7wsh Citations

Cross-species recognition and molecular basis of SARS-CoV-2 and SARS-CoV binding to ACE2s of marine animals.

OpenAccess logo Natl Sci Rev 9 nwac122 (2022)
Related entries: 7wse, 7wsf, 7wsg

Cited: 5 times
EuropePMC logo PMID: 36187898

Abstract

Severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) has an extremely broad host range that includes hippopotami, which are phylogenetically closely related to whales. The cellular ACE2 receptor is one of the key determinants of the host range. Here, we found that ACE2s from several marine mammals and hippopotami could efficiently bind to the receptor-binding domain (RBD) of both SARS-CoV and SARS-CoV-2 and facilitate the transduction of SARS-CoV and SARS-CoV-2 pseudoviruses into ACE2-expressing cells. We further resolved the cryo-electron microscopy complex structures of the minke whale ACE2 and sea lion ACE2, respectively, bound to the RBDs, revealing that they have similar binding modes to human ACE2 when it comes to the SARS-CoV-2 RBD and SARS-CoV RBD. Our results indicate that marine mammals could potentially be new victims or virus carriers of SARS-CoV-2, which deserves further careful investigation and study. It will provide an early warning for the prospective monitoring of marine mammals.

Articles - 7wsh mentioned but not cited (1)

  1. Cross-species recognition and molecular basis of SARS-CoV-2 and SARS-CoV binding to ACE2s of marine animals. Li S, Yang R, Zhang D, Han P, Xu Z, Chen Q, Zhao R, Zhao X, Qu X, Zheng A, Wang L, Li L, Hu Y, Zhang R, Su C, Niu S, Zhang Y, Qi J, Liu K, Wang Q, Gao GF. Natl Sci Rev 9 nwac122 (2022)


Articles citing this publication (4)

  1. Beluga whale and bottlenose dolphin ACE2 proteins allow cell entry mediated by spike protein from three variants of SARS-CoV-2. Stone HM, Unal E, Romano TA, Turner PE. Biol Lett 19 20230321 (2023)
  2. Cryo-EM structures and binding of mouse and human ACE2 to SARS-CoV-2 variants of concern indicate that mutations enabling immune escape could expand host range. Ni D, Turelli P, Beckert B, Nazarov S, Uchikawa E, Myasnikov A, Pojer F, Trono D, Stahlberg H, Lau K. PLoS Pathog 19 e1011206 (2023)
  3. Structural basis for receptor binding and broader interspecies receptor recognition of currently circulating Omicron sub-variants. Zhao Z, Xie Y, Bai B, Luo C, Zhou J, Li W, Meng Y, Li L, Li D, Li X, Li X, Wang X, Sun J, Xu Z, Sun Y, Zhang W, Fan Z, Zhao X, Wu L, Ma J, Li OY, Shang G, Chai Y, Liu K, Wang P, Gao GF, Qi J. Nat Commun 14 4405 (2023)
  4. Structural basis of white-tailed deer, Odocoileus virginianus, ACE2 recognizing all the SARS-CoV-2 variants of concern with high affinity. Han P, Meng Y, Zhang D, Xu Z, Li Z, Pan X, Zhao Z, Li L, Tang L, Qi J, Liu K, Gao GF. J Virol 97 e0050523 (2023)