNAThird scaffoldGlycoRNABiologyMajor targetGlycosylationGlycansSialic acid
2020
Generating orthogonal glycosyltransferase and nucleotide sugar pairs as next-generation glycobiology tools
Cioce A, Malaker SA, Schumann B. Generating orthogonal glycosyltransferase and nucleotide sugar pairs as next-generation glycobiology tools. Current Opinion In Chemical Biology 2020, 60: 66-78. PMID: 33125942, PMCID: PMC7955280, DOI: 10.1016/j.cbpa.2020.09.001.Peer-Reviewed Original ResearchConceptsMass spectrometry glycoproteomicsCell surface glycoproteomeProtein glycosylationBiological processesQuantitative biologyMutant glycosyltransferasesGlycoproteomicsDifferent glycansGlycansPrecision toolsGlycosyltransferasesBiosynthesisGlycoproteomeGlycomeGlycosyltransferaseBiologyGlycosylationGlycobiologyLabeling reagentLimited specificityPhysiologySpecificityParticular subtypeRoleCellsTargeted glycan degradation potentiates the anticancer immune response in vivo
Gray MA, Stanczak MA, Mantuano NR, Xiao H, Pijnenborg JFA, Malaker SA, Miller CL, Weidenbacher PA, Tanzo JT, Ahn G, Woods EC, Läubli H, Bertozzi CR. Targeted glycan degradation potentiates the anticancer immune response in vivo. Nature Chemical Biology 2020, 16: 1376-1384. PMID: 32807964, PMCID: PMC7727925, DOI: 10.1038/s41589-020-0622-x.Peer-Reviewed Original ResearchMeSH KeywordsAllograftsAnimalsAntibodies, MonoclonalB7-H1 AntigenCell Line, TumorHumansHydrolysisImmunoconjugatesImmunotherapyKiller Cells, NaturalMelanoma, ExperimentalMiceMice, Inbred C57BLMice, KnockoutModels, MolecularMolecular Targeted TherapyNeuraminidasePolysaccharidesProgrammed Cell Death 1 ReceptorProtein BindingProtein Interaction Domains and MotifsProtein Structure, SecondaryReceptor, ErbB-2Sialic Acid Binding Immunoglobulin-like LectinsSurvival AnalysisT-LymphocytesConceptsImmune checkpoint inhibitor therapyTumor-infiltrating myeloid cellsCheckpoint inhibitor therapyImmune cell infiltrationPowerful treatment optionAnticancer immune responseSurvival of miceSyngeneic breast cancer modelImmune cell activationBreast cancer modelBreast cancer cellsCheckpoint therapyMost patientsInhibitor therapyPD-1Checkpoint receptorsImmune suppressionTreatment optionsCell infiltrationImmune responseMyeloid cellsCancer modelCell activationCertain cancersCancer types
2019
Isolation of Major Histocompatibility Complex (MHC)-Associated Peptides by Immunoaffinity Purification
Penny SA, Malaker SA. Isolation of Major Histocompatibility Complex (MHC)-Associated Peptides by Immunoaffinity Purification. Methods In Molecular Biology 2019, 2024: 235-243. PMID: 31364053, DOI: 10.1007/978-1-4939-9597-4_14.ChaptersConceptsMass spectrometryAntibody conjugationImmunoaffinity purificationSurface of cellsMajor histocompatibility complexAutoimmune diseasesT cellsImmune componentsDisease processMoleculesHistocompatibility complexAntigenic peptidesMHCAssociated peptidePurificationPeptidesSurfaceSpectrometryElutionCellsComplexesConjugationCD8CD4Cancer
2017
Peptide-binding motifs of two common equine class I MHC molecules in Thoroughbred horses
Bergmann T, Lindvall M, Moore E, Moore E, Sidney J, Miller D, Tallmadge RL, Myers PT, Malaker SA, Shabanowitz J, Osterrieder N, Peters B, Hunt DF, Antczak DF, Sette A. Peptide-binding motifs of two common equine class I MHC molecules in Thoroughbred horses. Immunogenetics 2017, 69: 351-358. PMID: 28315936, PMCID: PMC5555743, DOI: 10.1007/s00251-017-0978-6.Peer-Reviewed Original Research