Tags

Type your tag names separated by a space and hit enter

Structure of the S1 subunit C-terminal domain from bat-derived coronavirus HKU5 spike protein.
Virology. 2017 07; 507:101-109.V

Abstract

Accumulating evidence indicates that MERS-CoV originated from bat coronaviruses (BatCoVs). Previously, we demonstrated that both MERS-CoV and BatCoV HKU4 use CD26 as a receptor, but how the BatCoVs evolved to bind CD26 is an intriguing question. Here, we solved the crystal structure of the S1 subunit C-terminal domain of HKU5 (HKU5-CTD), another BatCoV that is phylogenetically related to MERS-CoV but cannot bind to CD26. We observed that the conserved core subdomain and those of other betacoronaviruses (betaCoVs) have a similar topology of the external subdomain, indicating the same ancestor of lineage C betaCoVs. However, two deletions in two respective loops located in HKU5-CTD result in conformational variations in CD26-binding interface and are responsible for the non-binding of HKU5-CTD to CD26. Combined with sequence variation in the HKU5-CTD receptor binding interface, we propose the necessity for surveilling the mutation in BatCoV HKU5 spike protein in case of bat-to-human interspecies transmission.

Authors+Show Affiliations

CAS Key Laboratory of Pathogenic Microbiology and Immunology, Institute of Microbiology, Chinese Academy of Sciences, Beijing 100101, China; University of Chinese Academy of Sciences, Beijing 100049, China.CAS Key Laboratory of Pathogenic Microbiology and Immunology, Institute of Microbiology, Chinese Academy of Sciences, Beijing 100101, China.CAS Key Laboratory of Pathogenic Microbiology and Immunology, Institute of Microbiology, Chinese Academy of Sciences, Beijing 100101, China; Research Network of Immunity and Health (RNIH), Beijing Institutes of Life Science, Chinese Academy of Sciences, Beijing 100101, China.CAS Key Laboratory of Microbial Physiological and Metabolic Engineering, Institute of Microbiology, Chinese Academy of Sciences, Beijing 100101, China; Shenzhen Key Laboratory of Pathogen and Immunity, Shenzhen Third People's Hospital, Shenzhen 518112, China.CAS Key Laboratory of Pathogenic Microbiology and Immunology, Institute of Microbiology, Chinese Academy of Sciences, Beijing 100101, China; University of Chinese Academy of Sciences, Beijing 100049, China.Shenzhen Key Laboratory of Pathogen and Immunity, Shenzhen Third People's Hospital, Shenzhen 518112, China; School of Basic Medical Sciences, Wuhan University, Wuhan 430071, China.West China Hospital Emergency Department (WCHED), State Key Laboratory of Biotherapy, West China Hospital, Sichuan University, and Collaborative Innovation Center of Biotherapy, Chengdu, Sichuan 610041, China.State Key Laboratory for Emerging Infectious Diseases, The University of Hong Kong, Pokfulam 999077, Hong Kong Special Administration Region; Department of Microbiology, The University of Hong Kong, Pokfulam 999077, Hong Kong Special Administration Region; Collaborative Innovation Center for Diagnosis and Treatment of Infectious Diseases, Zhejiang University, Hangzhou 310003, China.CAS Key Laboratory of Pathogenic Microbiology and Immunology, Institute of Microbiology, Chinese Academy of Sciences, Beijing 100101, China; University of Chinese Academy of Sciences, Beijing 100049, China; Shenzhen Key Laboratory of Pathogen and Immunity, Shenzhen Third People's Hospital, Shenzhen 518112, China; Center for Influenza Research and Early-warning (CASCIRE), Chinese Academy of Sciences, Beijing 100101, China. Electronic address: shiyi@im.ac.cn.CAS Key Laboratory of Pathogenic Microbiology and Immunology, Institute of Microbiology, Chinese Academy of Sciences, Beijing 100101, China; University of Chinese Academy of Sciences, Beijing 100049, China; Research Network of Immunity and Health (RNIH), Beijing Institutes of Life Science, Chinese Academy of Sciences, Beijing 100101, China; Shenzhen Key Laboratory of Pathogen and Immunity, Shenzhen Third People's Hospital, Shenzhen 518112, China; Collaborative Innovation Center for Diagnosis and Treatment of Infectious Diseases, Zhejiang University, Hangzhou 310003, China; Center for Influenza Research and Early-warning (CASCIRE), Chinese Academy of Sciences, Beijing 100101, China; National Institute for Viral Disease Control and Prevention, Chinese Center for Disease Control and Prevention (China CDC), Beijing 102206, China. Electronic address: gaof@im.ac.cn.

Pub Type(s)

Journal Article
Research Support, Non-U.S. Gov't

Language

eng

PubMed ID

28432925

Citation

Han, Xue, et al. "Structure of the S1 Subunit C-terminal Domain From Bat-derived Coronavirus HKU5 Spike Protein." Virology, vol. 507, 2017, pp. 101-109.
Han X, Qi J, Song H, et al. Structure of the S1 subunit C-terminal domain from bat-derived coronavirus HKU5 spike protein. Virology. 2017;507:101-109.
Han, X., Qi, J., Song, H., Wang, Q., Zhang, Y., Wu, Y., Lu, G., Yuen, K. Y., Shi, Y., & Gao, G. F. (2017). Structure of the S1 subunit C-terminal domain from bat-derived coronavirus HKU5 spike protein. Virology, 507, 101-109. https://doi.org/10.1016/j.virol.2017.04.016
Han X, et al. Structure of the S1 Subunit C-terminal Domain From Bat-derived Coronavirus HKU5 Spike Protein. Virology. 2017;507:101-109. PubMed PMID: 28432925.
* Article titles in AMA citation format should be in sentence-case
TY - JOUR T1 - Structure of the S1 subunit C-terminal domain from bat-derived coronavirus HKU5 spike protein. AU - Han,Xue, AU - Qi,Jianxun, AU - Song,Hao, AU - Wang,Qihui, AU - Zhang,Yanfang, AU - Wu,Ying, AU - Lu,Guangwen, AU - Yuen,Kwok-Yung, AU - Shi,Yi, AU - Gao,George F, Y1 - 2017/04/19/ PY - 2017/03/12/received PY - 2017/04/10/revised PY - 2017/04/15/accepted PY - 2017/4/23/pubmed PY - 2017/7/18/medline PY - 2017/4/23/entrez KW - BatCoV HKU5 KW - CTD KW - Crystal structure KW - Evolution KW - MERS-CoV SP - 101 EP - 109 JF - Virology JO - Virology VL - 507 N2 - Accumulating evidence indicates that MERS-CoV originated from bat coronaviruses (BatCoVs). Previously, we demonstrated that both MERS-CoV and BatCoV HKU4 use CD26 as a receptor, but how the BatCoVs evolved to bind CD26 is an intriguing question. Here, we solved the crystal structure of the S1 subunit C-terminal domain of HKU5 (HKU5-CTD), another BatCoV that is phylogenetically related to MERS-CoV but cannot bind to CD26. We observed that the conserved core subdomain and those of other betacoronaviruses (betaCoVs) have a similar topology of the external subdomain, indicating the same ancestor of lineage C betaCoVs. However, two deletions in two respective loops located in HKU5-CTD result in conformational variations in CD26-binding interface and are responsible for the non-binding of HKU5-CTD to CD26. Combined with sequence variation in the HKU5-CTD receptor binding interface, we propose the necessity for surveilling the mutation in BatCoV HKU5 spike protein in case of bat-to-human interspecies transmission. SN - 1096-0341 UR - https://www.unboundmedicine.com/medline/citation/28432925/Structure_of_the_S1_subunit_C_terminal_domain_from_bat_derived_coronavirus_HKU5_spike_protein_ L2 - https://linkinghub.elsevier.com/retrieve/pii/S0042-6822(17)30124-1 DB - PRIME DP - Unbound Medicine ER -