Gammacoronavirus Spike Protein Glycosylation and Structural Data

Structural and glycoproteomic data for spike proteins from two distinct gammacoronaviruses infecting marine mammals. The dataset includes cryo-EM structural information and analysis of over 100 N-glycans per trimer, with specific O-glycosylation sites. It was authored by Ruben J. G. Hulswit and shared on figshare in 2026.

Use Cases

• Analyze the unique tripodal quaternary assembly of the S1 subunit described in the cryo-EM reconstructions.
• Study the distribution and abundance of high-mannose glycans on the S1⁰ domain and O-glycosylation within the mucin-like loop.
• Compare sequence and structural features of the two gammacoronavirus spike proteins which share 75.7% sequence identity.
• Investigate the structural similarity of the novel S1⁰ domain to members of the cupin protein superfamily.

Strengths

• Includes high-resolution cryo-EM structural data for two distinct virus spike proteins.
• Documents extensive glycosylation with over 100 N-glycans per trimer and specific O-glycosylation sites.
• Released under a permissive CC-BY-4.0 license for reuse.

Limitations

• The dataset is small at 787.4 KB, indicating limited scope and likely a focused subset of analyzed data.
• Specific row counts and column schemas are not provided, limiting immediate understanding of data organization.

Provenance

Source

figshare, authored by Ruben J. G. Hulswit.

Collection Method

Data derived from cryo-EM structural studies and glycoproteomic analyses.

Freshness

Last updated in April 2026, indicating recent data.