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Postfusion structure of human-infecting Bourbon virus envelope glycoprotein.

Abstract

Thogotoviruses are important zoonotic viruses infecting a variety of domestic animals, as well as humans. Among these viruses, Bourbon virus (BRBV) is one of the several human-infecting members, which emerged in the US in recent years and caused human deaths. Here, we report the crystal structure of the BRBV envelope glycoprotein in the postfusion conformation. The structure adopts the typical fold of a class III viral fusion protein and displays an extensive positively charged electrostatic potential pattern, which resembles the glycoprotein of Dhori virus and is consistent with our previous predictions. In addition, compared to other previously defined class III viral fusion proteins, the structures of all thogotovirus glycoproteins and homologs are more similar to herpes virus glycoprotein Bs than to the rhabdovirus G proteins. Thus, class III viral fusion proteins are quite diverse in structure, and sub-classes may have developed during evolution.

Authors+Show Affiliations

CAS Key Laboratory of Pathogenic Microbiology and Immunology, Institute of Microbiology, Chinese Academy of Sciences, Beijing 100101, China; Central Laboratory, Chinese Medicine Hospital of Shanxi Province, Taiyuan 030012, 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; 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; 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; 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; National Institute for Viral Disease Control and Prevention, Chinese Center for Disease Control and Prevention (China CDC), Beijing 102206, China.CAS Key Laboratory of Pathogenic Microbiology and Immunology, Institute of Microbiology, Chinese Academy of Sciences, Beijing 100101, China.Tianjin Institute of Industrial Biotechnology, Chinese Academy of Sciences, Tianjin 300308, China. Electronic address: gaofeng@tib.cas.cn.

Pub Type(s)

Journal Article

Language

eng

PubMed ID

31419524

Citation

Bai, Chongzhi, et al. "Postfusion Structure of Human-infecting Bourbon Virus Envelope Glycoprotein." Journal of Structural Biology, 2019.
Bai C, Qi J, Wu Y, et al. Postfusion structure of human-infecting Bourbon virus envelope glycoprotein. J Struct Biol. 2019.
Bai, C., Qi, J., Wu, Y., Wang, X., Gao, G. F., Peng, R., & Gao, F. (2019). Postfusion structure of human-infecting Bourbon virus envelope glycoprotein. Journal of Structural Biology, doi:10.1016/j.jsb.2019.08.005.
Bai C, et al. Postfusion Structure of Human-infecting Bourbon Virus Envelope Glycoprotein. J Struct Biol. 2019 Aug 13; PubMed PMID: 31419524.
* Article titles in AMA citation format should be in sentence-case
TY - JOUR T1 - Postfusion structure of human-infecting Bourbon virus envelope glycoprotein. AU - Bai,Chongzhi, AU - Qi,Jianxun, AU - Wu,Yan, AU - Wang,Xinjie, AU - Gao,George Fu, AU - Peng,Ruchao, AU - Gao,Feng, Y1 - 2019/08/13/ PY - 2019/04/18/received PY - 2019/08/10/revised PY - 2019/08/12/accepted PY - 2019/8/17/pubmed PY - 2019/8/17/medline PY - 2019/8/17/entrez KW - Bourbon virus (BRBV) KW - Crystal structure KW - Fusion protein KW - Thogotoviruses JF - Journal of structural biology JO - J. Struct. Biol. N2 - Thogotoviruses are important zoonotic viruses infecting a variety of domestic animals, as well as humans. Among these viruses, Bourbon virus (BRBV) is one of the several human-infecting members, which emerged in the US in recent years and caused human deaths. Here, we report the crystal structure of the BRBV envelope glycoprotein in the postfusion conformation. The structure adopts the typical fold of a class III viral fusion protein and displays an extensive positively charged electrostatic potential pattern, which resembles the glycoprotein of Dhori virus and is consistent with our previous predictions. In addition, compared to other previously defined class III viral fusion proteins, the structures of all thogotovirus glycoproteins and homologs are more similar to herpes virus glycoprotein Bs than to the rhabdovirus G proteins. Thus, class III viral fusion proteins are quite diverse in structure, and sub-classes may have developed during evolution. SN - 1095-8657 UR - https://www.unboundmedicine.com/medline/citation/31419524/Postfusion_structure_of_human-infecting_Bourbon_virus_envelope_glycoprotein L2 - https://linkinghub.elsevier.com/retrieve/pii/S1047-8477(19)30175-3 DB - PRIME DP - Unbound Medicine ER -