Communication Dans Un Congrès Année : 2025

Fine-tuning the N-glycosylation of epigenetic transgene silencing in Chlamydomonas reinhardtii

Résumé

Microalgae are considered as attractive expression systems for the production of biologics. As photosynthetic unicellular organisms, they do not require costly and complex media for growing, and are able to secrete proteins and perform protein glycosylation (1). Some biologics have been successfully produced in the green microalgae Chlamydomonas reinhardtii. However, posttranslational modifications like glycosylation of these Chlamydomonas-made biologics have poorly been investigated so far. Therefore, we reported on the first structural investigation of glycans linked to human erythropoietin (hEPO) expressed in a wild-type C. reinhardtii strain and in mutants impaired in key Golgi glycosyltransferases (2). The glycoproteomic analysis of recombinant hEPO (rhEPO) expressed in the wild-type strain demonstrated that the three Nglycosylation sites are 100% glycosylated with mature N-glycans containing four to five mannose residues and carrying core-xylose, core-fucose and O-methyl groups (Figure 1). Moreover, expression in C. reinhardtii insertional mutants defective in XYLOSYLTRANSFERASES A and B and FUCOSYLTRANSFERASE resulted in drastic decreases of core-xylosylation and corefucosylation of glycans N-linked to the rhEPOs, thus demonstrating that this strategy offers perspectives for humanizing the N-glycosylation of the Chlamydomonas-made biologics.

Fichier non déposé

Dates et versions

hal-05245216 , version 1 (03-10-2025)

Identifiants

  • HAL Id : hal-05245216 , version 1

Citer

Elodie Mathieu‐Rivet. Fine-tuning the N-glycosylation of epigenetic transgene silencing in Chlamydomonas reinhardtii. 21th INTERNATIONAL CONFERENCE ON THE CELL AND MOLECULAR BIOLOGY OF CHLAMYDOMONAS, UNIVERSITE DE MUNSTER, Aug 2025, MUNSTER, Germany. ⟨hal-05245216⟩
60 Consultations
2 Téléchargements

Partager

  • More