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. 2005 Mar 9;196(4):963–966. doi: 10.1016/0022-2836(87)90422-0

Evidence for a coiled-coil structure in the spike proteins of coronaviruses☆

RJ de Groot 1, W Luytjes 1, MC Horzinek 1, BAM van der Zeijst 2, WJM Spaan 1, JA Lenstra 2
PMCID: PMC7131189  PMID: 3681988

Abstract

The amino acid sequences of the spike proteins from three distantly related coronaviruses have been deduced from cDNA sequences. In the C-terminal half, an homology of about 30% was found, while there was no detectable sequence conservation in the N-terminal regions. Hydrophobic “heptad” repeat patterns indicated the presence of two α-helices with predicted lengths of 100 and 50 Å, respectively. It is suggested that, in the spike oligomer. these α-helices form a complex coiled-coil, resembling the supersecondary structures in two other elongated membrane proteins, the haemagglutinin of influenza virus and the variable surface glycoprotein of trypanosomes.

Abbreviations: MHV, mouse hepatitis virus; IBV, infectious bronchitis virus; FIPV, feline infectious peritonitis virus; HA, haemagglutinin trimer

Footnotes

☆

This work was supported by a research grant from Duphar B.V., Weesp, The Netherlands.

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