Highlights • SARS-CoV recognizes host receptor ACE2 via its receptor-binding domain (RBD). • Residue differences in host ACE2 present species barriers for SARS-CoV infections. • SARS-CoV can adapt to ACE2 from several species through RBD mutations. • Structural studies have revealed receptor adaptation mechanisms of SARS-CoV. • Structural studies also allow predictions of future SARS-CoV evolution. 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”.
【저자키워드】 coronavirus, Virus evolution, Spike protein, Severe acute respiratory syndrome, Middle East respiratory syndrome,