Human Neonatal Fc Receptor Is the Cellular Uncoating Receptor for Enterovirus B

Enterovirus B (EV-B), a major proportion of the genus Enterovirus in the family Picornaviridae, is the causative agent of severe human infectious diseases. Although cellular receptors for coxsackievirus B in EV-B have been identified, receptors mediating virus entry, especially the uncoating process...

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Published inCell Vol. 177; no. 6; pp. 1553 - 1565.e16
Main Authors Zhao, Xin, Zhang, Guigen, Liu, Sheng, Chen, Xiangpeng, Peng, Ruchao, Dai, Lianpan, Qu, Xiao, Li, Shihua, Song, Hao, Gao, Zhengrong, Yuan, Pengfei, Liu, Zhiheng, Li, Changyao, Shang, Zifang, Li, Yan, Zhang, Meifan, Qi, Jianxun, Wang, Han, Du, Ning, Wu, Yan, Bi, Yuhai, Gao, Shan, Shi, Yi, Yan, Jinghua, Zhang, Yong, Xie, Zhengde, Wei, Wensheng, Gao, George F.
Format Journal Article
LanguageEnglish
Published United States Elsevier Inc 30.05.2019
Subjects
attachment
Capsid - metabolism
cryo-electron microscopy
cryo-EM
Cryoelectron Microscopy
echovirus
Enterovirus
Enterovirus B
Enterovirus B, Human - metabolism
Enterovirus B, Human - pathogenicity
Enterovirus Infections - metabolism
etiological agents
FcRn
Histocompatibility Antigens Class I - metabolism
Histocompatibility Antigens Class I - physiology
Histocompatibility Antigens Class I - ultrastructure
human neonatal Fc receptor
Humans
infectious diseases
Models, Molecular
Phylogeny
receptor
receptors
Receptors, Fc - metabolism
Receptors, Fc - physiology
Receptors, Fc - ultrastructure
uncoating
Virion
Virus Internalization
viruses
uncoating
receptor
enterovirus
attachment
FcRn
human neonatal Fc receptor
cryo-EM
echovirus
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Abstract Enterovirus B (EV-B), a major proportion of the genus Enterovirus in the family Picornaviridae, is the causative agent of severe human infectious diseases. Although cellular receptors for coxsackievirus B in EV-B have been identified, receptors mediating virus entry, especially the uncoating process of echovirus and other EV-B remain obscure. Here, we found that human neonatal Fc receptor (FcRn) is the uncoating receptor for major EV-B. FcRn binds to the virus particles in the “canyon” through its FCGRT subunit. By obtaining multiple cryo-electron microscopy structures at different stages of virus entry at atomic or near-atomic resolution, we deciphered the underlying mechanisms of enterovirus attachment and uncoating. These structures revealed that different from the attachment receptor CD55, binding of FcRn to the virions induces efficient release of “pocket factor” under acidic conditions and initiates the conformational changes in viral particle, providing a structural basis for understanding the mechanisms of enterovirus entry. [Display omitted] •CRISPR screening identified FcRn as an essential and universal EV-B receptor•FcRn facilitates EV-B uncoating and CD55 for attachment•High-resolution Cryo-EM structures described the mechanism of virus entry•The molecular mechanism of dual (attachment versus uncoating) receptor-usage was illustrated The human neonatal Fc receptor is the uncoating receptor that facilitates cellular viral entry for Enteroviruses, such as echovirus.
AbstractList Enterovirus B (EV-B), a major proportion of the genus Enterovirus in the family Picornaviridae, is the causative agent of severe human infectious diseases. Although cellular receptors for coxsackievirus B in EV-B have been identified, receptors mediating virus entry, especially the uncoating process of echovirus and other EV-B remain obscure. Here, we found that human neonatal Fc receptor (FcRn) is the uncoating receptor for major EV-B. FcRn binds to the virus particles in the “canyon” through its FCGRT subunit. By obtaining multiple cryo-electron microscopy structures at different stages of virus entry at atomic or near-atomic resolution, we deciphered the underlying mechanisms of enterovirus attachment and uncoating. These structures revealed that different from the attachment receptor CD55, binding of FcRn to the virions induces efficient release of “pocket factor” under acidic conditions and initiates the conformational changes in viral particle, providing a structural basis for understanding the mechanisms of enterovirus entry.
Enterovirus B (EV-B), a major proportion of the genus Enterovirus in the family Picornaviridae, is the causative agent of severe human infectious diseases. Although cellular receptors for coxsackievirus B in EV-B have been identified, receptors mediating virus entry, especially the uncoating process of echovirus and other EV-B remain obscure. Here, we found that human neonatal Fc receptor (FcRn) is the uncoating receptor for major EV-B. FcRn binds to the virus particles in the "canyon" through its FCGRT subunit. By obtaining multiple cryo-electron microscopy structures at different stages of virus entry at atomic or near-atomic resolution, we deciphered the underlying mechanisms of enterovirus attachment and uncoating. These structures revealed that different from the attachment receptor CD55, binding of FcRn to the virions induces efficient release of "pocket factor" under acidic conditions and initiates the conformational changes in viral particle, providing a structural basis for understanding the mechanisms of enterovirus entry.
Enterovirus B (EV-B), a major proportion of the genus Enterovirus in the family Picornaviridae , is the causative agent of severe human infectious diseases. Although cellular receptors for coxsackievirus B in EV-B have been identified, receptors mediating virus entry, especially the uncoating process of echovirus and other EV-B remain obscure. Here, we found that human neonatal Fc receptor (FcRn) is the uncoating receptor for major EV-B. FcRn binds to the virus particles in the “canyon” through its FCGRT subunit. By obtaining multiple cryo-electron microscopy structures at different stages of virus entry at atomic or near-atomic resolution, we deciphered the underlying mechanisms of enterovirus attachment and uncoating. These structures revealed that different from the attachment receptor CD55, binding of FcRn to the virions induces efficient release of “pocket factor” under acidic conditions and initiates the conformational changes in viral particle, providing a structural basis for understanding the mechanisms of enterovirus entry. • CRISPR screening identified FcRn as an essential and universal EV-B receptor • FcRn facilitates EV-B uncoating and CD55 for attachment • High-resolution Cryo-EM structures described the mechanism of virus entry • The molecular mechanism of dual (attachment versus uncoating) receptor-usage was illustrated The human neonatal Fc receptor is the uncoating receptor that facilitates cellular viral entry for Enteroviruses, such as echovirus.
Enterovirus B (EV-B), a major proportion of the genus Enterovirus in the family Picornaviridae, is the causative agent of severe human infectious diseases. Although cellular receptors for coxsackievirus B in EV-B have been identified, receptors mediating virus entry, especially the uncoating process of echovirus and other EV-B remain obscure. Here, we found that human neonatal Fc receptor (FcRn) is the uncoating receptor for major EV-B. FcRn binds to the virus particles in the "canyon" through its FCGRT subunit. By obtaining multiple cryo-electron microscopy structures at different stages of virus entry at atomic or near-atomic resolution, we deciphered the underlying mechanisms of enterovirus attachment and uncoating. These structures revealed that different from the attachment receptor CD55, binding of FcRn to the virions induces efficient release of "pocket factor" under acidic conditions and initiates the conformational changes in viral particle, providing a structural basis for understanding the mechanisms of enterovirus entry.Enterovirus B (EV-B), a major proportion of the genus Enterovirus in the family Picornaviridae, is the causative agent of severe human infectious diseases. Although cellular receptors for coxsackievirus B in EV-B have been identified, receptors mediating virus entry, especially the uncoating process of echovirus and other EV-B remain obscure. Here, we found that human neonatal Fc receptor (FcRn) is the uncoating receptor for major EV-B. FcRn binds to the virus particles in the "canyon" through its FCGRT subunit. By obtaining multiple cryo-electron microscopy structures at different stages of virus entry at atomic or near-atomic resolution, we deciphered the underlying mechanisms of enterovirus attachment and uncoating. These structures revealed that different from the attachment receptor CD55, binding of FcRn to the virions induces efficient release of "pocket factor" under acidic conditions and initiates the conformational changes in viral particle, providing a structural basis for understanding the mechanisms of enterovirus entry.
Enterovirus B (EV-B), a major proportion of the genus Enterovirus in the family Picornaviridae, is the causative agent of severe human infectious diseases. Although cellular receptors for coxsackievirus B in EV-B have been identified, receptors mediating virus entry, especially the uncoating process of echovirus and other EV-B remain obscure. Here, we found that human neonatal Fc receptor (FcRn) is the uncoating receptor for major EV-B. FcRn binds to the virus particles in the “canyon” through its FCGRT subunit. By obtaining multiple cryo-electron microscopy structures at different stages of virus entry at atomic or near-atomic resolution, we deciphered the underlying mechanisms of enterovirus attachment and uncoating. These structures revealed that different from the attachment receptor CD55, binding of FcRn to the virions induces efficient release of “pocket factor” under acidic conditions and initiates the conformational changes in viral particle, providing a structural basis for understanding the mechanisms of enterovirus entry. [Display omitted] •CRISPR screening identified FcRn as an essential and universal EV-B receptor•FcRn facilitates EV-B uncoating and CD55 for attachment•High-resolution Cryo-EM structures described the mechanism of virus entry•The molecular mechanism of dual (attachment versus uncoating) receptor-usage was illustrated The human neonatal Fc receptor is the uncoating receptor that facilitates cellular viral entry for Enteroviruses, such as echovirus.
Author Liu, Zhiheng
Shi, Yi
Dai, Lianpan
Xie, Zhengde
Chen, Xiangpeng
Qu, Xiao
Li, Changyao
Shang, Zifang
Song, Hao
Bi, Yuhai
Gao, George F.
Gao, Shan
Li, Shihua
Li, Yan
Yuan, Pengfei
Zhang, Meifan
Gao, Zhengrong
Liu, Sheng
Peng, Ruchao
Zhao, Xin
Zhang, Guigen
Qi, Jianxun
Wu, Yan
Wei, Wensheng
Yan, Jinghua
Wang, Han
Du, Ning
Zhang, Yong
AuthorAffiliation 11 CAS Key Laboratory of Microbial Physiological and Metabolic Engineering, Institute of Microbiology, Chinese Academy of Sciences, 100101 Beijing, China
10 CAS Key Laboratory of Bio-medical Diagnostics, Suzhou Institute of Biomedical Engineering and Technology, Chinese Academy of Sciences, 215163 Suzhou, China
8 EdiGene Inc, Life Science Park, 22 KeXueYuan Road, Changping District, 102206 Beijing, China
9 Academy for Advanced Interdisciplinary Studies, Peking University, 100871 Beijing, China
5 School of Life Sciences, University of Science and Technology of China, Hefei, 230026 Anhui, China
12 National Institute for Viral Disease Control and Prevention, Chinese Center for Disease Control and Prevention (China CDC), 102206 Beijing, China
3 Key Laboratory of Major Diseases in Children, Ministry of Education, National Clinical Research Center for Respiratory Diseases, Beijing Key Laboratory of Pediatric Respiratory Infection Diseases, Virology Laboratory, Beijing Pediatric Research Institute,
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BackLink https://www.ncbi.nlm.nih.gov/pubmed/31104841$$D View this record in MEDLINE/PubMed
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Issue 6
Keywords uncoating
receptor
enterovirus
attachment
FcRn
human neonatal Fc receptor
cryo-EM
echovirus
Language English
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Snippet Enterovirus B (EV-B), a major proportion of the genus Enterovirus in the family Picornaviridae, is the causative agent of severe human infectious diseases....
Enterovirus B (EV-B), a major proportion of the genus Enterovirus in the family Picornaviridae , is the causative agent of severe human infectious diseases....
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SubjectTerms attachment
Capsid - metabolism
cryo-electron microscopy
cryo-EM
Cryoelectron Microscopy
echovirus
Enterovirus
Enterovirus B
Enterovirus B, Human - metabolism
Enterovirus B, Human - pathogenicity
Enterovirus Infections - metabolism
etiological agents
FcRn
Histocompatibility Antigens Class I - metabolism
Histocompatibility Antigens Class I - physiology
Histocompatibility Antigens Class I - ultrastructure
human neonatal Fc receptor
Humans
infectious diseases
Models, Molecular
Phylogeny
receptor
receptors
Receptors, Fc - metabolism
Receptors, Fc - physiology
Receptors, Fc - ultrastructure
uncoating
Virion
Virus Internalization
viruses
Title Human Neonatal Fc Receptor Is the Cellular Uncoating Receptor for Enterovirus B
URI https://dx.doi.org/10.1016/j.cell.2019.04.035
https://www.ncbi.nlm.nih.gov/pubmed/31104841
https://www.proquest.com/docview/2232059005
https://www.proquest.com/docview/2286905565
https://pubmed.ncbi.nlm.nih.gov/PMC7111318
Volume 177
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