{"id":229,"date":"2014-02-11T08:48:42","date_gmt":"2014-02-11T08:48:42","guid":{"rendered":"http:\/\/www.virologyhighlights.com\/?p=229"},"modified":"2018-05-25T08:17:43","modified_gmt":"2018-05-25T08:17:43","slug":"turnip-crinkle-virus-uses-coat-protein-to-alter-disease-development","status":"publish","type":"post","link":"https:\/\/www.elsevierblogs.com\/virology\/turnip-crinkle-virus-uses-coat-protein-to-alter-disease-development\/","title":{"rendered":"Turnip crinkle virus uses coat protein to alter disease development"},"content":{"rendered":"<p><b>Turnip crinkle virus coat protein inhibits the basal immune response to virus invasion in <i>Arabidopsis<\/i> by binding to the NAC transcription factor TIP<\/b><\/p>\n<p><a href=\"http:\/\/www.sciencedirect.com\/science\/article\/pii\/S0042682213006387\">Read the full article on ScienceDirect<\/a>.<\/p>\n<p>The innate immune system used in any organism against a pathogen is a complicated dance of gene expression and protein interaction. Therefore a major challenge in plant biology is to understand the molecular basis of pathogenesis and the mechanisms by which plants defend themselves against plant pathogens.<\/p>\n<p>In our study, we focused on the exposing a key part of the innate immune defense system of <i>Arabidopsis<\/i> against the model virus, Turnip crinkle virus (TCV). Previous work done by our lab revealed the coat protein (CP) of TCV has the ability to bind to a transcription factor, TIP, and alter the disease development associated with the infection. We monitored virus accumulation and gene expression in <i>Arabidopsis<\/i> infected with wildtype TCV or the TCV mutant, R6A, which cannot bind TIP. We were able to reveal that TCV gained a reproductive advantage by evolving the ability to bind TIP and alter disease progression. The altered disease symptoms were linked to TCV altering the salicylic acid hormone signaling pathway and the induction of the senescence which lead to a decrease in virus accumulation and an increase in disease symptoms during R6A infection. This work helps us understand one of the key roles that the CP plays in slowing down the innate immune defense signaling against TCV.<\/p>\n<p>The next step will be to further explore R6A and other TCV mutants in the resistant <em>Arabidopsis<\/em> ecotype Dijon-17 and how TIP interaction affects the TCV mutants in overcoming the resistance mechanisms.<\/p>\n<figure id=\"attachment_230\" aria-describedby=\"caption-attachment-230\" style=\"width: 520px\" class=\"wp-caption alignnone\"><a href=\"http:\/\/www.elsevierblogs.com\/virology\/wp-content\/uploads\/2014\/02\/TCV-model-12-14-13.jpg\"><img loading=\"lazy\" decoding=\"async\" class=\"size-large wp-image-230 \" alt=\"Model of the TIP-TCV CP interaction during TCV infection in the susceptible host Col-0. We propose that TCV CP is recognized by an uncharacterized toll-like receptor (TLR) that provokes SA defense signaling with a leucine rich repeat (LRR) domain for protein-protein interaction and a transmembrane domain (TM). The TLR kinase domain (KD) signaling leads to a MAPK cascade and enhanced basal defense. Infection by wildtype TCV results in the interaction of the CP with TIP that alters the rate of migration into the nucleus leading to the basal defense genes not being induced. Infection by the TCV mutant, R6A, is unable to repress the basal defense response because it can\u2019t interact with TIP. This difference in basal defense regulation in the susceptible host gives a selective advantage to TCV early in infection.\" src=\"http:\/\/www.elsevierblogs.com\/virology\/wp-content\/uploads\/2014\/02\/TCV-model-12-14-13-1024x768.jpg\" width=\"520\" height=\"390\" srcset=\"https:\/\/www.elsevierblogs.com\/virology\/wp-content\/uploads\/2014\/02\/TCV-model-12-14-13-1024x768.jpg 1024w, https:\/\/www.elsevierblogs.com\/virology\/wp-content\/uploads\/2014\/02\/TCV-model-12-14-13-300x225.jpg 300w\" sizes=\"auto, (max-width: 520px) 100vw, 520px\" \/><\/a><figcaption id=\"caption-attachment-230\" class=\"wp-caption-text\">Model of the TIP-TCV CP interaction during TCV infection in the susceptible host Col-0. We propose that TCV CP is recognized by an uncharacterized toll-like receptor (TLR) that provokes SA defense signaling with a leucine rich repeat (LRR) domain for protein-protein interaction and a transmembrane domain (TM). The TLR kinase domain (KD) signaling leads to a MAPK cascade and enhanced basal defense. Infection by wildtype TCV results in the interaction of the CP with TIP that alters the rate of migration into the nucleus leading to the basal defense genes not being induced. Infection by the TCV mutant, R6A, is unable to repress the basal defense response because it can\u2019t interact with TIP. This difference in basal defense regulation in the susceptible host gives a selective advantage to TCV early in infection.<\/figcaption><\/figure>\n<p><b>Introducing the authors<\/b><\/p>\n<p><a href=\"http:\/\/www.elsevierblogs.com\/virology\/wp-content\/uploads\/2014\/02\/Donze.jpg\"><img loading=\"lazy\" decoding=\"async\" class=\"size-medium wp-image-231 alignnone\" alt=\"Donze\" src=\"http:\/\/www.elsevierblogs.com\/virology\/wp-content\/uploads\/2014\/02\/Donze-300x225.jpg\" width=\"338\" height=\"254\" srcset=\"https:\/\/www.elsevierblogs.com\/virology\/wp-content\/uploads\/2014\/02\/Donze-300x225.jpg 300w, https:\/\/www.elsevierblogs.com\/virology\/wp-content\/uploads\/2014\/02\/Donze-1024x768.jpg 1024w\" sizes=\"auto, (max-width: 338px) 100vw, 338px\" \/><\/a><a href=\"http:\/\/www.elsevierblogs.com\/virology\/wp-content\/uploads\/2014\/02\/Morris-at-the-bench.jpg\"><img loading=\"lazy\" decoding=\"async\" alt=\"Morris at the bench\" src=\"http:\/\/www.elsevierblogs.com\/virology\/wp-content\/uploads\/2014\/02\/Morris-at-the-bench.jpg\" width=\"265\" height=\"255\" \/><\/a><\/p>\n<p>Teresa Donze and Jack Morris<br \/>\n<a href=\"http:\/\/biosci.unl.edu\/\">School of Biological Sciences<\/a>, University of Nebraska-Lincoln, USA<\/p>\n<p><b>About the research<\/b><\/p>\n<p><a href=\"http:\/\/www.sciencedirect.com\/science\/article\/pii\/S0042682213006387\">Turnip crinkle virus coat protein inhibits the basal immune response to virus invasion in Arabidopsis by binding to the NAC transcription factor TIP<\/a><br \/>\n<i>Virology<\/i>, Volume 449, 20 January 2014, Pages 207\u2013214<br \/>\nTeresa Donze, Feng Qu, Paul Twigg, T. Jack Morris<\/p>\n<p><a href=\"http:\/\/www.sciencedirect.com\/science\/article\/pii\/S0042682213006387\">Read the full article on ScienceDirect<\/a>.<\/p>\n<!-- AddThis Advanced Settings generic via filter on the_content --><!-- AddThis Share Buttons generic via filter on the_content -->","protected":false},"excerpt":{"rendered":"<p>Turnip crinkle virus coat protein inhibits the basal immune response to virus invasion in Arabidopsis by binding to the NAC transcription factor TIP Read the full article on ScienceDirect. The innate immune system used in any organism against a pathogen is a complicated dance of gene expression and protein interaction. Therefore a major challenge in <a class=\"read-more\" href=\"https:\/\/www.elsevierblogs.com\/virology\/turnip-crinkle-virus-uses-coat-protein-to-alter-disease-development\/\">Read More&#8230;<\/a><!-- AddThis Advanced Settings generic via filter on get_the_excerpt --><!-- AddThis Share Buttons generic via filter on get_the_excerpt --><\/p>\n","protected":false},"author":1,"featured_media":230,"comment_status":"closed","ping_status":"open","sticky":false,"template":"","format":"standard","meta":{"footnotes":""},"categories":[5,632,631],"tags":[142,144,143,141],"class_list":["post-229","post","type-post","status-publish","format-standard","has-post-thumbnail","hentry","category-highlighted-article","category-immunity-to-viruses","category-viral-pathogenesis","tag-coat-protein","tag-disease-progression","tag-tcv","tag-turnip-crinkle-virus"],"_links":{"self":[{"href":"https:\/\/www.elsevierblogs.com\/virology\/wp-json\/wp\/v2\/posts\/229","targetHints":{"allow":["GET"]}}],"collection":[{"href":"https:\/\/www.elsevierblogs.com\/virology\/wp-json\/wp\/v2\/posts"}],"about":[{"href":"https:\/\/www.elsevierblogs.com\/virology\/wp-json\/wp\/v2\/types\/post"}],"author":[{"embeddable":true,"href":"https:\/\/www.elsevierblogs.com\/virology\/wp-json\/wp\/v2\/users\/1"}],"replies":[{"embeddable":true,"href":"https:\/\/www.elsevierblogs.com\/virology\/wp-json\/wp\/v2\/comments?post=229"}],"version-history":[{"count":3,"href":"https:\/\/www.elsevierblogs.com\/virology\/wp-json\/wp\/v2\/posts\/229\/revisions"}],"predecessor-version":[{"id":235,"href":"https:\/\/www.elsevierblogs.com\/virology\/wp-json\/wp\/v2\/posts\/229\/revisions\/235"}],"wp:featuredmedia":[{"embeddable":true,"href":"https:\/\/www.elsevierblogs.com\/virology\/wp-json\/wp\/v2\/media\/230"}],"wp:attachment":[{"href":"https:\/\/www.elsevierblogs.com\/virology\/wp-json\/wp\/v2\/media?parent=229"}],"wp:term":[{"taxonomy":"category","embeddable":true,"href":"https:\/\/www.elsevierblogs.com\/virology\/wp-json\/wp\/v2\/categories?post=229"},{"taxonomy":"post_tag","embeddable":true,"href":"https:\/\/www.elsevierblogs.com\/virology\/wp-json\/wp\/v2\/tags?post=229"}],"curies":[{"name":"wp","href":"https:\/\/api.w.org\/{rel}","templated":true}]}}