2021
Small 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 ResearchMeSH KeywordsAnimalsAntibodiesBase SequenceBiosynthetic PathwaysCell LineCell MembraneCell SurvivalHumansMass SpectrometryN-Acetylneuraminic AcidPolyadenylationPolysaccharidesRNARNA, UntranslatedSialic Acid Binding Immunoglobulin-like LectinsStaining and LabelingConceptsLiving 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
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
2019
The mucin-selective protease StcE enables molecular and functional analysis of human cancer-associated mucins
Malaker SA, Pedram K, Ferracane MJ, Bensing BA, Krishnan V, Pett C, Yu J, Woods EC, Kramer JR, Westerlind U, Dorigo O, Bertozzi CR. The mucin-selective protease StcE enables molecular and functional analysis of human cancer-associated mucins. Proceedings Of The National Academy Of Sciences Of The United States Of America 2019, 116: 7278-7287. PMID: 30910957, PMCID: PMC6462054, DOI: 10.1073/pnas.1813020116.Peer-Reviewed Original ResearchMeSH KeywordsAmino Acid MotifsAntigens, CDAntigens, Differentiation, MyelomonocyticEscherichia coliEscherichia coli ProteinsHumansLectinsMass SpectrometryMetalloendopeptidasesMucinsNeoplasm ProteinsSialic Acid Binding Immunoglobulin-like LectinsSubstrate SpecificityConceptsModular protein domainsProtein domainsSecreted proteinsMucin domainFunctional analysisHuman diseasesMucin biologyGlycosylation patternsCultured cellsMolecular levelCell surfaceSequence coverageKey playersBacterial proteasesCancer-associated mucinsDiscrete peptidesBiological ligandsProteaseHuman mucinsGlycoform analysisStcESiglec-9Domain structureMass spectrometryDomain