2023
Comprehensive analysis of platelet glycoprotein Ibα ectodomain glycosylation
Hollenhorst M, Tiemeyer K, Mahoney K, Aoki K, Ishihara M, Lowery S, Rangel-Angarita V, Bertozzi C, Malaker S. Comprehensive analysis of platelet glycoprotein Ibα ectodomain glycosylation. Journal Of Thrombosis And Haemostasis 2023, 21: 995-1009. PMID: 36740532, PMCID: PMC10065957, DOI: 10.1016/j.jtha.2023.01.009.Peer-Reviewed Original ResearchConceptsO-glycositesGPIb-IX-V complexMajor ligand-binding subunitAmino acid sitesLigand-binding subunitVon Willebrand factor bindingPlatelet glycoprotein IbαMechanosensory domainFactor bindingEndogenous proteinsRecombinant proteinsN-glycositesStructural rolePlatelet biologyGlycan structuresGlycoprotein IbαO-glycansT antigenGlycosylation profileDiverse repertoireGlycosylationGlycansComprehensive analysisGlycositesVon Willebrand factor
2021
Genome-wide CRISPR screens reveal a specific ligand for the glycan-binding immune checkpoint receptor Siglec-7
Wisnovsky S, Möckl L, Malaker SA, Pedram K, Hess GT, Riley NM, Gray MA, Smith BAH, Bassik MC, Moerner WE, Bertozzi CR. Genome-wide CRISPR screens reveal a specific ligand for the glycan-binding immune checkpoint receptor Siglec-7. Proceedings Of The National Academy Of Sciences Of The United States Of America 2021, 118: e2015024118. PMID: 33495350, PMCID: PMC7865165, DOI: 10.1073/pnas.2015024118.Peer-Reviewed Original Research
2020
Targeted 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
2017
Shared peptide binding of HLA Class I and II alleles associate with cutaneous nevirapine hypersensitivity and identify novel risk alleles
Pavlos R, McKinnon EJ, Ostrov DA, Peters B, Buus S, Koelle D, Chopra A, Schutte R, Rive C, Redwood A, Restrepo S, Bracey A, Kaever T, Myers P, Speers E, Malaker SA, Shabanowitz J, Jing Y, Gaudieri S, Hunt DF, Carrington M, Haas DW, Mallal S, Phillips EJ. Shared peptide binding of HLA Class I and II alleles associate with cutaneous nevirapine hypersensitivity and identify novel risk alleles. Scientific Reports 2017, 7: 8653. PMID: 28819312, PMCID: PMC5561238, DOI: 10.1038/s41598-017-08876-0.Peer-Reviewed Original ResearchConceptsHypersensitivity reactionsHLA moleculesTreatment-limiting hypersensitivity reactionClass IDrug hypersensitivity syndromeHuman leukocyte antigen (HLA) systemHLA class IHLA-C allelesClass II allelesLeukocyte antigen systemHLA-B allelesNevirapine hypersensitivityHypersensitivity syndromeHLA associationsIndependent associationHLA-DRB1T cellsImmune responseNovel risk allelesPathogenic mechanismsDrug specific interactionsMultiple class IAntigen systemPrimary predispositionRisk allelesPeptide-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
2016
Identification and Characterization of Complex Glycosylated Peptides Presented by the MHC Class II Processing Pathway in Melanoma
Malaker SA, Ferracane MJ, Depontieu FR, Zarling AL, Shabanowitz J, Bai DL, Topalian SL, Engelhard VH, Hunt DF. Identification and Characterization of Complex Glycosylated Peptides Presented by the MHC Class II Processing Pathway in Melanoma. Journal Of Proteome Research 2016, 16: 228-237. PMID: 27550523, PMCID: PMC5218890, DOI: 10.1021/acs.jproteome.6b00496.Peer-Reviewed Original ResearchAmino Acid SequenceBinding SitesCarbohydrate SequenceCell Line, TumorComplementarity Determining RegionsCrystallography, X-RayDisulfidesGlycopeptidesGlycosylationHLA-DR AntigensHumansMelanocytesModels, MolecularProtein BindingProtein Conformation, alpha-HelicalProtein Conformation, beta-StrandProtein Interaction Domains and MotifsThermodynamics