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Middle East respiratory syndrome coronavirus and bat coronavirus HKU9 both can utilize GRP78 for attachment onto host cells.

Identifieur interne : 000873 ( PubMed/Corpus ); précédent : 000872; suivant : 000874

Middle East respiratory syndrome coronavirus and bat coronavirus HKU9 both can utilize GRP78 for attachment onto host cells.

Auteurs : Hin Chu ; Che-Man Chan ; Xi Zhang ; Yixin Wang ; Shuofeng Yuan ; Jie Zhou ; Rex Kwok-Him Au-Yeung ; Kong-Hung Sze ; Dong Yang ; Huiping Shuai ; Yuxin Hou ; Cun Li ; Xiaoyu Zhao ; Vincent Kwok-Man Poon ; Sze Pui Leung ; Man-Lung Yeung ; Jinghua Yan ; Guangwen Lu ; Dong-Yan Jin ; George Fu Gao ; Jasper Fuk-Woo Chan ; Kwok-Yung Yuen

Source :

RBID : pubmed:29887526

English descriptors

Abstract

Coronavirus tropism is predominantly determined by the interaction between coronavirus spikes and the host receptors. In this regard, coronaviruses have evolved a complicated receptor-recognition system through their spike proteins. Spikes from highly related coronaviruses can recognize distinct receptors, whereas spikes of distant coronaviruses can employ the same cell-surface molecule for entry. Moreover, coronavirus spikes can recognize a broad range of cell-surface molecules in addition to the receptors and thereby can augment coronavirus attachment or entry. The receptor of Middle East respiratory syndrome coronavirus (MERS-CoV) is dipeptidyl peptidase 4 (DPP4). In this study, we identified membrane-associated 78-kDa glucose-regulated protein (GRP78) as an additional binding target of the MERS-CoV spike. Further analyses indicated that GRP78 could not independently render nonpermissive cells susceptible to MERS-CoV infection but could facilitate MERS-CoV entry into permissive cells by augmenting virus attachment. More importantly, by exploring potential interactions between GRP78 and spikes of other coronaviruses, we discovered that the highly conserved human GRP78 could interact with the spike protein of bat coronavirus HKU9 (bCoV-HKU9) and facilitate its attachment to the host cell surface. Taken together, our study has identified GRP78 as a host factor that can interact with the spike proteins of two Betacoronaviruses, the lineage C MERS-CoV and the lineage D bCoV-HKU9. The capacity of GRP78 to facilitate surface attachment of both a human coronavirus and a phylogenetically related bat coronavirus exemplifies the need for continuous surveillance of the evolution of animal coronaviruses to monitor their potential for human adaptations.

DOI: 10.1074/jbc.RA118.001897
PubMed: 29887526

Links to Exploration step

pubmed:29887526

Le document en format XML

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<name sortKey="Zhou, Jie" sort="Zhou, Jie" uniqKey="Zhou J" first="Jie" last="Zhou">Jie Zhou</name>
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<name sortKey="Au Yeung, Rex Kwok Him" sort="Au Yeung, Rex Kwok Him" uniqKey="Au Yeung R" first="Rex Kwok-Him" last="Au-Yeung">Rex Kwok-Him Au-Yeung</name>
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<name sortKey="Yang, Dong" sort="Yang, Dong" uniqKey="Yang D" first="Dong" last="Yang">Dong Yang</name>
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<name sortKey="Shuai, Huiping" sort="Shuai, Huiping" uniqKey="Shuai H" first="Huiping" last="Shuai">Huiping Shuai</name>
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<name sortKey="Hou, Yuxin" sort="Hou, Yuxin" uniqKey="Hou Y" first="Yuxin" last="Hou">Yuxin Hou</name>
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<name sortKey="Li, Cun" sort="Li, Cun" uniqKey="Li C" first="Cun" last="Li">Cun Li</name>
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<name sortKey="Zhao, Xiaoyu" sort="Zhao, Xiaoyu" uniqKey="Zhao X" first="Xiaoyu" last="Zhao">Xiaoyu Zhao</name>
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<name sortKey="Yan, Jinghua" sort="Yan, Jinghua" uniqKey="Yan J" first="Jinghua" last="Yan">Jinghua Yan</name>
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<nlm:affiliation>the CAS Key Laboratory of Pathogenic Microbiology and Immunology, Institute of Microbiology, Chinese Academy of Sciences, Beijing 100101.</nlm:affiliation>
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<name sortKey="Chan, Jasper Fuk Woo" sort="Chan, Jasper Fuk Woo" uniqKey="Chan J" first="Jasper Fuk-Woo" last="Chan">Jasper Fuk-Woo Chan</name>
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<nlm:affiliation>From the State Key Laboratory of Emerging Infectious Diseases, jfwchan@hku.hk.</nlm:affiliation>
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<name sortKey="Yuen, Kwok Yung" sort="Yuen, Kwok Yung" uniqKey="Yuen K" first="Kwok-Yung" last="Yuen">Kwok-Yung Yuen</name>
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<term>Betacoronavirus (physiology)</term>
<term>Cell Line</term>
<term>Chlorocebus aethiops</term>
<term>Coronavirus (physiology)</term>
<term>Coronavirus Infections (metabolism)</term>
<term>Dipeptidyl Peptidase 4 (metabolism)</term>
<term>Heat-Shock Proteins (metabolism)</term>
<term>Host-Pathogen Interactions</term>
<term>Humans</term>
<term>Middle East Respiratory Syndrome Coronavirus (physiology)</term>
<term>Protein Interaction Maps</term>
<term>Receptors, Virus (metabolism)</term>
<term>Spike Glycoprotein, Coronavirus (metabolism)</term>
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<term>Dipeptidyl Peptidase 4</term>
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<term>Receptors, Virus</term>
<term>Spike Glycoprotein, Coronavirus</term>
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<term>Coronavirus Infections</term>
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<term>Middle East Respiratory Syndrome Coronavirus</term>
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<term>Cell Line</term>
<term>Chlorocebus aethiops</term>
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<div type="abstract" xml:lang="en">Coronavirus tropism is predominantly determined by the interaction between coronavirus spikes and the host receptors. In this regard, coronaviruses have evolved a complicated receptor-recognition system through their spike proteins. Spikes from highly related coronaviruses can recognize distinct receptors, whereas spikes of distant coronaviruses can employ the same cell-surface molecule for entry. Moreover, coronavirus spikes can recognize a broad range of cell-surface molecules in addition to the receptors and thereby can augment coronavirus attachment or entry. The receptor of Middle East respiratory syndrome coronavirus (MERS-CoV) is dipeptidyl peptidase 4 (DPP4). In this study, we identified membrane-associated 78-kDa glucose-regulated protein (GRP78) as an additional binding target of the MERS-CoV spike. Further analyses indicated that GRP78 could not independently render nonpermissive cells susceptible to MERS-CoV infection but could facilitate MERS-CoV entry into permissive cells by augmenting virus attachment. More importantly, by exploring potential interactions between GRP78 and spikes of other coronaviruses, we discovered that the highly conserved human GRP78 could interact with the spike protein of bat coronavirus HKU9 (bCoV-HKU9) and facilitate its attachment to the host cell surface. Taken together, our study has identified GRP78 as a host factor that can interact with the spike proteins of two
<i>Betacoronaviruses</i>
, the lineage C MERS-CoV and the lineage D bCoV-HKU9. The capacity of GRP78 to facilitate surface attachment of both a human coronavirus and a phylogenetically related bat coronavirus exemplifies the need for continuous surveillance of the evolution of animal coronaviruses to monitor their potential for human adaptations.</div>
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<AbstractText>Coronavirus tropism is predominantly determined by the interaction between coronavirus spikes and the host receptors. In this regard, coronaviruses have evolved a complicated receptor-recognition system through their spike proteins. Spikes from highly related coronaviruses can recognize distinct receptors, whereas spikes of distant coronaviruses can employ the same cell-surface molecule for entry. Moreover, coronavirus spikes can recognize a broad range of cell-surface molecules in addition to the receptors and thereby can augment coronavirus attachment or entry. The receptor of Middle East respiratory syndrome coronavirus (MERS-CoV) is dipeptidyl peptidase 4 (DPP4). In this study, we identified membrane-associated 78-kDa glucose-regulated protein (GRP78) as an additional binding target of the MERS-CoV spike. Further analyses indicated that GRP78 could not independently render nonpermissive cells susceptible to MERS-CoV infection but could facilitate MERS-CoV entry into permissive cells by augmenting virus attachment. More importantly, by exploring potential interactions between GRP78 and spikes of other coronaviruses, we discovered that the highly conserved human GRP78 could interact with the spike protein of bat coronavirus HKU9 (bCoV-HKU9) and facilitate its attachment to the host cell surface. Taken together, our study has identified GRP78 as a host factor that can interact with the spike proteins of two
<i>Betacoronaviruses</i>
, the lineage C MERS-CoV and the lineage D bCoV-HKU9. The capacity of GRP78 to facilitate surface attachment of both a human coronavirus and a phylogenetically related bat coronavirus exemplifies the need for continuous surveillance of the evolution of animal coronaviruses to monitor their potential for human adaptations.</AbstractText>
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