scholarly journals Ubiquitin-Conjugating Enzyme E2 E Inhibits the Accumulation of Rice Stripe Virus in Laodelphax striatellus (Fallén)

Viruses ◽  
2020 ◽  
Vol 12 (9) ◽  
pp. 908
Author(s):  
Yao Li ◽  
Ze Zhou ◽  
Mi Shen ◽  
Linquan Ge ◽  
Fang Liu
Keyword(s):  
Brown Planthopper ◽  
Rice Stripe Virus ◽  
Ubiquitin Proteasome System ◽  
Plant Viruses ◽  
Pcr Analysis ◽  
Laodelphax Striatellus ◽  
Protein Levels ◽  
Ubiquitin Conjugating Enzyme ◽  
Rapid Amplification ◽  
Conjugating Enzyme

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 Laodelphax striatellus, the small brown planthopper, were identified and classified into 17 groups by transcriptomic and phylogenetic analysis. Full-length cDNAs of four LstrE2s (LstrE2 A/E/G2/H) were obtained by rapid-amplification of cDNA ends (RACE-PCR) analysis. Expression of the four LstrE2s showed tissue- and development-specific patterns. RT-qPCR analyses revealed that Rice stripe viruse (RSV) infection increased the level of LstrE2 A/E/G2/H. Further study indicated that repression of LstrE2 E 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.

scholarly journals Interplay of Rice Stripe Virus and Rice Black Streaked Dwarf Virus during Their Acquisition and Accumulation in Insect Vector

Viruses ◽  
2021 ◽  
Vol 13 (6) ◽  
pp. 1121
Author(s):  
Marcia Beatriz Moya Fernández ◽  
Wenwen Liu ◽  
Lu Zhang ◽  
Jamal-U-Ddin Hajano ◽  
Xifeng Wang
Keyword(s):  
Epithelial Cells ◽  
Crop Production ◽  
Brown Planthopper ◽  
Rice Stripe Virus ◽  
Plant Viruses ◽  
Dwarf Virus ◽  
Insect Vector ◽  
Laodelphax Striatellus ◽  
Persistent Viruses ◽  
Vector Insect

Plant viruses transmitted by hemipteran vectors commonly cause losses to crop production. Rice stripe virus (RSV) and rice black streaked dwarf virus (RBSDV) are transmitted to rice plants by the same vector, the small brown planthopper (SBPH), Laodelphax striatellus Fallén, in a persistent propagative manner. However, rarely do the respective diseases they cause occur simultaneously in a field. Here, we determined the acquisition efficiency of RSV and RBSDV when acquired in succession or simultaneously by SBPH. When RBSDV was acquired first, RSV acquisition efficiency was significantly lower than when only acquiring RSV. However, RBSDV acquisition efficiency from insects that acquired RSV first was not significantly different between the insects only acquiring RBSDV. Immunofluorescence assays showed that the acquisition of RBSDV first might inhibit RSV entry into midgut epithelial cells, but RSV did not affect RBSDV entry. SBPHs were more likely to acquire RBSDV when they were feeding on plants coinfected with the two viruses. When RBSDV was acquired before RSV, RBSDV titer was significantly higher and RSV titer first declined, then increased compared to when only acquiring RBSDV or RSV. Only 5% of the SBPHs acquired both viruses when feeding on plants coinfected with RSV and RBSDV. These results provide a better understanding of the interaction between two persistent viruses when present in the same vector insect and explain why RSV and RBSDV occur in intermittent epidemics.

scholarly journals Two Ubiquitin-Conjugating Enzymes, UbcP1/Ubc4 and UbcP4/Ubc11, Have Distinct Functions for Ubiquitination of Mitotic Cyclin

2003 ◽  
Vol 23 (10) ◽  
pp. 3497-3505 ◽  
Author(s):  
Hiroaki Seino ◽  
Tsutomu Kishi ◽  
Hideo Nishitani ◽  
Fumiaki Yamao
Keyword(s):  
Fission Yeast ◽  
Ubiquitin Proteasome System ◽  
High Expression ◽  
Mitotic Cyclin ◽  
Ubiquitin Conjugating Enzyme ◽  
Conjugating Enzymes ◽  
Ubiquitin Conjugating Enzymes ◽  
Mutant Cells ◽  
Conjugating Enzyme

ABSTRACT Cell cycle events are regulated by sequential activation and inactivation of Cdk kinases. Mitotic exit is accomplished by the inactivation of mitotic Cdk kinase, which is mainly achieved by degradation of cyclins. The ubiquitin-proteasome system is involved in this process, requiring APC/C (anaphase-promoting complex/cyclosome) as a ubiquitin ligase. In Xenopus and clam oocytes, the ubiquitin-conjugating enzymes that function with APC/C have been identified as two proteins, UBC4 and UBCx/E2-C. Previously we reported that the fission yeast ubiquitin-conjugating enzyme UbcP4/Ubc11, a homologue of UBCx/E2-C, is required for mitotic transition. Here we show that the other fission yeast ubiquitin-conjugating enzyme, UbcP1/Ubc4, which is homologous to UBC4, is also required for mitotic transition in the same manner as UbcP4/Ubc11. Both ubiquitin-conjugating enzymes are essential for cell division and directly required for the degradation of mitotic cyclin Cdc13. They function nonredundantly in the ubiquitination of CDC13 because a defect in ubcP1/ubc4 + cannot be suppressed by high expression of UbcP4/Ubc11 and a defect in ubcP4/ubc11 + cannot be suppressed by high expression of UbcP1/Ubc4. In vivo analysis of the ubiquitinated state of Cdc13 shows that the ubiquitin chains on Cdc13 were short in ubcP1/ubc4 mutant cells while ubiquitinated Cdc13 was totally reduced in ubcP4/ubc11 mutant cells. Taken together, these results indicate that the two ubiquitin-conjugating enzymes play distinct and essential roles in the degradation of mitotic cyclin Cdc13, with the UbcP4/Ubc11-pathway initiating ubiquitination of Cdc13 and the UbcP1/Ubc4-pathway elongating the short ubiquitin chains on Cdc13.

scholarly journals Elevating the level of Cdc34/Ubc3 ubiquitin-conjugating enzyme in mitosis inhibits association of CENP-E with kinetochores and blocks the metaphase alignment of chromosomes

2001 ◽  
Vol 154 (4) ◽  
pp. 707-718 ◽  
Author(s):  
Leana M. Topper ◽  
Holger Bastians ◽  
Joan V. Ruderman ◽  
Gary J. Gorbsky
Keyword(s):  
Mammalian Cells ◽  
Proteasome Inhibitors ◽  
Metaphase Plate ◽  
Cytoplasmic Dynein ◽  
Mitogen Activated Protein Kinase ◽  
Protein Levels ◽  
Mitogen Activated Protein ◽  
Associated Proteins ◽  
Ubiquitin Conjugating Enzyme ◽  
Conjugating Enzyme

Cdc34/Ubc3 is a ubiquitin-conjugating enzyme that functions in targeting proteins for proteasome-mediated degradation at the G1 to S cell cycle transition. Elevation of Cdc34 protein levels by microinjection of bacterially expressed Cdc34 into mammalian cells at prophase inhibited chromosome congression to the metaphase plate with many chromosomes remaining near the spindle poles. Chromosome condensation and nuclear envelope breakdown occurred normally, and chromosomes showed oscillatory movements along mitotic spindle microtubules. Most injected cells arrested in a prometaphase-like state. Kinetochores, even those of chromosomes that failed to congress, possessed the normal trilaminar plate ultrastructure. The elevation of Cdc34 protein levels in early mitosis selectively blocked centromere protein E (CENP-E), a mitotic kinesin, from associating with kinetochores. Other proteins, including two CENP-E–associated proteins, BubR1 and phospho-p42/p44 mitogen-activated protein kinase, and mitotic centromere-associated kinesin, cytoplasmic dynein, Cdc20, and Mad2, all exhibited normal localization to kinetochores. Proteasome inhibitors did not affect the prometaphase arrest induced by Cdc34 injection. These studies suggest that CENP-E targeting to kinetochores is regulated by ubiquitylation not involving proteasome-mediated degradation.

Detecting Rice stripe virus (RSV) in the small brown planthopper (Laodelphax striatellus) with high specificity by RT-PCR

2003 ◽  
Vol 112 (1-2) ◽  
pp. 115-120 ◽  
Author(s):  
Cai Lijun ◽  
Ma Xizhi ◽  
Kang Lin ◽  
Deng Kejing ◽  
Zhao Shouyuan ◽  
...  
Keyword(s):  
Brown Planthopper ◽  
Rice Stripe Virus ◽  
High Specificity ◽  
Laodelphax Striatellus ◽  
Rt Pcr ◽  
Small Brown Planthopper

scholarly journals The α-tubulin of Laodelphax striatellus facilitates the passage of rice stripe virus (RSV) and enhances horizontal transmission

2018 ◽  
Author(s):  
Yao Li ◽  
Danyu Chen ◽  
Jia Hu ◽  
Lu Zhang ◽  
Yin Xiang ◽  
...  
Keyword(s):  
Salivary Glands ◽  
Nonstructural Protein ◽  
Horizontal Transmission ◽  
Brown Planthopper ◽  
Rice Stripe Virus ◽  
Laodelphax Striatellus ◽  
Rice Stripe Disease ◽  
Rsv Infection

Rice stripe virus (RSV), causal agent of rice stripe disease, is transmitted by the small brown planthopper (SBPH, Laodelphax striatellus) in a persistent manner. The midgut and salivary glands of SBPH are the first and last barriers in viral circulation and transmission, respectively; however, the precise mechanisms used by RSV to cross these organs and re-inoculate rice have not been fully elucidated. We obtained full-length cDNA of L. striatellus α-tubulin 2 (LsTUB) and found that RSV infection increased the level of LsTUB in vivo. Furthermore, LsTUB was shown to bind the RSV nonstructural protein 3 (NS3) in vitro. RNAi was used to reduce LsTUB expression, which caused a significant reduction in RSV titer, NS3 expression, RSV inoculation rates, and transmission to healthy plants. Electrical penetration graphs (EPG) showed that LsTUB knockdown by RNAi did not impact SBPH feeding; therefore, the reduction in RSV inoculation rate was likely caused by the decrease in RSV transmission. These findings suggest that LsTUB mediates the passage of RSV through midgut and salivary glands and leads to successful horizontal transmission.

scholarly journals Sublethal Effects of Imidacloprid on Fecundity, Apoptosis and Virus Transmission in the Small Brown Planthopper Laodelphax striatellus

Insects ◽  
2021 ◽  
Vol 12 (12) ◽  
pp. 1131
Author(s):  
Yuanyuan Zhang ◽  
Gang Xu ◽  
Yu Jiang ◽  
Chao Ma ◽  
Guoqing Yang
Keyword(s):  
Sublethal Effects ◽  
Control Strategies ◽  
Brown Planthopper ◽  
Virus Transmission ◽  
Rice Stripe Virus ◽  
Underlying Mechanism ◽  
Terminal Deoxynucleotidyl Transferase ◽  
Laodelphax Striatellus ◽  
Expression Levels ◽  
Sublethal Concentrations

Laodelphax striatellus damages plants directly through sucking plant sap and indirectly as a vector of rice stripe virus (RSV), resulting in serious losses of rice yield. It is one of the most destructive insects of rice in East Asia. Insecticides are primarily used for pest management, but the sublethal concentrations of insecticides may benefit several insects. The present research attempted to explore the effects of sublethal concentrations of imidacloprid on the fecundity, apoptosis and RSV transmission in the viruliferous SBPH. The results showed that the fecundity of SBPH was significantly increased after treatment with the LC10 dose of imidacloprid, while the LC30 dose of imidacloprid reduced the fecundity compared with the control. To further investigate the underlying mechanism of increased fecundity after exposure to the LC10 dose of imidacloprid, we examined the expression levels of vitellogenin (Vg), Vg receptor (VgR) and caspases in the ovaries of SBPH, and observed the apoptosis by terminal deoxynucleotidyl transferase (TDT)-mediated dUTP-digoxigenin nick end labeling (TUNEL). qRT-PCR results indicated that the expression levels of Vg, VgR and four caspase genes were all significantly increased by the LC10 dose of imidacloprid, and TUNEL assays suggested that the frequency of apoptosis was significantly higher in the SBPH treated by the LC10 dose of imidacloprid, suggesting a potential correlation between the increased fecundity and the apoptosis of SBPH ovarioles. Additionally, the expression levels of RNA3 and capsid protein (CP) were both increased significantly by the LC10 dose of imidacloprid, whereas were decreased by the LC30 dose of imidacloprid compared to the control. Therefore, this study clarifies the mechanisms of sublethal effects of imidacloprid on viruliferous SBPH and could be used to optimize pest control strategies.

The human ubiquitin-conjugating enzyme Cdc34 controls cellular proliferation through regulation of p27Kip1 protein levels

2005 ◽  
Vol 303 (2) ◽  
pp. 482-493 ◽  
Author(s):  
Nicole Butz ◽  
Stephan Ruetz ◽  
Francois Natt ◽  
Jonathan Hall ◽  
Jan Weiler ◽  
...  
Keyword(s):  
Cellular Proliferation ◽  
P27kip1 Protein ◽  
Protein Levels ◽  
Human Ubiquitin ◽  
Ubiquitin Conjugating Enzyme ◽  
Conjugating Enzyme
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