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. 2022 Jan 4;41(1):e109962. doi: 10.15252/embj.2021109962

Molecular basis of cross‐species ACE2 interactions with SARS‐CoV‐2‐like viruses of pangolin origin

Sheng Niu, Jia Wang, Bin Bai, Lili Wu, Anqi Zheng, Qian Chen, Pei Du, Pengcheng Han, Yanfang Zhang, Yunfei Jia, Chengpeng Qiao, Jianxun Qi, Wen‐xia Tian, Hong‐Wei Wang, Qihui Wang, George Fu Gao
PMCID: PMC8724768  PMID: 34981520

Abstract

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Correction to: The EMBO Journal (2021) 40: e107786. DOI 10.15252/embj.2021107786 | Published online 8 June 2021

The authors would like to add three references to the paper: Starr et al and Zahradník et al also reported that the Q498H or Q498R mutation has enhanced binding affinity to ACE2; and Liu et al reported on the binding of bat coronavirus to ACE2.

Starr et al and Zahradník et al have now been cited in the Discussion section, and the following sentence has been corrected from:

“According to our data, the SARS‐CoV‐2 RBD with Q498H increases the binding strength to hACE2 by 5‐fold, suggesting the Q498H mutant is more ready to interact with human receptor than the wildtype and highlighting the necessity for more strict control of virus and virus‐infected animals”.

to

“Here, according to our data and two recently published papers, the SARS‐CoV‐2 RBD with Q498H or Q498R increases the binding strength to hACE2 (Starr et al, 2020; Zahradník et al, 2021), suggesting the mutant with Q498H or Q498R is more ready to interact with human receptor than the wild type and highlighting the necessity for more strict control of virus and virus‐infected animals”.

The Liu et al citation has been added to the following sentence:

“In another paper published by our group recently, RaTG13 RBD was found to bind to hACE2 with much lower binding affinity than SARS‐CoV‐2 though RaTG13 displays the highest whole‐genome sequence identity (96.2%) with the SARS‐CoV‐2 (Liu et al, 2021)”.

Additionally, the authors have added the GISAID accession IDs to the sequence names of the SARS‐CoV‐2 in two human samples (Discussion section). To make identification unambiguous, the sequence names have been updated from “SA‐lsf‐27 and SA‐lsf‐37” to “GISAID accession ID: EPI_ISL_672581 and EPI_ISL_672589”.

Lastly, the authors declare in the Materials and Methods section that all experiments employed SARS‐CoV‐2 pseudovirus in cultured cells. These experiments were performed in a BSL‐2‐level laboratory and approved by Science and Technology Conditions Platform Office, Institute of Microbiology, Chinese Academy of Sciences.

These changes are herewith incorporated into the paper.

The EMBO Journal (2022) 41: e109962.

References

  1. Liu K, Pan X, Li L, Yu F, Zheng A, Du P, Han P, Meng Y, Zhang Y, Wu L et al (2021) Binding and molecular basis of the bat coronavirus RaTG13 virus to ACE2 in humans and other species. Cell 184: 3438–3451 [DOI] [PMC free article] [PubMed] [Google Scholar]
  2. Starr TN, Greaney AJ, Hilton SK, Ellis D, Crawford KHD, Dingens AS, Navarro MJ, Bowen JE, Tortorici MA, Walls AC et al (2020) Deep mutational scanning of SARS‐CoV‐2 receptor binding domain reveals constraints on folding and ACE2 binding. Cell 182: 1295–1310 [DOI] [PMC free article] [PubMed] [Google Scholar]
  3. Zahradník J, Marciano S, Shemesh M, Zoler E, Harari D, Chiaravalli J, Meyer B, Rudich Y, Li C, Marton I et al (2021) SARS‐CoV‐2 variant prediction and antiviral drug design are enabled by RBD in vitro evolution. Nat Microbiol 6: 1188–1198 [DOI] [PubMed] [Google Scholar]

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