The Lipid Transfer Protein 1 from <i>Nicotiana benthamiana</i> Assists <i>Bamboo mosaic virus</i> Accumulation
Host factors play a pivotal role in regulating virus infection. Uncovering the mechanism of how host factors are involved in virus infection could pave the way to defeat viral disease. In this study, we characterized a lipid transfer protein, designated <i>NbLTP1</i> in <i>Nicotian...
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MDPI AG
2020-11-01
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| Series: | Viruses |
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| Online Access: | https://www.mdpi.com/1999-4915/12/12/1361 |
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| author | Ling-Ying Chiu I-Hsuan Chen Yau-Heiu Hsu Ching-Hsiu Tsai |
| author_facet | Ling-Ying Chiu I-Hsuan Chen Yau-Heiu Hsu Ching-Hsiu Tsai |
| author_sort | Ling-Ying Chiu |
| collection | DOAJ |
| description | Host factors play a pivotal role in regulating virus infection. Uncovering the mechanism of how host factors are involved in virus infection could pave the way to defeat viral disease. In this study, we characterized a lipid transfer protein, designated <i>NbLTP1</i> in <i>Nicotiana benthamiana,</i> which was downregulated after <i>Bamboo mosaic virus</i> (BaMV) inoculation. BaMV accumulation significantly decreased in NbLTP1-knockdown leaves and protoplasts compared with the controls. The subcellular localization of the NbLTP1-orange fluorescent protein (OFP) was mainly the extracellular matrix. However, when we removed the signal peptide (NbLTP1/ΔSP-OFP), most of the expressed protein targeted chloroplasts. Both NbLTP1-OFP and NbLTP1/ΔSP-OFP were localized in chloroplasts when we removed the cell wall. These results suggest that NbLTP1 may have a secondary targeting signal. Transient overexpression of NbLTP1 had no effect on BaMV accumulation, but that of NbLTP1/ΔSP significantly increased BaMV expression. NbLTP1 may be a positive regulator of BaMV accumulation especially when its expression is associated with chloroplasts, where BaMV replicates. The mutation was introduced to the predicted phosphorylation site to simulate the phosphorylated status, NbLTP/ΔSP/P(+), which could still assist BaMV accumulation. By contrast, a mutant lacking calmodulin-binding or simulates the phosphorylation-negative status could not support BaMV accumulation. The lipid-binding activity of LTP1 was reported to be associated with calmodulin-binding and phosphorylation, by which the C-terminus functional domain of NbLTP1 may play a critical role in BaMV accumulation. |
| first_indexed | 2024-03-10T14:29:52Z |
| format | Article |
| id | doaj.art-5b1e83e381ba4ad88786bcde9fc8ea89 |
| institution | Directory Open Access Journal |
| issn | 1999-4915 |
| language | English |
| last_indexed | 2024-03-10T14:29:52Z |
| publishDate | 2020-11-01 |
| publisher | MDPI AG |
| record_format | Article |
| series | Viruses |
| spelling | doaj.art-5b1e83e381ba4ad88786bcde9fc8ea892023-11-20T22:41:37ZengMDPI AGViruses1999-49152020-11-011212136110.3390/v12121361The Lipid Transfer Protein 1 from <i>Nicotiana benthamiana</i> Assists <i>Bamboo mosaic virus</i> AccumulationLing-Ying Chiu0I-Hsuan Chen1Yau-Heiu Hsu2Ching-Hsiu Tsai3Graduate Institute of Biotechnology, National Chung Hsing University, Taichung 402, TaiwanGraduate Institute of Biotechnology, National Chung Hsing University, Taichung 402, TaiwanGraduate Institute of Biotechnology, National Chung Hsing University, Taichung 402, TaiwanGraduate Institute of Biotechnology, National Chung Hsing University, Taichung 402, TaiwanHost factors play a pivotal role in regulating virus infection. Uncovering the mechanism of how host factors are involved in virus infection could pave the way to defeat viral disease. In this study, we characterized a lipid transfer protein, designated <i>NbLTP1</i> in <i>Nicotiana benthamiana,</i> which was downregulated after <i>Bamboo mosaic virus</i> (BaMV) inoculation. BaMV accumulation significantly decreased in NbLTP1-knockdown leaves and protoplasts compared with the controls. The subcellular localization of the NbLTP1-orange fluorescent protein (OFP) was mainly the extracellular matrix. However, when we removed the signal peptide (NbLTP1/ΔSP-OFP), most of the expressed protein targeted chloroplasts. Both NbLTP1-OFP and NbLTP1/ΔSP-OFP were localized in chloroplasts when we removed the cell wall. These results suggest that NbLTP1 may have a secondary targeting signal. Transient overexpression of NbLTP1 had no effect on BaMV accumulation, but that of NbLTP1/ΔSP significantly increased BaMV expression. NbLTP1 may be a positive regulator of BaMV accumulation especially when its expression is associated with chloroplasts, where BaMV replicates. The mutation was introduced to the predicted phosphorylation site to simulate the phosphorylated status, NbLTP/ΔSP/P(+), which could still assist BaMV accumulation. By contrast, a mutant lacking calmodulin-binding or simulates the phosphorylation-negative status could not support BaMV accumulation. The lipid-binding activity of LTP1 was reported to be associated with calmodulin-binding and phosphorylation, by which the C-terminus functional domain of NbLTP1 may play a critical role in BaMV accumulation.https://www.mdpi.com/1999-4915/12/12/1361BaMVLTP1chloroplast-localizationviral RNA accumulationcalmodulin-bindingdual-localization |
| spellingShingle | Ling-Ying Chiu I-Hsuan Chen Yau-Heiu Hsu Ching-Hsiu Tsai The Lipid Transfer Protein 1 from <i>Nicotiana benthamiana</i> Assists <i>Bamboo mosaic virus</i> Accumulation Viruses BaMV LTP1 chloroplast-localization viral RNA accumulation calmodulin-binding dual-localization |
| title | The Lipid Transfer Protein 1 from <i>Nicotiana benthamiana</i> Assists <i>Bamboo mosaic virus</i> Accumulation |
| title_full | The Lipid Transfer Protein 1 from <i>Nicotiana benthamiana</i> Assists <i>Bamboo mosaic virus</i> Accumulation |
| title_fullStr | The Lipid Transfer Protein 1 from <i>Nicotiana benthamiana</i> Assists <i>Bamboo mosaic virus</i> Accumulation |
| title_full_unstemmed | The Lipid Transfer Protein 1 from <i>Nicotiana benthamiana</i> Assists <i>Bamboo mosaic virus</i> Accumulation |
| title_short | The Lipid Transfer Protein 1 from <i>Nicotiana benthamiana</i> Assists <i>Bamboo mosaic virus</i> Accumulation |
| title_sort | lipid transfer protein 1 from i nicotiana benthamiana i assists i bamboo mosaic virus i accumulation |
| topic | BaMV LTP1 chloroplast-localization viral RNA accumulation calmodulin-binding dual-localization |
| url | https://www.mdpi.com/1999-4915/12/12/1361 |
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