Ubiquitin-Conjugating Enzyme E2 E Inhibits the Accumulation of Rice Stripe Virus in <i>Laodelphax striatellus</i> (Fallén)
The ubiquitin–proteasome system (UPS) is an essential protagonist in host–pathogen interactions. Among the three classes of enzymes in the UPS, ubiquitin-conjugating enzyme E2 plays a dual role in viral pathogenesis; however, the role of insect E2s in interactions with plant viruses is unclear. Twen...
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MDPI AG
2020-08-01
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| Series: | Viruses |
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| Online Access: | https://www.mdpi.com/1999-4915/12/9/908 |
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| author | Yao Li Ze Zhou Mi Shen Linquan Ge Fang Liu |
| author_facet | Yao Li Ze Zhou Mi Shen Linquan Ge Fang Liu |
| author_sort | Yao Li |
| collection | DOAJ |
| description | The ubiquitin–proteasome system (UPS) is an essential protagonist in host–pathogen interactions. Among the three classes of enzymes in the UPS, ubiquitin-conjugating enzyme E2 plays a dual role in viral pathogenesis; however, the role of insect E2s in interactions with plant viruses is unclear. Twenty E2-encoding genes in <i>Laodelphax striatellus</i>, the small brown planthopper, were identified and classified into 17 groups by transcriptomic and phylogenetic analysis. Full-length cDNAs of four <i>LstrE2s</i> (<i>LstrE2 A/E/G2/H</i>) were obtained by rapid-amplification of cDNA ends (RACE-PCR) analysis. Expression of the four <i>LstrE2s</i> showed tissue- and development-specific patterns. RT-qPCR analyses revealed that Rice stripe viruse (RSV) infection increased the level of <i>LstrE2 A/E/G2/H</i>. Further study indicated that repression of <i>LstrE2 E</i> via RNAi caused significant increases in the expression of RSV coat protein mRNA and protein levels. These findings suggest that LstrE2 E inhibits RSV accumulation in the planthopper body. Understanding the function of LstrE2 E in RSV accumulation may ultimately result in the development of novel antiviral strategies. |
| first_indexed | 2024-03-10T17:12:06Z |
| format | Article |
| id | doaj.art-74c7a35e663843ca980402e4c90cee26 |
| institution | Directory Open Access Journal |
| issn | 1999-4915 |
| language | English |
| last_indexed | 2024-03-10T17:12:06Z |
| publishDate | 2020-08-01 |
| publisher | MDPI AG |
| record_format | Article |
| series | Viruses |
| spelling | doaj.art-74c7a35e663843ca980402e4c90cee262023-11-20T10:38:05ZengMDPI AGViruses1999-49152020-08-0112990810.3390/v12090908Ubiquitin-Conjugating Enzyme E2 E Inhibits the Accumulation of Rice Stripe Virus in <i>Laodelphax striatellus</i> (Fallén)Yao Li0Ze Zhou1Mi Shen2Linquan Ge3Fang Liu4College of Horticulture and Plant Protection, Yangzhou University, Yangzhou 225009, ChinaCollege of Horticulture and Plant Protection, Yangzhou University, Yangzhou 225009, ChinaCollege of Horticulture and Plant Protection, Yangzhou University, Yangzhou 225009, ChinaCollege of Horticulture and Plant Protection, Yangzhou University, Yangzhou 225009, ChinaCollege of Horticulture and Plant Protection, Yangzhou University, Yangzhou 225009, ChinaThe ubiquitin–proteasome system (UPS) is an essential protagonist in host–pathogen interactions. Among the three classes of enzymes in the UPS, ubiquitin-conjugating enzyme E2 plays a dual role in viral pathogenesis; however, the role of insect E2s in interactions with plant viruses is unclear. Twenty E2-encoding genes in <i>Laodelphax striatellus</i>, the small brown planthopper, were identified and classified into 17 groups by transcriptomic and phylogenetic analysis. Full-length cDNAs of four <i>LstrE2s</i> (<i>LstrE2 A/E/G2/H</i>) were obtained by rapid-amplification of cDNA ends (RACE-PCR) analysis. Expression of the four <i>LstrE2s</i> showed tissue- and development-specific patterns. RT-qPCR analyses revealed that Rice stripe viruse (RSV) infection increased the level of <i>LstrE2 A/E/G2/H</i>. Further study indicated that repression of <i>LstrE2 E</i> via RNAi caused significant increases in the expression of RSV coat protein mRNA and protein levels. These findings suggest that LstrE2 E inhibits RSV accumulation in the planthopper body. Understanding the function of LstrE2 E in RSV accumulation may ultimately result in the development of novel antiviral strategies.https://www.mdpi.com/1999-4915/12/9/908<i>Laodelphax striatellus</i>rice stripe virusubiquitin-conjugating enzyme E2viral accumulation |
| spellingShingle | Yao Li Ze Zhou Mi Shen Linquan Ge Fang Liu Ubiquitin-Conjugating Enzyme E2 E Inhibits the Accumulation of Rice Stripe Virus in <i>Laodelphax striatellus</i> (Fallén) Viruses <i>Laodelphax striatellus</i> rice stripe virus ubiquitin-conjugating enzyme E2 viral accumulation |
| title | Ubiquitin-Conjugating Enzyme E2 E Inhibits the Accumulation of Rice Stripe Virus in <i>Laodelphax striatellus</i> (Fallén) |
| title_full | Ubiquitin-Conjugating Enzyme E2 E Inhibits the Accumulation of Rice Stripe Virus in <i>Laodelphax striatellus</i> (Fallén) |
| title_fullStr | Ubiquitin-Conjugating Enzyme E2 E Inhibits the Accumulation of Rice Stripe Virus in <i>Laodelphax striatellus</i> (Fallén) |
| title_full_unstemmed | Ubiquitin-Conjugating Enzyme E2 E Inhibits the Accumulation of Rice Stripe Virus in <i>Laodelphax striatellus</i> (Fallén) |
| title_short | Ubiquitin-Conjugating Enzyme E2 E Inhibits the Accumulation of Rice Stripe Virus in <i>Laodelphax striatellus</i> (Fallén) |
| title_sort | ubiquitin conjugating enzyme e2 e inhibits the accumulation of rice stripe virus in i laodelphax striatellus i fallen |
| topic | <i>Laodelphax striatellus</i> rice stripe virus ubiquitin-conjugating enzyme E2 viral accumulation |
| url | https://www.mdpi.com/1999-4915/12/9/908 |
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