Zala Živič (Author), Žiga Strmšek (Author), Marko Novinec (Author), Jurij Lah (Author), San Hadži (Author)

Abstract

Spike trimer plays a key role in SARS-CoV-2 infection and vaccine development. It consists of a globular head and a flexible stalk domain that anchors the protein into the viral membrane. While the head domain has been extensively studied, the properties of the adjoining stalk are poorly understood. Here, we characterize the coiled-coil formation and thermodynamic stability of the stalk domain and its segments. We find that the N-terminal segment of the stalk does not form coiled-coils and remains disordered in solution. The C-terminal stalk segment forms a trimeric coiled-coil in solution, which becomes significantly stabilized in the context of the full-length stalk. Its crystal structure reveals a novel antiparallel tetramer coiled-coil with an unusual combination of a-d and e-a-d hydrophobic core packing. Structural analysis shows that a subset of hydrophobic residues stabilizes different coiled-coil structures: trimer, tetramer, and heterohexamer, underscoring a highly polymorphic nature of the SARS-CoV-2 stalk sequence.

Keywords

protein spike;korona virus;obvita vijačnica;spike protein;corona virus;coiled-coil;

Data

Language: English
Year of publishing:
Typology: 1.01 - Original Scientific Article
Organization: UL FKKT - Faculty of Chemistry and Chemical Technology
UDC: 577.322
COBISS: 97817859 Link will open in a new window
ISSN: 0892-6638
Views: 105
Downloads: 33
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Other data

Secondary language: Slovenian
Secondary keywords: SARS-CoV-2 (virus);
Type (COBISS): Article
Pages: str. 1-11
Volume: ǂVol. ǂ36
Issue: ǂiss. ǂ3
Chronology: Mar. 2022
DOI: 10.1096/fj.202101670R
ID: 15437279