Abstract
The SARS-CoV-2 spike (S) protein, a primary target for COVID-19 vaccine development, presents its receptor binding domain in two conformations, the receptor-accessible 'up' or receptor-inaccessible 'down' states. Here we report that the commonly used stabilized S ectodomain construct '2P' is sensitive to cold temperatures, and this cold sensitivity is abrogated in a 'down' state-stabilized ectodomain. Our findings will impact structural, functional and vaccine studies that use the SARS-CoV-2 S ectodomain.
Publication types
-
Research Support, N.I.H., Extramural
-
Research Support, U.S. Gov't, Non-P.H.S.
-
Research Support, U.S. Gov't, P.H.S.
MeSH terms
-
Antibodies, Viral / chemistry
-
COVID-19 Vaccines / chemistry
-
Cold Temperature
-
Cryoelectron Microscopy
-
Enzyme-Linked Immunosorbent Assay
-
Humans
-
Protein Denaturation
-
Protein Domains
-
Protein Stability
-
Spike Glycoprotein, Coronavirus / chemistry*
-
Spike Glycoprotein, Coronavirus / ultrastructure
-
Surface Plasmon Resonance
Substances
-
Antibodies, Viral
-
COVID-19 Vaccines
-
Spike Glycoprotein, Coronavirus
-
spike protein, SARS-CoV-2