Elsevier

Antiviral Research

Volume 100, Issue 1, October 2013, Pages 246-254
Antiviral Research

Review
Receptor recognition and cross-species infections of SARS coronavirus

https://doi.org/10.1016/j.antiviral.2013.08.014 Get rights and content

Highlights

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    SARS-CoV recognizes host receptor ACE2 via its receptor-binding domain (RBD).

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    Residue differences in host ACE2 present species barriers for SARS-CoV infections.

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    SARS-CoV can adapt to ACE2 from several species through RBD mutations.

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    Structural studies have revealed receptor adaptation mechanisms of SARS-CoV.

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    Structural studies also allow predictions of future SARS-CoV evolution.

Abstract

Receptor recognition is a major determinant of the host range, cross-species infections, and pathogenesis of the severe acute respiratory syndrome coronavirus (SARS-CoV). A defined receptor-binding domain (RBD) in the SARS-CoV spike protein specifically recognizes its host receptor, angiotensin-converting enzyme 2 (ACE2). This article reviews the latest knowledge about how RBDs from different SARS-CoV strains interact with ACE2 from several animal species. Detailed research on these RBD/ACE2 interactions has established important principles on host receptor adaptations, cross-species infections, and future evolution of SARS-CoV. These principles may apply to other emerging animal viruses, including the recently emerged Middle East respiratory syndrome coronavirus (MERS-CoV). This paper forms part of a series of invited articles in Antiviral Research on “From SARS to MERS: 10 years of research on highly pathogenic human coronaviruses”.

Keywords

Coronavirus
Spike protein
Severe acute respiratory syndrome
Middle East respiratory syndrome
Virus evolution

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