The TGEV Membrane Protein Interacts with HSC70 To Direct Virus Internalization through Clathrin-Mediated Endocytosis
Coronavirus membrane protein is a major component of the viral envelope and plays a central role in the viral life cycle. Studies of the coronavirus membrane protein (M) have mainly focused on its role in viral assembly and budding, but whether M protein is involved in the initial stage of viral rep...
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creator | Ji, Zhaoyang Dong, Hui Jiao, Ruixue Zhu, Xiaoyuan Shi, Hongyan Chen, Jianfei Shi, Da Liu, Jianbo Jing, Zhaoyang Zhang, Jialin Wang, Xiaobo Ye, Dandan Zhang, Jiyu Zhang, Xin Feng, Li |
description | Coronavirus membrane protein is a major component of the viral envelope and plays a central role in the viral life cycle. Studies of the coronavirus membrane protein (M) have mainly focused on its role in viral assembly and budding, but whether M protein is involved in the initial stage of viral replication remains unclear. In this study, eight proteins in transmissible gastroenteritis virus (TGEV)-infected cells coimmunoprecipitated with monoclonal antibodies (MAb) against M protein in PK-15 cells, heat shock cognate protein 70 (HSC70), and clathrin were identified by matrix-assisted laser desorption ionization-tandem time of flight mass spectrometry (MALDI-TOF MS). Further studies demonstrated that HSC70 and TGEV M colocalized on the cell surface in early stages of TGEV infection; specifically, HSC70 bound M protein through its substrate-binding domain (SBD) and preincubation of TGEV with anti-M serum to block the interaction of M and HSC70 reduced the internalization of TGEV, thus demonstrating that the M-HSC70 interaction mediates the internalization of TGEV. Remarkably, the process of internalization was dependent on clathrin-mediated endocytosis (CME) in PK-15 cells. Furthermore, inhibition of the ATPase activity of HSC70 reduced the efficiency of CME. Collectively, our results indicated that HSC70 is a newly identified host factor involved in TGEV infection. Taken together, our findings clearly illustrate a novel role for TGEV M protein in the viral life cycle and present a unique strategy used by HSC70 to promote TGEV infection in which the interaction with M protein directs viral internalization. These studies provide new insights into the life cycle of coronaviruses.
TGEV is the causative agent of porcine diarrhea, a viral disease that economically affects the pig industry in many countries. However, the molecular mechanisms underlying viral replication remain incompletely understood. Here, we provide evidence of a previously undescribed role of M protein in viral replication during early stages. We also identified HSC70 as a new host factor affecting TGEV infection. We demonstrate that the interaction between M and HSC70 directs TGEV internalization in a manner dependent on CME, thus revealing a novel mechanism for TGEV replication. We believe that this study may change our understanding of the first steps of infection of cells with coronavirus. This study should facilitate the development of anti-TGEV therapeutic agents by targeting the host fa |
doi_str_mv | 10.1128/jvi.00128-23 |
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TGEV is the causative agent of porcine diarrhea, a viral disease that economically affects the pig industry in many countries. However, the molecular mechanisms underlying viral replication remain incompletely understood. Here, we provide evidence of a previously undescribed role of M protein in viral replication during early stages. We also identified HSC70 as a new host factor affecting TGEV infection. We demonstrate that the interaction between M and HSC70 directs TGEV internalization in a manner dependent on CME, thus revealing a novel mechanism for TGEV replication. We believe that this study may change our understanding of the first steps of infection of cells with coronavirus. This study should facilitate the development of anti-TGEV therapeutic agents by targeting the host factors and may provide a new strategy for the control of porcine diarrhea.</description><identifier>ISSN: 0022-538X</identifier><identifier>ISSN: 1098-5514</identifier><identifier>EISSN: 1098-5514</identifier><identifier>DOI: 10.1128/jvi.00128-23</identifier><identifier>PMID: 36975782</identifier><language>eng</language><publisher>United States: American Society for Microbiology</publisher><subject>Animals ; Cell Line ; Clathrin ; Clathrin - metabolism ; clathrin-mediated endocytosis ; Coronavirus ; Coronavirus Infections ; Coronavirus M Proteins ; Coronavirus M Proteins - metabolism ; Diarrhea ; Endocytosis ; Host-Microbial Interactions ; HSC70 ; HSC70 Heat-Shock Proteins ; HSP70 Heat-Shock Proteins ; Humans ; Immunology ; Insect Science ; internalization ; Life sciences ; membrane protein ; Membrane Proteins ; Microbiology ; Médecine vétérinaire & santé animale ; Sciences du vivant ; Swine ; transmissible gastroenteritis virus ; Transmissible gastroenteritis virus - physiology ; Veterinary medicine & animal health ; Virology ; Virus Internalization ; Virus Replication ; Virus-Cell Interactions</subject><ispartof>Journal of virology, 2023-04, Vol.97 (4), p.e0012823-e0012823</ispartof><rights>Copyright © 2023 Ji et al.</rights><rights>Copyright © 2023 Ji et al. 2023 Ji et al.</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-a463t-9c8d9d91f0a87fec8cd3ae262e9d6bdd5897152096b95e614fb3cb675f6c8f673</citedby><cites>FETCH-LOGICAL-a463t-9c8d9d91f0a87fec8cd3ae262e9d6bdd5897152096b95e614fb3cb675f6c8f673</cites><orcidid>0000-0003-4123-0892</orcidid></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://www.ncbi.nlm.nih.gov/pmc/articles/PMC10134871/pdf/$$EPDF$$P50$$Gpubmedcentral$$Hfree_for_read</linktopdf><linktohtml>$$Uhttps://www.ncbi.nlm.nih.gov/pmc/articles/PMC10134871/$$EHTML$$P50$$Gpubmedcentral$$Hfree_for_read</linktohtml><link.rule.ids>230,314,727,780,784,885,27924,27925,53791,53793</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/36975782$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><contributor>Gallagher, Tom</contributor><creatorcontrib>Ji, Zhaoyang</creatorcontrib><creatorcontrib>Dong, Hui</creatorcontrib><creatorcontrib>Jiao, Ruixue</creatorcontrib><creatorcontrib>Zhu, Xiaoyuan</creatorcontrib><creatorcontrib>Shi, Hongyan</creatorcontrib><creatorcontrib>Chen, Jianfei</creatorcontrib><creatorcontrib>Shi, Da</creatorcontrib><creatorcontrib>Liu, Jianbo</creatorcontrib><creatorcontrib>Jing, Zhaoyang</creatorcontrib><creatorcontrib>Zhang, Jialin</creatorcontrib><creatorcontrib>Wang, Xiaobo</creatorcontrib><creatorcontrib>Ye, Dandan</creatorcontrib><creatorcontrib>Zhang, Jiyu</creatorcontrib><creatorcontrib>Zhang, Xin</creatorcontrib><creatorcontrib>Feng, Li</creatorcontrib><title>The TGEV Membrane Protein Interacts with HSC70 To Direct Virus Internalization through Clathrin-Mediated Endocytosis</title><title>Journal of virology</title><addtitle>J Virol</addtitle><addtitle>J Virol</addtitle><description>Coronavirus membrane protein is a major component of the viral envelope and plays a central role in the viral life cycle. Studies of the coronavirus membrane protein (M) have mainly focused on its role in viral assembly and budding, but whether M protein is involved in the initial stage of viral replication remains unclear. In this study, eight proteins in transmissible gastroenteritis virus (TGEV)-infected cells coimmunoprecipitated with monoclonal antibodies (MAb) against M protein in PK-15 cells, heat shock cognate protein 70 (HSC70), and clathrin were identified by matrix-assisted laser desorption ionization-tandem time of flight mass spectrometry (MALDI-TOF MS). Further studies demonstrated that HSC70 and TGEV M colocalized on the cell surface in early stages of TGEV infection; specifically, HSC70 bound M protein through its substrate-binding domain (SBD) and preincubation of TGEV with anti-M serum to block the interaction of M and HSC70 reduced the internalization of TGEV, thus demonstrating that the M-HSC70 interaction mediates the internalization of TGEV. Remarkably, the process of internalization was dependent on clathrin-mediated endocytosis (CME) in PK-15 cells. Furthermore, inhibition of the ATPase activity of HSC70 reduced the efficiency of CME. Collectively, our results indicated that HSC70 is a newly identified host factor involved in TGEV infection. Taken together, our findings clearly illustrate a novel role for TGEV M protein in the viral life cycle and present a unique strategy used by HSC70 to promote TGEV infection in which the interaction with M protein directs viral internalization. These studies provide new insights into the life cycle of coronaviruses.
TGEV is the causative agent of porcine diarrhea, a viral disease that economically affects the pig industry in many countries. However, the molecular mechanisms underlying viral replication remain incompletely understood. Here, we provide evidence of a previously undescribed role of M protein in viral replication during early stages. We also identified HSC70 as a new host factor affecting TGEV infection. We demonstrate that the interaction between M and HSC70 directs TGEV internalization in a manner dependent on CME, thus revealing a novel mechanism for TGEV replication. We believe that this study may change our understanding of the first steps of infection of cells with coronavirus. This study should facilitate the development of anti-TGEV therapeutic agents by targeting the host factors and may provide a new strategy for the control of porcine diarrhea.</description><subject>Animals</subject><subject>Cell Line</subject><subject>Clathrin</subject><subject>Clathrin - metabolism</subject><subject>clathrin-mediated endocytosis</subject><subject>Coronavirus</subject><subject>Coronavirus Infections</subject><subject>Coronavirus M Proteins</subject><subject>Coronavirus M Proteins - metabolism</subject><subject>Diarrhea</subject><subject>Endocytosis</subject><subject>Host-Microbial Interactions</subject><subject>HSC70</subject><subject>HSC70 Heat-Shock Proteins</subject><subject>HSP70 Heat-Shock Proteins</subject><subject>Humans</subject><subject>Immunology</subject><subject>Insect Science</subject><subject>internalization</subject><subject>Life sciences</subject><subject>membrane protein</subject><subject>Membrane Proteins</subject><subject>Microbiology</subject><subject>Médecine vétérinaire & santé animale</subject><subject>Sciences du vivant</subject><subject>Swine</subject><subject>transmissible gastroenteritis virus</subject><subject>Transmissible gastroenteritis virus - physiology</subject><subject>Veterinary medicine & animal health</subject><subject>Virology</subject><subject>Virus Internalization</subject><subject>Virus Replication</subject><subject>Virus-Cell Interactions</subject><issn>0022-538X</issn><issn>1098-5514</issn><issn>1098-5514</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2023</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNp1kUtv1DAUhS0EokNhxxp5CVJT_Ej8WCE0DG2lViAxVOwsx7mZeJSJi-1MVX496aRUsGDlI_m75z4OQq8pOaWUqffbvT8lZFIF40_QghKtiqqi5VO0IISxouLqxxF6kdJ2ospSlM_RERdaVlKxBcrrDvD6bHWNr2BXRzsA_hpDBj_giyFDtC4nfOtzh8-_LSXB64A_-Qgu42sfxzRDg-39L5t9GHDuYhg3HV72dpJ-KK6g8TZDg1dDE9xdDsmnl-hZa_sErx7eY_T982q9PC8uv5xdLD9eFrYUPBfaqUY3mrbEKtmCU67hFphgoBtRN02ltKQVI1rUugJBy7bmrhayaoVTrZD8GH2YfW_GegeNgyFH25ub6Hc23plgvfn3Z_Cd2YS9oYTyUkk6OfDZofewARNi7c2eHSoPeuw3xjpTg2FMKMNpSZSeqt4-9I3h5wgpm51PDvp-Om8Yk2GKSE0lY2xCT2bUxZBShPZxOkrMfb5mytcc8jWMT_i7Gbdpx8w2jPe3T_9j3_y9_aPxn_D5b3oIr-M</recordid><startdate>20230427</startdate><enddate>20230427</enddate><creator>Ji, Zhaoyang</creator><creator>Dong, Hui</creator><creator>Jiao, Ruixue</creator><creator>Zhu, Xiaoyuan</creator><creator>Shi, Hongyan</creator><creator>Chen, Jianfei</creator><creator>Shi, Da</creator><creator>Liu, Jianbo</creator><creator>Jing, Zhaoyang</creator><creator>Zhang, Jialin</creator><creator>Wang, Xiaobo</creator><creator>Ye, Dandan</creator><creator>Zhang, Jiyu</creator><creator>Zhang, Xin</creator><creator>Feng, Li</creator><general>American Society for Microbiology</general><scope>CGR</scope><scope>CUY</scope><scope>CVF</scope><scope>ECM</scope><scope>EIF</scope><scope>NPM</scope><scope>AAYXX</scope><scope>CITATION</scope><scope>7X8</scope><scope>Q33</scope><scope>5PM</scope><orcidid>https://orcid.org/0000-0003-4123-0892</orcidid></search><sort><creationdate>20230427</creationdate><title>The TGEV Membrane Protein Interacts with HSC70 To Direct Virus Internalization through Clathrin-Mediated Endocytosis</title><author>Ji, Zhaoyang ; Dong, Hui ; Jiao, Ruixue ; Zhu, Xiaoyuan ; Shi, Hongyan ; Chen, Jianfei ; Shi, Da ; Liu, Jianbo ; Jing, Zhaoyang ; Zhang, Jialin ; Wang, Xiaobo ; Ye, Dandan ; Zhang, Jiyu ; Zhang, Xin ; Feng, Li</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-a463t-9c8d9d91f0a87fec8cd3ae262e9d6bdd5897152096b95e614fb3cb675f6c8f673</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2023</creationdate><topic>Animals</topic><topic>Cell Line</topic><topic>Clathrin</topic><topic>Clathrin - metabolism</topic><topic>clathrin-mediated endocytosis</topic><topic>Coronavirus</topic><topic>Coronavirus Infections</topic><topic>Coronavirus M Proteins</topic><topic>Coronavirus M Proteins - metabolism</topic><topic>Diarrhea</topic><topic>Endocytosis</topic><topic>Host-Microbial Interactions</topic><topic>HSC70</topic><topic>HSC70 Heat-Shock Proteins</topic><topic>HSP70 Heat-Shock Proteins</topic><topic>Humans</topic><topic>Immunology</topic><topic>Insect Science</topic><topic>internalization</topic><topic>Life sciences</topic><topic>membrane protein</topic><topic>Membrane Proteins</topic><topic>Microbiology</topic><topic>Médecine vétérinaire & santé animale</topic><topic>Sciences du vivant</topic><topic>Swine</topic><topic>transmissible gastroenteritis virus</topic><topic>Transmissible gastroenteritis virus - physiology</topic><topic>Veterinary medicine & animal health</topic><topic>Virology</topic><topic>Virus Internalization</topic><topic>Virus Replication</topic><topic>Virus-Cell Interactions</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Ji, Zhaoyang</creatorcontrib><creatorcontrib>Dong, Hui</creatorcontrib><creatorcontrib>Jiao, Ruixue</creatorcontrib><creatorcontrib>Zhu, Xiaoyuan</creatorcontrib><creatorcontrib>Shi, Hongyan</creatorcontrib><creatorcontrib>Chen, Jianfei</creatorcontrib><creatorcontrib>Shi, Da</creatorcontrib><creatorcontrib>Liu, Jianbo</creatorcontrib><creatorcontrib>Jing, Zhaoyang</creatorcontrib><creatorcontrib>Zhang, Jialin</creatorcontrib><creatorcontrib>Wang, Xiaobo</creatorcontrib><creatorcontrib>Ye, Dandan</creatorcontrib><creatorcontrib>Zhang, Jiyu</creatorcontrib><creatorcontrib>Zhang, Xin</creatorcontrib><creatorcontrib>Feng, Li</creatorcontrib><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>MEDLINE - Academic</collection><collection>Université de Liège - Open Repository and Bibliography (ORBI)</collection><collection>PubMed Central (Full Participant titles)</collection><jtitle>Journal of virology</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Ji, Zhaoyang</au><au>Dong, Hui</au><au>Jiao, Ruixue</au><au>Zhu, Xiaoyuan</au><au>Shi, Hongyan</au><au>Chen, Jianfei</au><au>Shi, Da</au><au>Liu, Jianbo</au><au>Jing, Zhaoyang</au><au>Zhang, Jialin</au><au>Wang, Xiaobo</au><au>Ye, Dandan</au><au>Zhang, Jiyu</au><au>Zhang, Xin</au><au>Feng, Li</au><au>Gallagher, Tom</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>The TGEV Membrane Protein Interacts with HSC70 To Direct Virus Internalization through Clathrin-Mediated Endocytosis</atitle><jtitle>Journal of virology</jtitle><stitle>J Virol</stitle><addtitle>J Virol</addtitle><date>2023-04-27</date><risdate>2023</risdate><volume>97</volume><issue>4</issue><spage>e0012823</spage><epage>e0012823</epage><pages>e0012823-e0012823</pages><issn>0022-538X</issn><issn>1098-5514</issn><eissn>1098-5514</eissn><abstract>Coronavirus membrane protein is a major component of the viral envelope and plays a central role in the viral life cycle. Studies of the coronavirus membrane protein (M) have mainly focused on its role in viral assembly and budding, but whether M protein is involved in the initial stage of viral replication remains unclear. In this study, eight proteins in transmissible gastroenteritis virus (TGEV)-infected cells coimmunoprecipitated with monoclonal antibodies (MAb) against M protein in PK-15 cells, heat shock cognate protein 70 (HSC70), and clathrin were identified by matrix-assisted laser desorption ionization-tandem time of flight mass spectrometry (MALDI-TOF MS). Further studies demonstrated that HSC70 and TGEV M colocalized on the cell surface in early stages of TGEV infection; specifically, HSC70 bound M protein through its substrate-binding domain (SBD) and preincubation of TGEV with anti-M serum to block the interaction of M and HSC70 reduced the internalization of TGEV, thus demonstrating that the M-HSC70 interaction mediates the internalization of TGEV. Remarkably, the process of internalization was dependent on clathrin-mediated endocytosis (CME) in PK-15 cells. Furthermore, inhibition of the ATPase activity of HSC70 reduced the efficiency of CME. Collectively, our results indicated that HSC70 is a newly identified host factor involved in TGEV infection. Taken together, our findings clearly illustrate a novel role for TGEV M protein in the viral life cycle and present a unique strategy used by HSC70 to promote TGEV infection in which the interaction with M protein directs viral internalization. These studies provide new insights into the life cycle of coronaviruses.
TGEV is the causative agent of porcine diarrhea, a viral disease that economically affects the pig industry in many countries. However, the molecular mechanisms underlying viral replication remain incompletely understood. Here, we provide evidence of a previously undescribed role of M protein in viral replication during early stages. We also identified HSC70 as a new host factor affecting TGEV infection. We demonstrate that the interaction between M and HSC70 directs TGEV internalization in a manner dependent on CME, thus revealing a novel mechanism for TGEV replication. We believe that this study may change our understanding of the first steps of infection of cells with coronavirus. This study should facilitate the development of anti-TGEV therapeutic agents by targeting the host factors and may provide a new strategy for the control of porcine diarrhea.</abstract><cop>United States</cop><pub>American Society for Microbiology</pub><pmid>36975782</pmid><doi>10.1128/jvi.00128-23</doi><tpages>19</tpages><orcidid>https://orcid.org/0000-0003-4123-0892</orcidid><oa>free_for_read</oa></addata></record> |
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subjects | Animals Cell Line Clathrin Clathrin - metabolism clathrin-mediated endocytosis Coronavirus Coronavirus Infections Coronavirus M Proteins Coronavirus M Proteins - metabolism Diarrhea Endocytosis Host-Microbial Interactions HSC70 HSC70 Heat-Shock Proteins HSP70 Heat-Shock Proteins Humans Immunology Insect Science internalization Life sciences membrane protein Membrane Proteins Microbiology Médecine vétérinaire & santé animale Sciences du vivant Swine transmissible gastroenteritis virus Transmissible gastroenteritis virus - physiology Veterinary medicine & animal health Virology Virus Internalization Virus Replication Virus-Cell Interactions |
title | The TGEV Membrane Protein Interacts with HSC70 To Direct Virus Internalization through Clathrin-Mediated Endocytosis |
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