Comprehensive characterization of N- and O- glycosylation of SARS- CoV-2 human receptor angiotensin converting enzyme 2
proteomics structural biology therapeutics
Authors: Asif Shajahan, Stephanie Archer-Hartmann, Nitin T. Supekar, Anne S. Gleinich, Christian Heiss, and Parastoo Azadi*
Link to paper: https://www.biorxiv.org/content/10.1101/2020.05.01.071688v1
Journal/ Pre-Print: bioRvix
Tags: Proteomics, Structural Biology, Therapeutics
1. Quantitative glycosylation mapping on hACE2
2. Glycan occupancy at all seven possible N-glycosylation sites
3. Glycan occupancy at three O-glycosylation sites
Glycoproteomics and glycomics were performed on the human angiotensin-converting enzyme 2 (hACE2), entry receptor for SARS-CoV-1 and SARS-CoV-2, expressed in human embryonic kidney 293 (HEK293) cells. The authors identified, that all seven possible N-glycosylation sites were occupied with complex glycans (N53, N90, N103, N322, N432, N564, N690) characterising them in full. Furthermore, three additional O-glycosylation sites were identified at sites O155, O494 and O773.
Impact for SARS-CoV2/COVID19 research efforts
Understand the virology and/or cell biology of SARS-CoV2/COVID19
Inhibit of SARS-CoV2/COVID19 transmission
· In vitro study
Strengths and limitations of the paper
Novelty: Identifying O-glycosylation sites of hACE2.
Standing in the field: Several publications show that all seven possible N-glycosylation sites are occupied in hACE2 (e.g. Tipnis et al. 2000; Li et al. 2003, Sun, Z. et al 2020).
Appropriate statistics: Yes
Viral model used: Human recombinant hACE2(Gln18 to Ser740) was expressed in HEK293 cells.
Translatability: Very limited may help us understand the hACE2 interaction with SARS-CoV-2 RBD and look to exploit this therapeutically.
Main limitations: The hACE2 analysed is expressed in kidney cells it may be interesting to compare the glycosylation to for example to lung epithelial hACE2