Role of N-linked glycosylation sites in human ACE2 in SARS-CoV-2 and hCoV-NL63 infection
Several human coronaviruses use angiotensin-converting enzyme 2 (ACE2) as a primary receptor for infection of human cells. ACE2 is glycosylated at seven distinct positions, and the role of glycans for the entry of SARS-CoV-2 and hCoV-NL63 into their target cells is incompletely understood. Here, we examined the impact of individual and combined mutations in hACE2 glycosylation sites on Spike-mediated VSV-pseudoparticle and genuine SARS-CoV-2 and hCoV-NL63 infection and cell-to-cell fusion. Our results provide new information on the role of glycans in hACE2 for infection by highly pathogenic and seasonal coronaviruses.
Authors
- Christoph Jung (ORCID: https://orcid.org/0000-0002-1422-4991)
- Rayhane Nchioua (ORCID: https://orcid.org/0009-0001-1436-1232)
- Fabian Zech (ORCID: https://orcid.org/0000-0002-1668-8060)
- Chiara Pastorio (ORCID: https://orcid.org/0000-0002-4745-3678)
- Sabrina Noettger (ORCID: https://orcid.org/0000-0003-0059-5289)
- Steffen Stenger (ORCID: https://orcid.org/0000-0001-5471-0807)
- Timo Jacob (ORCID: https://orcid.org/0000-0001-7777-2306)
- Frank Kirchhoff (ORCID: https://orcid.org/0000-0002-7052-2360)
Institutions
- Karlsruhe Institute of Technology (DE)
- University Medical Center (US)
- Helmholtz-Institute Ulm (DE)
- Institute of Medical Microbiology and Hygiene (DE)
Publication Details
- Journal
- Journal of Virology
- Published
- 2025-03-28
- DOI
- https://doi.org/10.1128/jvi.02202-24
- Citations
- 2
- Primary Topic
- SARS-CoV-2 and COVID-19 Research
- Type
- article
- Field-Weighted Citation Impact
- 2.79