| Autor: |
Rebeca Kawahara, Julian Ugonotti, Sayantani Chatterjee, Harry C. Tjondro, Ian Loke, Benjamin L. Parker, Vignesh Venkatakrishnan, Regis Dieckmann, Zeynep Sumer-Bayraktar, Anna Karlsson-Bengtsson, Johan Bylund, Morten Thaysen-Andersen |
| Rok vydání: |
2023 |
| DOI: |
10.1101/2023.01.18.524318 |
| Popis: |
Neutrophils store microbicidal glycoproteins in cytosolic granules to fight intruding pathogens, but their granule distribution and formation mechanism(s) during granulopoiesis remain unmapped. Herein, we perform comprehensive spatiotemporalN-glycoproteome profiling of isolated granule populations from blood-derived neutrophils and during their maturation from bone marrow-derived progenitors using glycomics-assisted glycoproteomics. Interestingly, the granules of resting neutrophils exhibited distinctive glycophenotypes including, most strikingly, peculiar highly truncatedN-glycosylation in the azurophilic granules. Excitingly, proteomics and transcriptomics data from discrete myeloid progenitor stages revealed that profound glycoproteome remodelling underpins the promyelocytic-to-metamyelocyte transition and that remodelling is driven primarily by changes in protein expression and less by the glycosylation machinery. Notable exceptions were the oligosaccharyltransferase subunits responsible for initiation ofN-glycoprotein biosynthesis that were strongly expressed in early myeloid progenitors correlating with high glycosylation efficiencies of the azurophilic granule proteins. Our study provides spatiotemporal insights into the complex neutrophilN-glycoproteome featuring an intriguing granule-specificN-glycosylation formed by dynamic remodelling during myeloid progenitor-to-neutrophil maturation.Key pointsSystems glycobiology reveals that profoundN-glycoproteome remodelling accompanies early neutrophil granulopoiesisPrecision glycoproteomics produces detailed cartography of neutrophils that exhibit site-, protein- and granule-specific N-glycosylation |
| Databáze: |
OpenAIRE |
| Externí odkaz: |
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