Receptor and viral determinants of SARS-coronavirus adaptation to human ACE2.

The EMBO Journal
Wenhui LiMichael Farzan

Abstract

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.

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Citations

Aug 14, 2013·Cell Research·Berend Jan BoschBart L Haagmans
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Datasets Mentioned

BETA
AY525636
AY274119
AY304486
AY881174

Methods Mentioned

BETA
glycosylation
immunoprecipitation
flow cytometry
glyosylation
PCR
flow
surface plasmon resonance
chip

Software Mentioned

EVALUATION
BIA
Biacore

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