Role of N-Glycosylation in SARS-CoV-2 Spike Protein Dynamics and Stability

Hydrogen/deuterium exchange-mass spectrometry data reveals conformational changes in the SARS-CoV-2 spike protein after enzymatic deglycosylation. The dataset, authored by Sarah H. Osman and last updated in April 2026, contains results from PNGase F treatment of the recombinant 614G HexaPro spike ectodomain. It provides insights into reduced thermal stability and altered binding behavior with antibodies and the human ACE2 receptor.

Use Cases

• Modeling protein conformational dynamics based on hydrogen/deuterium exchange data.
• Analyzing the impact of glycosylation on viral fusion machinery, based on changes in the heptad repeat 2 region.
• Studying the relationship between glycans and receptor-binding domain (RBD) positioning, based on disorder in the 630 loop.
• Investigating glycan-mediated effects on antibody and ACE2 binding affinity.
• Assessing protein thermal stability changes following glycan removal.

Strengths

• Data is derived from a specific, well-described experimental method: hydrogen/deuterium exchange-mass spectrometry.
• Focuses on a key viral protein, the recombinant 614G HexaPro spike ectodomain, with clear biological relevance.
• Results link structural changes to functional outcomes like antibody binding and thermal stability.

Limitations

• Row count is unknown, which may limit suitability assessment.
• Column-level documentation is absent; field semantics must be inferred after download.
• The dataset is very small at 55.1 KB, indicating limited scope.

Provenance

Source

Sarah H. Osman via figshare.

Collection Method

Experimental data from PNGase F glycosidase treatment and hydrogen/deuterium exchange-mass spectrometry.

Time Range

Experimental timeframe not specified; dataset metadata updated April 2026.

Freshness

Last updated 2026-04-22 17:11:04; freshness should be verified.

Geography

Geographic origin of the research not specified.