Files and links (1)
Preprint (Author's original)Open Access (License Unspecified), Open
Preprint
Temperature-dependent Spike-ACE2 interaction of Omicron subvariants is associated with viral transmission
bioRxiv.org
23 Jan 2024
Abstract
The continued evolution of SARS-CoV-2 requires persistent monitoring of its subvariants. Omicron subvariants are responsible for the vast majority of SARS-CoV-2 infections worldwide, with XBB and BA.2.86 sublineages representing more than 90% of circulating strains as of January 2024. In this study, we characterized the functional properties of Spike glycoproteins from BA.2.75, CH.1.1, DV.7.1, BA.4/5, BQ.1.1, XBB, XBB.1, XBB.1.16, XBB.1.5, FD.1.1, EG.5.1, HK.3 BA.2.86 and JN.1. We tested their capacity to evade plasma-mediated recognition and neutralization, ACE2 binding, their susceptibility to cold inactivation, Spike processing, as well as the impact of temperature on Spike-ACE2 interaction. We found that compared to the early wild-type (D614G) strain, most Omicron subvariants Spike glycoproteins evolved to escape recognition and neutralization by plasma from individuals who received a fifth dose of bivalent (BA.1 or BA.4/5) mRNA vaccine and improve ACE2 binding, particularly at low temperatures. Moreover, BA.2.86 had the best affinity for ACE2 at all temperatures tested. We found that Omicron subvariants Spike processing is associated with their susceptibility to cold inactivation. Intriguingly, we found that Spike-ACE2 binding at low temperature was significantly associated with growth rates of Omicron subvariants in humans. Overall, we report that Spikes from newly emerged Omicron subvariants are relatively more stable and resistant to plasma-mediated neutralization, present improved affinity for ACE2 which is associated, particularly at low temperatures, with their growth rates.
Metrics
12 Record Views
Details
- Title
- Temperature-dependent Spike-ACE2 interaction of Omicron subvariants is associated with viral transmission
- Creators
- Mehdi Benlarbi - Centre Hospitalier de l’Université de MontréalShilei Ding - Centre Hospitalier de l’Université de MontréalEtienne Belanger - Centre Hospitalier de l’Université de MontréalAlexandra Tauzin - Centre Hospitalier de l’Université de MontréalRaphael Poujol - Montreal Heart InstituteHalima Medjahed - Centre Hospitalier de l’Université de MontréalOmar El Ferri - University of OttawaYuxia Bo - University of OttawaCatherine Bourassa - Centre Hospitalier de l’Université de MontréalJulie Hussin - Montreal Heart InstituteJudith Fafard - Institut National de Santé Publique du QuébecMarzena Pazgier - Uniformed Services University of the Health SciencesInes Levade - Institut National de Santé Publique du QuébecCameron F Abrams - Drexel University, Chemical and Biological EngineeringMarceline Cote - University of OttawaAndres Finzi - Centre Hospitalier de l’Université de Montréal
- Publication Details
- bioRxiv.org
- Publisher
- Cold Spring Harbor Laboratory Press; Cold Spring Harbor
- Resource Type
- Preprint
- Language
- English
- Academic Unit
- Chemical and Biological Engineering
- Other Identifier
- 991021882015704721