Receptor and viral determinants of SARS-coronavirus adaptation to human ACE2
By Wenhui Li, Chengsheng Zhang, J. Sui, J. Kuhn, M. J. Moore, S. Luo, S. Wong, I-Chueh Huang, KeMing Xu, N. Vasilieva and 6 more. EMBO Journal, 2005
977 citations recorded by the source corpus.
Human angiotensin‐converting enzyme 2 (ACE2) is a functional receptor for SARS coronavirus (SARS‐CoV). Here we identify the SARS‐CoV spike (S)‐protein‐binding site on ACE2. We also compare S proteins of SARS‐CoV isolated during the 2002–2003 SARS outbreak and during the much less severe 2003–2004 outbreak, and from palm civets, a possible source of SARS‐CoV found in humans. All three S proteins bound to and utilized palm‐civet ACE2 efficiently, but the latter two S proteins utilized human ACE2 markedly less efficiently than did the S protein obtained during the earlier human outbreak. The lower affinity of these S proteins could be complemented by altering specific residues within the S‐protein‐binding site of human ACE2 to those of civet ACE2, or by altering S‐protein residues 479 and 487 to residues conserved during the 2002–2003 outbreak. Collectively, these data describe molecular interactions important to the adaptation of SARS‐CoV to human cells, and provide insight into the severity of the 2002–2003 SARS epidemic.
Subfields: Animal Science and Zoology, Infectious Diseases
View Paper: https://www.semanticscholar.org/paper/003144973764dfce847ccaa197fa156a7fbebdd0
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Citations in the corpus
- Renin–Angiotensin–Aldosterone System Inhibitors in Patients with Covid-19 (2020, neutral): “Angiotensin II AT1 receptors regulate ACE2 and angiotensin-(1-7) expression in the aorta of spontaneously hypertensive rats.”
- Deep mutational scanning of SARS-CoV-2 receptor binding domain reveals constraints on folding and ACE2 binding (2020, positive): “The core-RBD subdomain consists of a central beta sheet flanked by alpha-helices, and presents a stably folded scaffold for the receptor binding motif (RBM, residues 437-508; (Li et al., 2005a)) which encodes ACE2-binding and receptor specificity (Letko et al., 2020).”
- Structure, Function, and Antigenicity of the SARS-CoV-2 Spike Glycoprotein (2020, methodology): “Indeed, SARS-CoV isolates from the three phases of the 2002-2003 epidemic were more efficiently transmitted among humans and more pathogenic than the isolates associated with the 2003-2004 re-emergence that caused only a few cases, in line with their binding affinities for hACE2 (Consortium, 2004; K”
- Olfactory and gustatory dysfunctions as a clinical presentation of mild-to-moderate forms of the coronavirus disease (COVID-19): a multicenter European study (2020, background): “In other words, the expression level of ACE2 in different tissues might be critical for the susceptibility, symptoms, and outcomes of COVID-19 infection [21].”
- SARS-CoV-2 Entry Genes Are Most Highly Expressed in Nasal Goblet and Ciliated Cells within Human Airways (2020, background): “For SARS, the binding affinity between the S protein and the ACE2 receptor was found to be a major determinant of viral replication rates and disease severity 19 .”
- ACE2 Receptor Expression and Severe Acute Respiratory Syndrome Coronavirus Infection Depend on Differentiation of Human Airway Epithelia (2005, background): “A region of the extracellular portion of ACE2 that includes the first -helix and lysine 353 and proximal residues of the N terminus of -sheet 5 interacts with high affinity to the receptor binding domain of the SARS-CoV S glycoprotein ( 22 ).”
- The protein expression profile of ACE2 in human tissues (2020, positive): “SARS-CoV has previously been shown to enter the cell via the ACE2 receptor, primed by the cellular serine protease TMPRSS2 (Li et al , 2005; Matsuyama et al , 2010).”