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Vaccinia virus dissemination requires p21-activated kinase 1
The orthopoxvirus vaccinia virus (VACV) interacts with both actin and microtubule cytoskeletons in order to generate and spread progeny virions. Here, we present evidence demonstrating the involvement of PAK1 (p21-activated kinase 1) in the dissemination of VACV. Although PAK1 activation has previou...
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Published in: | Archives of virology 2016-11, Vol.161 (11), p.2991-3002 |
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creator | Andrade, Luciana G. Albarnaz, Jonas D. Mügge, Fernanda L. B. David, Bruna A. Abrahão, Jônatas S. da Fonseca, Flávio G. Kroon, Erna G. Menezes, Gustavo B. McFadden, Grant Bonjardim, Cláudio A. |
description | The orthopoxvirus vaccinia virus (VACV) interacts with both actin and microtubule cytoskeletons in order to generate and spread progeny virions. Here, we present evidence demonstrating the involvement of PAK1 (p21-activated kinase 1) in the dissemination of VACV. Although PAK1 activation has previously been associated with optimal VACV entry via macropinocytosis, its absence does not affect the production of intracellular mature virions (IMVs) and extracellular enveloped virions (EEVs). Our data demonstrate that low-multiplicity infection of PAK1
-/-
MEFs leads to a reduction in plaque size followed by decreased production of both IMVs and EEVs, strongly suggesting that virus spread was impaired in the absence of PAK1. Confocal and scanning electron microscopy showed a substantial reduction in the amount of VACV-induced actin tails in PAK1
-/-
MEFs, but no significant alteration in the total amount of cell-associated enveloped virions (CEVs). Furthermore, the decreased VACV dissemination in PAK1
-/-
cells was correlated with the absence of phosphorylated ARPC1 (Thr21), a downstream target of PAK1 and a key regulatory subunit of the ARP2/3 complex, which is necessary for the formation of actin tails and viral spread. We conclude that PAK1, besides its role in virus entry, also plays a relevant role in VACV dissemination. |
doi_str_mv | 10.1007/s00705-016-2996-3 |
format | article |
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-/-
MEFs leads to a reduction in plaque size followed by decreased production of both IMVs and EEVs, strongly suggesting that virus spread was impaired in the absence of PAK1. Confocal and scanning electron microscopy showed a substantial reduction in the amount of VACV-induced actin tails in PAK1
-/-
MEFs, but no significant alteration in the total amount of cell-associated enveloped virions (CEVs). Furthermore, the decreased VACV dissemination in PAK1
-/-
cells was correlated with the absence of phosphorylated ARPC1 (Thr21), a downstream target of PAK1 and a key regulatory subunit of the ARP2/3 complex, which is necessary for the formation of actin tails and viral spread. We conclude that PAK1, besides its role in virus entry, also plays a relevant role in VACV dissemination.</description><identifier>ISSN: 0304-8608</identifier><identifier>EISSN: 1432-8798</identifier><identifier>DOI: 10.1007/s00705-016-2996-3</identifier><identifier>PMID: 27465567</identifier><language>eng</language><publisher>Vienna: Springer Vienna</publisher><subject>Actin ; Animals ; Biological Transport ; Biomedical and Life Sciences ; Biomedicine ; Cells, Cultured ; Endocytosis ; Host-Pathogen Interactions ; Infectious Diseases ; Medical Microbiology ; Mice ; Mice, Knockout ; Microscopy, Confocal ; Microscopy, Electron, Scanning ; Original Article ; p21-activated kinase ; p21-activated kinase 1 ; p21-Activated Kinases - genetics ; p21-Activated Kinases - metabolism ; Poxviridae ; Scanning electron microscopy ; Vaccinia virus ; Vaccinia virus - physiology ; Virions ; Virology ; Virus Internalization ; Viruses</subject><ispartof>Archives of virology, 2016-11, Vol.161 (11), p.2991-3002</ispartof><rights>Springer-Verlag Wien 2016</rights><rights>Springer-Verlag Wien 2016.</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c433t-f165308e4edbe7d2183c1b7c0aa6c0b54ab0e18c87e36d9eee90ebfd8951cab73</citedby><cites>FETCH-LOGICAL-c433t-f165308e4edbe7d2183c1b7c0aa6c0b54ab0e18c87e36d9eee90ebfd8951cab73</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><link.rule.ids>314,780,784,27924,27925</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/27465567$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Andrade, Luciana G.</creatorcontrib><creatorcontrib>Albarnaz, Jonas D.</creatorcontrib><creatorcontrib>Mügge, Fernanda L. B.</creatorcontrib><creatorcontrib>David, Bruna A.</creatorcontrib><creatorcontrib>Abrahão, Jônatas S.</creatorcontrib><creatorcontrib>da Fonseca, Flávio G.</creatorcontrib><creatorcontrib>Kroon, Erna G.</creatorcontrib><creatorcontrib>Menezes, Gustavo B.</creatorcontrib><creatorcontrib>McFadden, Grant</creatorcontrib><creatorcontrib>Bonjardim, Cláudio A.</creatorcontrib><title>Vaccinia virus dissemination requires p21-activated kinase 1</title><title>Archives of virology</title><addtitle>Arch Virol</addtitle><addtitle>Arch Virol</addtitle><description>The orthopoxvirus vaccinia virus (VACV) interacts with both actin and microtubule cytoskeletons in order to generate and spread progeny virions. Here, we present evidence demonstrating the involvement of PAK1 (p21-activated kinase 1) in the dissemination of VACV. Although PAK1 activation has previously been associated with optimal VACV entry via macropinocytosis, its absence does not affect the production of intracellular mature virions (IMVs) and extracellular enveloped virions (EEVs). Our data demonstrate that low-multiplicity infection of PAK1
-/-
MEFs leads to a reduction in plaque size followed by decreased production of both IMVs and EEVs, strongly suggesting that virus spread was impaired in the absence of PAK1. Confocal and scanning electron microscopy showed a substantial reduction in the amount of VACV-induced actin tails in PAK1
-/-
MEFs, but no significant alteration in the total amount of cell-associated enveloped virions (CEVs). Furthermore, the decreased VACV dissemination in PAK1
-/-
cells was correlated with the absence of phosphorylated ARPC1 (Thr21), a downstream target of PAK1 and a key regulatory subunit of the ARP2/3 complex, which is necessary for the formation of actin tails and viral spread. We conclude that PAK1, besides its role in virus entry, also plays a relevant role in VACV dissemination.</description><subject>Actin</subject><subject>Animals</subject><subject>Biological Transport</subject><subject>Biomedical and Life Sciences</subject><subject>Biomedicine</subject><subject>Cells, Cultured</subject><subject>Endocytosis</subject><subject>Host-Pathogen Interactions</subject><subject>Infectious Diseases</subject><subject>Medical Microbiology</subject><subject>Mice</subject><subject>Mice, Knockout</subject><subject>Microscopy, Confocal</subject><subject>Microscopy, Electron, Scanning</subject><subject>Original Article</subject><subject>p21-activated kinase</subject><subject>p21-activated kinase 1</subject><subject>p21-Activated Kinases - genetics</subject><subject>p21-Activated Kinases - metabolism</subject><subject>Poxviridae</subject><subject>Scanning electron microscopy</subject><subject>Vaccinia virus</subject><subject>Vaccinia virus - physiology</subject><subject>Virions</subject><subject>Virology</subject><subject>Virus Internalization</subject><subject>Viruses</subject><issn>0304-8608</issn><issn>1432-8798</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2016</creationdate><recordtype>article</recordtype><recordid>eNqNkc9LHTEQx0NR6tP2D_BSFrz0kjqTZPMDehGptiB40V5DNjuvRN_bfSa7gv-9kacihUovGch85hsyH8YOEb4hgDku9YCWA2ounNNcfmALVFJwa5zdYQuQoLjVYPfYfik3APVCth_ZnjBKt602C_b9d4gxDSk09ynPpelTKbROQ5jSODSZ7uaUqTQbgTzEKd2HifrmtvYLNfiJ7S7DqtDn53rArs9-XJ3-5BeX579OTy54VFJOfIm6lWBJUd-R6QVaGbEzEULQEbpWhQ4IbbSGpO4dETmgbtlb12IMnZEH7Os2d5PHu5nK5NepRFqtwkDjXDxaYRwaJdT_oHUH0kis6NFf6M0456F-xAvtWq2ckeY9qmYJKRVqqBRuqZjHUjIt_SandcgPHsE_ufJbV7668k-uvKwzX56T525N_evEi5wKiC1Qamv4Q_nN0_9MfQRke5yC</recordid><startdate>20161101</startdate><enddate>20161101</enddate><creator>Andrade, Luciana G.</creator><creator>Albarnaz, Jonas D.</creator><creator>Mügge, Fernanda L. 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B.</au><au>David, Bruna A.</au><au>Abrahão, Jônatas S.</au><au>da Fonseca, Flávio G.</au><au>Kroon, Erna G.</au><au>Menezes, Gustavo B.</au><au>McFadden, Grant</au><au>Bonjardim, Cláudio A.</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Vaccinia virus dissemination requires p21-activated kinase 1</atitle><jtitle>Archives of virology</jtitle><stitle>Arch Virol</stitle><addtitle>Arch Virol</addtitle><date>2016-11-01</date><risdate>2016</risdate><volume>161</volume><issue>11</issue><spage>2991</spage><epage>3002</epage><pages>2991-3002</pages><issn>0304-8608</issn><eissn>1432-8798</eissn><abstract>The orthopoxvirus vaccinia virus (VACV) interacts with both actin and microtubule cytoskeletons in order to generate and spread progeny virions. Here, we present evidence demonstrating the involvement of PAK1 (p21-activated kinase 1) in the dissemination of VACV. Although PAK1 activation has previously been associated with optimal VACV entry via macropinocytosis, its absence does not affect the production of intracellular mature virions (IMVs) and extracellular enveloped virions (EEVs). Our data demonstrate that low-multiplicity infection of PAK1
-/-
MEFs leads to a reduction in plaque size followed by decreased production of both IMVs and EEVs, strongly suggesting that virus spread was impaired in the absence of PAK1. Confocal and scanning electron microscopy showed a substantial reduction in the amount of VACV-induced actin tails in PAK1
-/-
MEFs, but no significant alteration in the total amount of cell-associated enveloped virions (CEVs). Furthermore, the decreased VACV dissemination in PAK1
-/-
cells was correlated with the absence of phosphorylated ARPC1 (Thr21), a downstream target of PAK1 and a key regulatory subunit of the ARP2/3 complex, which is necessary for the formation of actin tails and viral spread. We conclude that PAK1, besides its role in virus entry, also plays a relevant role in VACV dissemination.</abstract><cop>Vienna</cop><pub>Springer Vienna</pub><pmid>27465567</pmid><doi>10.1007/s00705-016-2996-3</doi><tpages>12</tpages></addata></record> |
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subjects | Actin Animals Biological Transport Biomedical and Life Sciences Biomedicine Cells, Cultured Endocytosis Host-Pathogen Interactions Infectious Diseases Medical Microbiology Mice Mice, Knockout Microscopy, Confocal Microscopy, Electron, Scanning Original Article p21-activated kinase p21-activated kinase 1 p21-Activated Kinases - genetics p21-Activated Kinases - metabolism Poxviridae Scanning electron microscopy Vaccinia virus Vaccinia virus - physiology Virions Virology Virus Internalization Viruses |
title | Vaccinia virus dissemination requires p21-activated kinase 1 |
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