Cold sensitivity of the SARS-CoV-2 spike ectodomain

Nat Struct Mol Biol. 2021 Feb;28(2):128-131. doi: 10.1038/s41594-020-00547-5. Epub 2021 Jan 5.

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