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. 2012 Jan 30;287(12):8904–8911. doi: 10.1074/jbc.M111.325803

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© 2012 by The American Society for Biochemistry and Molecular Biology, Inc.

This article is made available via the PMC Open Access Subset for unrestricted re-use and analyses in any form or by any means with acknowledgement of the original source. These permissions are granted for the duration of the COVID-19 pandemic or until permissions are revoked in writing. Upon expiration of these permissions, PMC is granted a perpetual license to make this article available via PMC and Europe PMC, consistent with existing copyright protections.

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FIGURE 3. — Molecular mechanisms of RBM mutations in SARS-CoV. A, surface plasmon resonance Biacore analysis of the binding interactions between hACE2 and wild-type or mutant hTor02 RBD. hACE2 was immobilized, and wild-type or mutant hTor02 RBD was flowed through. B, surface plasmon resonance Biacore analysis of the binding interactions between cACE2 and wild-type or mutant hTor02 RBD. cACE2 was immobilized, and wild-type or mutant hTor02 RBD was flowed through. C, pseudotyped viral infection assays of the interactions between different spike proteins and hACE2. D, pseudotyped viral infection assays of the interactions between different spike proteins and cACE2.