Superficial vimentin mediates DENV-2 infection of vascular endothelial cells
Damage to vascular endothelial cells (VECs) is a critical hallmark of hemorrhagic diseases caused by dengue virus (DENV). However, the precise molecular event involved in DENV binding and infection of VECs has yet to be clarified. In this study, vimentin (55 kDa) was identified to be involved in DEN...
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| Veröffentlicht in: | Scientific reports 2016-12, Vol.6 (1), p.38372-38372, Article 38372 |
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| creator | Yang, Jie Zou, Lingyun Yang, Yi Yuan, Jizhen Hu, Zhen Liu, Hui Peng, Huagang Shang, Weilong Zhang, Xiaopeng Zhu, Junmin Rao, Xiancai |
| description | Damage to vascular endothelial cells (VECs) is a critical hallmark of hemorrhagic diseases caused by dengue virus (DENV). However, the precise molecular event involved in DENV binding and infection of VECs has yet to be clarified. In this study, vimentin (55 kDa) was identified to be involved in DENV-2 adsorption into VECs. This protein is located on the surface of VECs and interacts with DENV-2 envelope protein domain III (EDIII). The expression level of the superficial vimentin on VECs was not affected by viral infection or siRNA interference, indicating that the protein exists in a particular mode. Furthermore, the rod domain of the vimentin protein mainly functions in DENV-2 adsorption into VECs. Molecular docking results predicted several residues in vimentin rod and DENV EDIII; these residues may be responsible for cell–virus interactions. We propose that the superficial vimentin could be a novel molecule involved in DENV binding and infection of VECs. DENV EDIII directly interacts with the rod domain of vimentin on the VEC surface and thus mediates the infection. |
| doi_str_mv | 10.1038/srep38372 |
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However, the precise molecular event involved in DENV binding and infection of VECs has yet to be clarified. In this study, vimentin (55 kDa) was identified to be involved in DENV-2 adsorption into VECs. This protein is located on the surface of VECs and interacts with DENV-2 envelope protein domain III (EDIII). The expression level of the superficial vimentin on VECs was not affected by viral infection or siRNA interference, indicating that the protein exists in a particular mode. Furthermore, the rod domain of the vimentin protein mainly functions in DENV-2 adsorption into VECs. Molecular docking results predicted several residues in vimentin rod and DENV EDIII; these residues may be responsible for cell–virus interactions. We propose that the superficial vimentin could be a novel molecule involved in DENV binding and infection of VECs. DENV EDIII directly interacts with the rod domain of vimentin on the VEC surface and thus mediates the infection.</description><identifier>ISSN: 2045-2322</identifier><identifier>EISSN: 2045-2322</identifier><identifier>DOI: 10.1038/srep38372</identifier><identifier>PMID: 27910934</identifier><language>eng</language><publisher>London: Nature Publishing Group UK</publisher><subject>13 ; 14 ; 14/19 ; 42/89 ; 45/77 ; 631/326/596/1413 ; 631/326/596/2557 ; 82/58 ; 82/80 ; 82/83 ; Adsorption ; Dengue hemorrhagic fever ; Endothelial cells ; Humanities and Social Sciences ; Infections ; multidisciplinary ; Proteins ; Science ; siRNA ; Vector-borne diseases ; Vimentin ; Viral envelope proteins ; Viral infections</subject><ispartof>Scientific reports, 2016-12, Vol.6 (1), p.38372-38372, Article 38372</ispartof><rights>The Author(s) 2016</rights><rights>Copyright Nature Publishing Group Dec 2016</rights><rights>Copyright © 2016, The Author(s) 2016 The Author(s)</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c504t-6d2edb8fdc9b927d46334b632ac9893d25df2b218fe582404a572e9017561923</citedby><cites>FETCH-LOGICAL-c504t-6d2edb8fdc9b927d46334b632ac9893d25df2b218fe582404a572e9017561923</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/PMC5133558/pdf/$$EPDF$$P50$$Gpubmedcentral$$Hfree_for_read</linktopdf><linktohtml>$$Uhttps://www.ncbi.nlm.nih.gov/pmc/articles/PMC5133558/$$EHTML$$P50$$Gpubmedcentral$$Hfree_for_read</linktohtml><link.rule.ids>230,314,727,780,784,864,885,27924,27925,41120,42189,51576,53791,53793</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/27910934$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Yang, Jie</creatorcontrib><creatorcontrib>Zou, Lingyun</creatorcontrib><creatorcontrib>Yang, Yi</creatorcontrib><creatorcontrib>Yuan, Jizhen</creatorcontrib><creatorcontrib>Hu, Zhen</creatorcontrib><creatorcontrib>Liu, Hui</creatorcontrib><creatorcontrib>Peng, Huagang</creatorcontrib><creatorcontrib>Shang, Weilong</creatorcontrib><creatorcontrib>Zhang, Xiaopeng</creatorcontrib><creatorcontrib>Zhu, Junmin</creatorcontrib><creatorcontrib>Rao, Xiancai</creatorcontrib><title>Superficial vimentin mediates DENV-2 infection of vascular endothelial cells</title><title>Scientific reports</title><addtitle>Sci Rep</addtitle><addtitle>Sci Rep</addtitle><description>Damage to vascular endothelial cells (VECs) is a critical hallmark of hemorrhagic diseases caused by dengue virus (DENV). However, the precise molecular event involved in DENV binding and infection of VECs has yet to be clarified. In this study, vimentin (55 kDa) was identified to be involved in DENV-2 adsorption into VECs. This protein is located on the surface of VECs and interacts with DENV-2 envelope protein domain III (EDIII). The expression level of the superficial vimentin on VECs was not affected by viral infection or siRNA interference, indicating that the protein exists in a particular mode. Furthermore, the rod domain of the vimentin protein mainly functions in DENV-2 adsorption into VECs. Molecular docking results predicted several residues in vimentin rod and DENV EDIII; these residues may be responsible for cell–virus interactions. We propose that the superficial vimentin could be a novel molecule involved in DENV binding and infection of VECs. DENV EDIII directly interacts with the rod domain of vimentin on the VEC surface and thus mediates the infection.</description><subject>13</subject><subject>14</subject><subject>14/19</subject><subject>42/89</subject><subject>45/77</subject><subject>631/326/596/1413</subject><subject>631/326/596/2557</subject><subject>82/58</subject><subject>82/80</subject><subject>82/83</subject><subject>Adsorption</subject><subject>Dengue hemorrhagic fever</subject><subject>Endothelial cells</subject><subject>Humanities and Social Sciences</subject><subject>Infections</subject><subject>multidisciplinary</subject><subject>Proteins</subject><subject>Science</subject><subject>siRNA</subject><subject>Vector-borne diseases</subject><subject>Vimentin</subject><subject>Viral envelope proteins</subject><subject>Viral infections</subject><issn>2045-2322</issn><issn>2045-2322</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2016</creationdate><recordtype>article</recordtype><sourceid>C6C</sourceid><sourceid>ABUWG</sourceid><sourceid>AFKRA</sourceid><sourceid>AZQEC</sourceid><sourceid>BENPR</sourceid><sourceid>CCPQU</sourceid><sourceid>DWQXO</sourceid><sourceid>GNUQQ</sourceid><recordid>eNplkUFrGzEQhUVJaELiQ_9AWeilLWwijaRd6RIIrtMETHKo6VVotdpYZi250q6h_74yTozT6DKC-ebNGx5Cnwi-IpiK6xTthgpawwd0DpjxEijAydH_DE1SWuH8OEhG5Ed0BrUkWFJ2jua_xo2NnTNO98XWra0fnC_WtnV6sKn4MXv8XULhfGfN4IIvQldsdTJjr2NhfRuGpe13o8b2fbpEp53uk5281Au0uJstpvfl_Onnw_R2XhqO2VBWLdi2EV1rZCOhbllFKWsqCtpIIWkLvO2gASI6ywUwzDSvwUpMal4RCfQC3exlN2OTnZrsOepebaJb6_hXBe3U2453S_UctooTSjkXWeDri0AMf0abBrV2aXeB9jaMSRHB8uKKYp7RL_-hqzBGn6_LlJS0kiB2gt_2lIkh5UC6gxmC1S4ldUgps5-P3R_I10wy8H0PpNzyzzYerXyn9g8EnJst</recordid><startdate>20161202</startdate><enddate>20161202</enddate><creator>Yang, Jie</creator><creator>Zou, Lingyun</creator><creator>Yang, Yi</creator><creator>Yuan, Jizhen</creator><creator>Hu, Zhen</creator><creator>Liu, Hui</creator><creator>Peng, Huagang</creator><creator>Shang, Weilong</creator><creator>Zhang, Xiaopeng</creator><creator>Zhu, Junmin</creator><creator>Rao, Xiancai</creator><general>Nature Publishing Group UK</general><general>Nature Publishing Group</general><scope>C6C</scope><scope>NPM</scope><scope>AAYXX</scope><scope>CITATION</scope><scope>3V.</scope><scope>7X7</scope><scope>7XB</scope><scope>88A</scope><scope>88E</scope><scope>88I</scope><scope>8FE</scope><scope>8FH</scope><scope>8FI</scope><scope>8FJ</scope><scope>8FK</scope><scope>ABUWG</scope><scope>AFKRA</scope><scope>AZQEC</scope><scope>BBNVY</scope><scope>BENPR</scope><scope>BHPHI</scope><scope>CCPQU</scope><scope>DWQXO</scope><scope>FYUFA</scope><scope>GHDGH</scope><scope>GNUQQ</scope><scope>HCIFZ</scope><scope>K9.</scope><scope>LK8</scope><scope>M0S</scope><scope>M1P</scope><scope>M2P</scope><scope>M7P</scope><scope>PIMPY</scope><scope>PQEST</scope><scope>PQQKQ</scope><scope>PQUKI</scope><scope>Q9U</scope><scope>7X8</scope><scope>5PM</scope></search><sort><creationdate>20161202</creationdate><title>Superficial vimentin mediates DENV-2 infection of vascular endothelial cells</title><author>Yang, Jie ; Zou, Lingyun ; Yang, Yi ; Yuan, Jizhen ; Hu, Zhen ; Liu, Hui ; Peng, Huagang ; Shang, Weilong ; Zhang, Xiaopeng ; Zhu, Junmin ; Rao, Xiancai</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c504t-6d2edb8fdc9b927d46334b632ac9893d25df2b218fe582404a572e9017561923</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2016</creationdate><topic>13</topic><topic>14</topic><topic>14/19</topic><topic>42/89</topic><topic>45/77</topic><topic>631/326/596/1413</topic><topic>631/326/596/2557</topic><topic>82/58</topic><topic>82/80</topic><topic>82/83</topic><topic>Adsorption</topic><topic>Dengue hemorrhagic fever</topic><topic>Endothelial cells</topic><topic>Humanities and Social Sciences</topic><topic>Infections</topic><topic>multidisciplinary</topic><topic>Proteins</topic><topic>Science</topic><topic>siRNA</topic><topic>Vector-borne diseases</topic><topic>Vimentin</topic><topic>Viral envelope proteins</topic><topic>Viral infections</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Yang, Jie</creatorcontrib><creatorcontrib>Zou, Lingyun</creatorcontrib><creatorcontrib>Yang, Yi</creatorcontrib><creatorcontrib>Yuan, Jizhen</creatorcontrib><creatorcontrib>Hu, Zhen</creatorcontrib><creatorcontrib>Liu, Hui</creatorcontrib><creatorcontrib>Peng, Huagang</creatorcontrib><creatorcontrib>Shang, Weilong</creatorcontrib><creatorcontrib>Zhang, Xiaopeng</creatorcontrib><creatorcontrib>Zhu, Junmin</creatorcontrib><creatorcontrib>Rao, Xiancai</creatorcontrib><collection>Springer Nature OA Free Journals</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>ProQuest Central (Corporate)</collection><collection>Health & Medical Collection</collection><collection>ProQuest Central (purchase pre-March 2016)</collection><collection>Biology Database (Alumni Edition)</collection><collection>Medical Database (Alumni Edition)</collection><collection>Science Database (Alumni Edition)</collection><collection>ProQuest SciTech Collection</collection><collection>ProQuest Natural Science Collection</collection><collection>Hospital Premium Collection</collection><collection>Hospital Premium Collection (Alumni Edition)</collection><collection>ProQuest Central (Alumni) (purchase pre-March 2016)</collection><collection>ProQuest Central (Alumni Edition)</collection><collection>ProQuest Central UK/Ireland</collection><collection>ProQuest Central Essentials</collection><collection>Biological Science Collection</collection><collection>ProQuest Central</collection><collection>Natural Science Collection</collection><collection>ProQuest One Community College</collection><collection>ProQuest Central Korea</collection><collection>Health Research Premium Collection</collection><collection>Health Research Premium Collection (Alumni)</collection><collection>ProQuest Central Student</collection><collection>SciTech Premium Collection</collection><collection>ProQuest Health & Medical Complete (Alumni)</collection><collection>ProQuest Biological Science Collection</collection><collection>Health & Medical Collection (Alumni Edition)</collection><collection>Medical Database</collection><collection>Science Database</collection><collection>Biological Science Database</collection><collection>Access via ProQuest (Open Access)</collection><collection>ProQuest One Academic Eastern Edition (DO NOT USE)</collection><collection>ProQuest One Academic</collection><collection>ProQuest One Academic UKI Edition</collection><collection>ProQuest Central Basic</collection><collection>MEDLINE - Academic</collection><collection>PubMed Central (Full Participant titles)</collection><jtitle>Scientific reports</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Yang, Jie</au><au>Zou, Lingyun</au><au>Yang, Yi</au><au>Yuan, Jizhen</au><au>Hu, Zhen</au><au>Liu, Hui</au><au>Peng, Huagang</au><au>Shang, Weilong</au><au>Zhang, Xiaopeng</au><au>Zhu, Junmin</au><au>Rao, Xiancai</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Superficial vimentin mediates DENV-2 infection of vascular endothelial cells</atitle><jtitle>Scientific reports</jtitle><stitle>Sci Rep</stitle><addtitle>Sci Rep</addtitle><date>2016-12-02</date><risdate>2016</risdate><volume>6</volume><issue>1</issue><spage>38372</spage><epage>38372</epage><pages>38372-38372</pages><artnum>38372</artnum><issn>2045-2322</issn><eissn>2045-2322</eissn><abstract>Damage to vascular endothelial cells (VECs) is a critical hallmark of hemorrhagic diseases caused by dengue virus (DENV). However, the precise molecular event involved in DENV binding and infection of VECs has yet to be clarified. In this study, vimentin (55 kDa) was identified to be involved in DENV-2 adsorption into VECs. This protein is located on the surface of VECs and interacts with DENV-2 envelope protein domain III (EDIII). The expression level of the superficial vimentin on VECs was not affected by viral infection or siRNA interference, indicating that the protein exists in a particular mode. Furthermore, the rod domain of the vimentin protein mainly functions in DENV-2 adsorption into VECs. Molecular docking results predicted several residues in vimentin rod and DENV EDIII; these residues may be responsible for cell–virus interactions. We propose that the superficial vimentin could be a novel molecule involved in DENV binding and infection of VECs. DENV EDIII directly interacts with the rod domain of vimentin on the VEC surface and thus mediates the infection.</abstract><cop>London</cop><pub>Nature Publishing Group UK</pub><pmid>27910934</pmid><doi>10.1038/srep38372</doi><tpages>1</tpages><oa>free_for_read</oa></addata></record> |
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| subjects | 13 14 14/19 42/89 45/77 631/326/596/1413 631/326/596/2557 82/58 82/80 82/83 Adsorption Dengue hemorrhagic fever Endothelial cells Humanities and Social Sciences Infections multidisciplinary Proteins Science siRNA Vector-borne diseases Vimentin Viral envelope proteins Viral infections |
| title | Superficial vimentin mediates DENV-2 infection of vascular endothelial cells |
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