Nucleocapsid of Tomato spotted wilt tospovirus forms mobile particles that traffic on an actin/endoplasmic reticulum network driven by myosin XI-K

© 2013 The Authors. New Phytologist © 2013 New Phytologist Trust.

Bibliographische Detailangaben
Veröffentlicht in:The New phytologist. - 1979. - 200(2013), 4 vom: 01. Dez., Seite 1212-24
1. Verfasser: Feng, Zhike (VerfasserIn)
Weitere Verfasser: Chen, Xiaojiao, Bao, Yiqun, Dong, Jiahong, Zhang, Zhongkai, Tao, Xiaorong
Format: Online-Aufsatz
Sprache:English
Veröffentlicht: 2013
Zugriff auf das übergeordnete Werk:The New phytologist
Schlagworte:Journal Article Research Support, Non-U.S. Gov't Tomato spotted wilt tospovirus actin filaments endoplasmic reticulum intracellular movement myosin motor nucleocapsid Actins Bridged Bicyclo Compounds, Heterocyclic mehr... Dinitrobenzenes Nucleocapsid Proteins Plant Proteins Sulfanilamides Thiazolidines nucleocapsid protein, Tospovirus oryzalin 662E385DWH Myosins EC 3.6.4.1 latrunculin B LW7U308U7U Dimethyl Sulfoxide YOW8V9698H
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245 1 0 |a Nucleocapsid of Tomato spotted wilt tospovirus forms mobile particles that traffic on an actin/endoplasmic reticulum network driven by myosin XI-K 
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520 |a A number of viral proteins from plant viruses, other than movement proteins, have been shown to traffic intracellularly along actin filaments and to be involved in viral infection. However, there has been no report that a viral capsid protein may traffic within a cell by utilizing the actin/endoplasmic reticulum (ER) network. We used Tomato spotted wilt tospovirus (TSWV) as a model virus to study the cell biological properties of a nucleocapsid (N) protein. We found that TSWV N protein was capable of forming highly motile cytoplasmic inclusions that moved along the ER and actin network. The disruption of actin filaments by latrunculin B, an actin-depolymerizing agent, almost stopped the intracellular movement of N inclusions, whereas treatment with a microtubule-depolymerizing reagent, oryzalin, did not. The over-expression of a myosin XI-K tail, functioning in a dominant-negative manner, completely halted the movement of N inclusions. Latrunculin B treatment strongly inhibited the formation of TSWV local lesions in Nicotiana tabacum cv Samsun NN and delayed systemic infection in N. benthamiana. Collectively, our findings provide the first evidence that the capsid protein of a plant virus has the novel property of intracellular trafficking. The findings add capsid protein as a new class of viral protein that traffics on the actin/ER system 
650 4 |a Journal Article 
650 4 |a Research Support, Non-U.S. Gov't 
650 4 |a Tomato spotted wilt tospovirus 
650 4 |a actin filaments 
650 4 |a endoplasmic reticulum 
650 4 |a intracellular movement 
650 4 |a myosin motor 
650 4 |a nucleocapsid 
650 7 |a Actins  |2 NLM 
650 7 |a Bridged Bicyclo Compounds, Heterocyclic  |2 NLM 
650 7 |a Dinitrobenzenes  |2 NLM 
650 7 |a Nucleocapsid Proteins  |2 NLM 
650 7 |a Plant Proteins  |2 NLM 
650 7 |a Sulfanilamides  |2 NLM 
650 7 |a Thiazolidines  |2 NLM 
650 7 |a nucleocapsid protein, Tospovirus  |2 NLM 
650 7 |a oryzalin  |2 NLM 
650 7 |a 662E385DWH  |2 NLM 
650 7 |a Myosins  |2 NLM 
650 7 |a EC 3.6.4.1  |2 NLM 
650 7 |a latrunculin B  |2 NLM 
650 7 |a LW7U308U7U  |2 NLM 
650 7 |a Dimethyl Sulfoxide  |2 NLM 
650 7 |a YOW8V9698H  |2 NLM 
700 1 |a Chen, Xiaojiao  |e verfasserin  |4 aut 
700 1 |a Bao, Yiqun  |e verfasserin  |4 aut 
700 1 |a Dong, Jiahong  |e verfasserin  |4 aut 
700 1 |a Zhang, Zhongkai  |e verfasserin  |4 aut 
700 1 |a Tao, Xiaorong  |e verfasserin  |4 aut 
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773 1 8 |g volume:200  |g year:2013  |g number:4  |g day:01  |g month:12  |g pages:1212-24 
856 4 0 |u http://dx.doi.org/10.1111/nph.12447  |3 Volltext 
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