Interaction of the Small GTPase Cdc42 with Arginine Kinase Restricts White Spot Syndrome Virus in Shrimp
Many types of small GTPases are widely expressed in eukaryotes and have different functions. As a crucial member of the Rho GTPase family, Cdc42 serves a number of functions, such as regulating cell growth, migration, and cell movement. Several RNA viruses employ Cdc42-hijacking tactics in their tar...
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| creator | Xu, Ji-Dong Jiang, Hai-Shan Wei, Tian-Di Zhang, Ke-Yi Wang, Xian-Wei Zhao, Xiao-Fan Wang, Jin-Xing |
| description | Many types of small GTPases are widely expressed in eukaryotes and have different functions. As a crucial member of the Rho GTPase family, Cdc42 serves a number of functions, such as regulating cell growth, migration, and cell movement. Several RNA viruses employ Cdc42-hijacking tactics in their target cell entry processes. However, the function of Cdc42 in shrimp antiviral immunity is not clear. In this study, we identified a Cdc42 protein in the kuruma shrimp (
) and named it
Cdc42.
Cdc42 was upregulated in shrimp challenged by white spot syndrome virus (WSSV). The knockdown of
Cdc42 and injection of Cdc42 inhibitors increased the proliferation of WSSV. Further experiments determined that
Cdc42 interacted with an arginine kinase (
AK). By analyzing the binding activity and enzyme activity of
AK and its mutant, Δ
AK, we found that
AK could enhance the replication of WSSV in shrimp.
AK interacted with the envelope protein VP26 of WSSV. An inhibitor of AK activity, quercetin, could impair the function of
AK in WSSV replication. Further study demonstrated that the binding of
Cdc42 and
AK depends on Cys
of
AK and suppresses the WSSV replication-promoting effect of
AK. By interacting with the active site of
AK and suppressing its enzyme activity,
Cdc42 inhibits WSSV replication in shrimp. Our results demonstrate a new function of Cdc42 in the cellular defense against viral infection in addition to the regulation of actin and phagocytosis, which has been reported in previous studies.
The interaction of Cdc42 with arginine kinase plays a crucial role in the host defense against WSSV infection. This study identifies a new mechanism of Cdc42 in innate immunity and enriches the knowledge of the antiviral innate immunity of invertebrates. |
| doi_str_mv | 10.1128/JVI.01916-16 |
| format | Article |
| fullrecord | <record><control><sourceid>proquest_pubme</sourceid><recordid>TN_cdi_pubmedcentral_primary_oai_pubmedcentral_nih_gov_5309935</recordid><sourceformat>XML</sourceformat><sourcesystem>PC</sourcesystem><sourcerecordid>1854106486</sourcerecordid><originalsourceid>FETCH-LOGICAL-c384t-cbf9aff136ad2865bf9d5ce5d0a409e119ed14ad0b074c6a8aae0218657718513</originalsourceid><addsrcrecordid>eNpVkUlPwzAQhS0EgrLcOCMfORDwJHbqXJBQxVJAAlG2m-U6DjFK7GK7IP49LpvgNBrNN2_e6CG0DWQfIOcH5_fjfQIVlBmUS2gApOIZY0CX0YCQPM9YwR_X0HoIz4QApSVdRWs5JwUUZT5A7dhG7aWKxlnsGhxbjSe97Dp8enstg8ajWtEcv5nY4iP_ZKyxGl8Yuxjd6BC9UTHgh9bEtDdzEU_ebe1dr_G98fOAjcWT1pt-tolWGtkFvfVdN9DdyfHt6Cy7vDodj44uM1VwGjM1bSrZNMmcrHNestTWTGlWE0lJpQEqXQOVNZmSIVWl5FJqkkMih0PgDIoNdPilO5tPe10rbaOXnZglD9K_CyeN-D-xphVP7lWwglRVwZLA7reAdy_z9KLoTVC666TVbh5EukKBlJSXCd37QpV3IXjd_J4BIhbhiBSO-AxHwALf-WvtF_5Jo_gAC6SLZA</addsrcrecordid><sourcetype>Open Access Repository</sourcetype><iscdi>true</iscdi><recordtype>article</recordtype><pqid>1854106486</pqid></control><display><type>article</type><title>Interaction of the Small GTPase Cdc42 with Arginine Kinase Restricts White Spot Syndrome Virus in Shrimp</title><source>MEDLINE</source><source>Elektronische Zeitschriftenbibliothek - Frei zugängliche E-Journals</source><source>PubMed Central</source><creator>Xu, Ji-Dong ; Jiang, Hai-Shan ; Wei, Tian-Di ; Zhang, Ke-Yi ; Wang, Xian-Wei ; Zhao, Xiao-Fan ; Wang, Jin-Xing</creator><contributor>McFadden, Grant</contributor><creatorcontrib>Xu, Ji-Dong ; Jiang, Hai-Shan ; Wei, Tian-Di ; Zhang, Ke-Yi ; Wang, Xian-Wei ; Zhao, Xiao-Fan ; Wang, Jin-Xing ; McFadden, Grant</creatorcontrib><description>Many types of small GTPases are widely expressed in eukaryotes and have different functions. As a crucial member of the Rho GTPase family, Cdc42 serves a number of functions, such as regulating cell growth, migration, and cell movement. Several RNA viruses employ Cdc42-hijacking tactics in their target cell entry processes. However, the function of Cdc42 in shrimp antiviral immunity is not clear. In this study, we identified a Cdc42 protein in the kuruma shrimp (
) and named it
Cdc42.
Cdc42 was upregulated in shrimp challenged by white spot syndrome virus (WSSV). The knockdown of
Cdc42 and injection of Cdc42 inhibitors increased the proliferation of WSSV. Further experiments determined that
Cdc42 interacted with an arginine kinase (
AK). By analyzing the binding activity and enzyme activity of
AK and its mutant, Δ
AK, we found that
AK could enhance the replication of WSSV in shrimp.
AK interacted with the envelope protein VP26 of WSSV. An inhibitor of AK activity, quercetin, could impair the function of
AK in WSSV replication. Further study demonstrated that the binding of
Cdc42 and
AK depends on Cys
of
AK and suppresses the WSSV replication-promoting effect of
AK. By interacting with the active site of
AK and suppressing its enzyme activity,
Cdc42 inhibits WSSV replication in shrimp. Our results demonstrate a new function of Cdc42 in the cellular defense against viral infection in addition to the regulation of actin and phagocytosis, which has been reported in previous studies.
The interaction of Cdc42 with arginine kinase plays a crucial role in the host defense against WSSV infection. This study identifies a new mechanism of Cdc42 in innate immunity and enriches the knowledge of the antiviral innate immunity of invertebrates.</description><identifier>ISSN: 0022-538X</identifier><identifier>EISSN: 1098-5514</identifier><identifier>DOI: 10.1128/JVI.01916-16</identifier><identifier>PMID: 28031362</identifier><language>eng</language><publisher>United States: American Society for Microbiology</publisher><subject>Amino Acid Sequence ; Animals ; Arginine Kinase - chemistry ; Arginine Kinase - metabolism ; Arthropod Proteins - chemistry ; Arthropod Proteins - metabolism ; cdc42 GTP-Binding Protein - chemistry ; cdc42 GTP-Binding Protein - metabolism ; Conserved Sequence ; Enzyme Induction - immunology ; Escherichia coli ; Host-Pathogen Interactions ; Immunity, Innate ; Molecular Docking Simulation ; Pathogenesis and Immunity ; Penaeidae - enzymology ; Penaeidae - immunology ; Penaeidae - virology ; Protein Binding ; Protein Interaction Maps ; Spotlight ; Up-Regulation ; Virus Replication ; White spot syndrome virus 1 - physiology</subject><ispartof>Journal of virology, 2017-03, Vol.91 (5)</ispartof><rights>Copyright © 2017 American Society for Microbiology.</rights><rights>Copyright © 2017 American Society for Microbiology. 2017 American Society for Microbiology</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c384t-cbf9aff136ad2865bf9d5ce5d0a409e119ed14ad0b074c6a8aae0218657718513</citedby><cites>FETCH-LOGICAL-c384t-cbf9aff136ad2865bf9d5ce5d0a409e119ed14ad0b074c6a8aae0218657718513</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://www.ncbi.nlm.nih.gov/pmc/articles/PMC5309935/pdf/$$EPDF$$P50$$Gpubmedcentral$$H</linktopdf><linktohtml>$$Uhttps://www.ncbi.nlm.nih.gov/pmc/articles/PMC5309935/$$EHTML$$P50$$Gpubmedcentral$$H</linktohtml><link.rule.ids>230,314,723,776,780,881,27901,27902,53766,53768</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/28031362$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><contributor>McFadden, Grant</contributor><creatorcontrib>Xu, Ji-Dong</creatorcontrib><creatorcontrib>Jiang, Hai-Shan</creatorcontrib><creatorcontrib>Wei, Tian-Di</creatorcontrib><creatorcontrib>Zhang, Ke-Yi</creatorcontrib><creatorcontrib>Wang, Xian-Wei</creatorcontrib><creatorcontrib>Zhao, Xiao-Fan</creatorcontrib><creatorcontrib>Wang, Jin-Xing</creatorcontrib><title>Interaction of the Small GTPase Cdc42 with Arginine Kinase Restricts White Spot Syndrome Virus in Shrimp</title><title>Journal of virology</title><addtitle>J Virol</addtitle><description>Many types of small GTPases are widely expressed in eukaryotes and have different functions. As a crucial member of the Rho GTPase family, Cdc42 serves a number of functions, such as regulating cell growth, migration, and cell movement. Several RNA viruses employ Cdc42-hijacking tactics in their target cell entry processes. However, the function of Cdc42 in shrimp antiviral immunity is not clear. In this study, we identified a Cdc42 protein in the kuruma shrimp (
) and named it
Cdc42.
Cdc42 was upregulated in shrimp challenged by white spot syndrome virus (WSSV). The knockdown of
Cdc42 and injection of Cdc42 inhibitors increased the proliferation of WSSV. Further experiments determined that
Cdc42 interacted with an arginine kinase (
AK). By analyzing the binding activity and enzyme activity of
AK and its mutant, Δ
AK, we found that
AK could enhance the replication of WSSV in shrimp.
AK interacted with the envelope protein VP26 of WSSV. An inhibitor of AK activity, quercetin, could impair the function of
AK in WSSV replication. Further study demonstrated that the binding of
Cdc42 and
AK depends on Cys
of
AK and suppresses the WSSV replication-promoting effect of
AK. By interacting with the active site of
AK and suppressing its enzyme activity,
Cdc42 inhibits WSSV replication in shrimp. Our results demonstrate a new function of Cdc42 in the cellular defense against viral infection in addition to the regulation of actin and phagocytosis, which has been reported in previous studies.
The interaction of Cdc42 with arginine kinase plays a crucial role in the host defense against WSSV infection. This study identifies a new mechanism of Cdc42 in innate immunity and enriches the knowledge of the antiviral innate immunity of invertebrates.</description><subject>Amino Acid Sequence</subject><subject>Animals</subject><subject>Arginine Kinase - chemistry</subject><subject>Arginine Kinase - metabolism</subject><subject>Arthropod Proteins - chemistry</subject><subject>Arthropod Proteins - metabolism</subject><subject>cdc42 GTP-Binding Protein - chemistry</subject><subject>cdc42 GTP-Binding Protein - metabolism</subject><subject>Conserved Sequence</subject><subject>Enzyme Induction - immunology</subject><subject>Escherichia coli</subject><subject>Host-Pathogen Interactions</subject><subject>Immunity, Innate</subject><subject>Molecular Docking Simulation</subject><subject>Pathogenesis and Immunity</subject><subject>Penaeidae - enzymology</subject><subject>Penaeidae - immunology</subject><subject>Penaeidae - virology</subject><subject>Protein Binding</subject><subject>Protein Interaction Maps</subject><subject>Spotlight</subject><subject>Up-Regulation</subject><subject>Virus Replication</subject><subject>White spot syndrome virus 1 - physiology</subject><issn>0022-538X</issn><issn>1098-5514</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2017</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNpVkUlPwzAQhS0EgrLcOCMfORDwJHbqXJBQxVJAAlG2m-U6DjFK7GK7IP49LpvgNBrNN2_e6CG0DWQfIOcH5_fjfQIVlBmUS2gApOIZY0CX0YCQPM9YwR_X0HoIz4QApSVdRWs5JwUUZT5A7dhG7aWKxlnsGhxbjSe97Dp8enstg8ajWtEcv5nY4iP_ZKyxGl8Yuxjd6BC9UTHgh9bEtDdzEU_ebe1dr_G98fOAjcWT1pt-tolWGtkFvfVdN9DdyfHt6Cy7vDodj44uM1VwGjM1bSrZNMmcrHNestTWTGlWE0lJpQEqXQOVNZmSIVWl5FJqkkMih0PgDIoNdPilO5tPe10rbaOXnZglD9K_CyeN-D-xphVP7lWwglRVwZLA7reAdy_z9KLoTVC666TVbh5EukKBlJSXCd37QpV3IXjd_J4BIhbhiBSO-AxHwALf-WvtF_5Jo_gAC6SLZA</recordid><startdate>20170301</startdate><enddate>20170301</enddate><creator>Xu, Ji-Dong</creator><creator>Jiang, Hai-Shan</creator><creator>Wei, Tian-Di</creator><creator>Zhang, Ke-Yi</creator><creator>Wang, Xian-Wei</creator><creator>Zhao, Xiao-Fan</creator><creator>Wang, Jin-Xing</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>5PM</scope></search><sort><creationdate>20170301</creationdate><title>Interaction of the Small GTPase Cdc42 with Arginine Kinase Restricts White Spot Syndrome Virus in Shrimp</title><author>Xu, Ji-Dong ; Jiang, Hai-Shan ; Wei, Tian-Di ; Zhang, Ke-Yi ; Wang, Xian-Wei ; Zhao, Xiao-Fan ; Wang, Jin-Xing</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c384t-cbf9aff136ad2865bf9d5ce5d0a409e119ed14ad0b074c6a8aae0218657718513</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2017</creationdate><topic>Amino Acid Sequence</topic><topic>Animals</topic><topic>Arginine Kinase - chemistry</topic><topic>Arginine Kinase - metabolism</topic><topic>Arthropod Proteins - chemistry</topic><topic>Arthropod Proteins - metabolism</topic><topic>cdc42 GTP-Binding Protein - chemistry</topic><topic>cdc42 GTP-Binding Protein - metabolism</topic><topic>Conserved Sequence</topic><topic>Enzyme Induction - immunology</topic><topic>Escherichia coli</topic><topic>Host-Pathogen Interactions</topic><topic>Immunity, Innate</topic><topic>Molecular Docking Simulation</topic><topic>Pathogenesis and Immunity</topic><topic>Penaeidae - enzymology</topic><topic>Penaeidae - immunology</topic><topic>Penaeidae - virology</topic><topic>Protein Binding</topic><topic>Protein Interaction Maps</topic><topic>Spotlight</topic><topic>Up-Regulation</topic><topic>Virus Replication</topic><topic>White spot syndrome virus 1 - physiology</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Xu, Ji-Dong</creatorcontrib><creatorcontrib>Jiang, Hai-Shan</creatorcontrib><creatorcontrib>Wei, Tian-Di</creatorcontrib><creatorcontrib>Zhang, Ke-Yi</creatorcontrib><creatorcontrib>Wang, Xian-Wei</creatorcontrib><creatorcontrib>Zhao, Xiao-Fan</creatorcontrib><creatorcontrib>Wang, Jin-Xing</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>PubMed Central (Full Participant titles)</collection><jtitle>Journal of virology</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Xu, Ji-Dong</au><au>Jiang, Hai-Shan</au><au>Wei, Tian-Di</au><au>Zhang, Ke-Yi</au><au>Wang, Xian-Wei</au><au>Zhao, Xiao-Fan</au><au>Wang, Jin-Xing</au><au>McFadden, Grant</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Interaction of the Small GTPase Cdc42 with Arginine Kinase Restricts White Spot Syndrome Virus in Shrimp</atitle><jtitle>Journal of virology</jtitle><addtitle>J Virol</addtitle><date>2017-03-01</date><risdate>2017</risdate><volume>91</volume><issue>5</issue><issn>0022-538X</issn><eissn>1098-5514</eissn><abstract>Many types of small GTPases are widely expressed in eukaryotes and have different functions. As a crucial member of the Rho GTPase family, Cdc42 serves a number of functions, such as regulating cell growth, migration, and cell movement. Several RNA viruses employ Cdc42-hijacking tactics in their target cell entry processes. However, the function of Cdc42 in shrimp antiviral immunity is not clear. In this study, we identified a Cdc42 protein in the kuruma shrimp (
) and named it
Cdc42.
Cdc42 was upregulated in shrimp challenged by white spot syndrome virus (WSSV). The knockdown of
Cdc42 and injection of Cdc42 inhibitors increased the proliferation of WSSV. Further experiments determined that
Cdc42 interacted with an arginine kinase (
AK). By analyzing the binding activity and enzyme activity of
AK and its mutant, Δ
AK, we found that
AK could enhance the replication of WSSV in shrimp.
AK interacted with the envelope protein VP26 of WSSV. An inhibitor of AK activity, quercetin, could impair the function of
AK in WSSV replication. Further study demonstrated that the binding of
Cdc42 and
AK depends on Cys
of
AK and suppresses the WSSV replication-promoting effect of
AK. By interacting with the active site of
AK and suppressing its enzyme activity,
Cdc42 inhibits WSSV replication in shrimp. Our results demonstrate a new function of Cdc42 in the cellular defense against viral infection in addition to the regulation of actin and phagocytosis, which has been reported in previous studies.
The interaction of Cdc42 with arginine kinase plays a crucial role in the host defense against WSSV infection. This study identifies a new mechanism of Cdc42 in innate immunity and enriches the knowledge of the antiviral innate immunity of invertebrates.</abstract><cop>United States</cop><pub>American Society for Microbiology</pub><pmid>28031362</pmid><doi>10.1128/JVI.01916-16</doi><oa>free_for_read</oa></addata></record> |
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| source | MEDLINE; Elektronische Zeitschriftenbibliothek - Frei zugängliche E-Journals; PubMed Central |
| subjects | Amino Acid Sequence Animals Arginine Kinase - chemistry Arginine Kinase - metabolism Arthropod Proteins - chemistry Arthropod Proteins - metabolism cdc42 GTP-Binding Protein - chemistry cdc42 GTP-Binding Protein - metabolism Conserved Sequence Enzyme Induction - immunology Escherichia coli Host-Pathogen Interactions Immunity, Innate Molecular Docking Simulation Pathogenesis and Immunity Penaeidae - enzymology Penaeidae - immunology Penaeidae - virology Protein Binding Protein Interaction Maps Spotlight Up-Regulation Virus Replication White spot syndrome virus 1 - physiology |
| title | Interaction of the Small GTPase Cdc42 with Arginine Kinase Restricts White Spot Syndrome Virus in Shrimp |
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