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Yeast surface display-based identification of ACE2 mutations that modulate SARS-CoV-2 spike binding across multiple mammalian species.

Publication ,  Journal Article
Heinzelman, P; Greenhalgh, JC; Romero, PA
Published in: Protein engineering, design & selection : PEDS
February 2022

Understanding how severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) interacts with different mammalian angiotensin-converting enzyme II (ACE2) cell entry receptors elucidates determinants of virus transmission and facilitates development of vaccines for humans and animals. Yeast display-based directed evolution identified conserved ACE2 mutations that increase spike binding across multiple species. Gln42Leu increased ACE2-spike binding for human and four of four other mammalian ACE2s; Leu79Ile had an effect for human and three of three mammalian ACE2s. These residues are highly represented, 83% for Gln42 and 56% for Leu79, among mammalian ACE2s. The above findings can be important in protecting humans and animals from existing and future SARS-CoV-2 variants.

Duke Scholars

Published In

Protein engineering, design & selection : PEDS

DOI

EISSN

1741-0134

ISSN

1741-0126

Publication Date

February 2022

Volume

35

Start / End Page

gzab035

Related Subject Headings

  • Spike Glycoprotein, Coronavirus
  • Saccharomyces cerevisiae
  • SARS-CoV-2
  • Protein Binding
  • Mutation
  • Humans
  • COVID-19
  • Biophysics
  • Animals
  • Angiotensin-Converting Enzyme 2
 

Citation

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Heinzelman, P., Greenhalgh, J. C., & Romero, P. A. (2022). Yeast surface display-based identification of ACE2 mutations that modulate SARS-CoV-2 spike binding across multiple mammalian species. Protein Engineering, Design & Selection : PEDS, 35, gzab035. https://doi.org/10.1093/protein/gzab035
Heinzelman, Pete, Jonathan C. Greenhalgh, and Philip A. Romero. “Yeast surface display-based identification of ACE2 mutations that modulate SARS-CoV-2 spike binding across multiple mammalian species.Protein Engineering, Design & Selection : PEDS 35 (February 2022): gzab035. https://doi.org/10.1093/protein/gzab035.
Heinzelman P, Greenhalgh JC, Romero PA. Yeast surface display-based identification of ACE2 mutations that modulate SARS-CoV-2 spike binding across multiple mammalian species. Protein engineering, design & selection : PEDS. 2022 Feb;35:gzab035.
Heinzelman, Pete, et al. “Yeast surface display-based identification of ACE2 mutations that modulate SARS-CoV-2 spike binding across multiple mammalian species.Protein Engineering, Design & Selection : PEDS, vol. 35, Feb. 2022, p. gzab035. Epmc, doi:10.1093/protein/gzab035.
Heinzelman P, Greenhalgh JC, Romero PA. Yeast surface display-based identification of ACE2 mutations that modulate SARS-CoV-2 spike binding across multiple mammalian species. Protein engineering, design & selection : PEDS. 2022 Feb;35:gzab035.
Journal cover image

Published In

Protein engineering, design & selection : PEDS

DOI

EISSN

1741-0134

ISSN

1741-0126

Publication Date

February 2022

Volume

35

Start / End Page

gzab035

Related Subject Headings

  • Spike Glycoprotein, Coronavirus
  • Saccharomyces cerevisiae
  • SARS-CoV-2
  • Protein Binding
  • Mutation
  • Humans
  • COVID-19
  • Biophysics
  • Animals
  • Angiotensin-Converting Enzyme 2