Warning: This is a preliminary report that has not been peer-reviewed. It should not be regarded as conclusive, guide clinical practice/health-related behavior, or be reported in news media as established information.

Evolving spike-protein N-glycosylation in SARS-CoV-2 variants (Preliminary Report)

It has been three years since SARS-CoV-2 emerged and the world plunged into a once in a century pandemic. Since then, multiple waves of infection have swept through the human population, led by variants that were able to evade any acquired immunity. The co-evolution of SARS-CoV-2 variants with human immunity ...
provides an excellent opportunity to study the interaction between viral pathogens and their human hosts. The heavily N-glycosylated spike-protein of SARS-CoV-2 plays a pivotal role in initiating infection and is the target for host immune response, both of which are impacted by host-installed N-glycans. We compared the N-glycan landscape of recombinantly expressed, stabilized, soluble spike-protein trimers representing seven of the most prominent SARS-CoV-2 variants and found that N-glycan processing is conserved at most sites. However, in multiple variants, processing of N-glycans from high mannose-to complex-type is reduced at sites N165, N343 and N616, implicated in spike-protein function.
Date: May. 09, 2023
Status: Preliminary Report
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