Youzhi Li

Dr. Youzhi Li


Research Focus & Metrics

Academic Career Length

12Years (2015-Present)

(Calculated once Scilit publication data is synced: current year − year of first publication + 1)

Representative Publications

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19 December 2019 in Frontiers in Physiology
Verified
Journal Article
Open access
KHKui Hu
Kui Hu
PTPing Tian
Ping Tian
YTYan Tang
Yan Tang
LYLu Yang
Lu Yang
LQLin Qiu
Lin Qiu
YLYouzhi Li
Youzhi Li
The yolk protein precursor, vitellogenin (Vg), provides nutrition for embryonic development whereas the vitellogenin receptor (VgR) is responsible for the uptake of yolk protein by maturing oocytes. These two proteins are key reproduction-related proteins in insects. We cloned and characterized Vg and VgR genes in Sogatella furcifera, and investigated their function in oocyte maturation. Cloned SfVg and SfVgR have open reading frames of 6 114 and 5 796 bp, encoding 2 037 and 1 931 amino acid residues, respectively. Structural analysis indicates that SfVg has the three conserved LPD_N, DUF1943 and VWFD domains, SfVgR contains all conservative motifs of the LDLR superfamily. Both genes were highly expressed in adult females; SfVg was most highly expressed in the fat body whereas SfVgR was mainly expressed in the ovary. Knockdown of either gene reduced yolk protein deposition in oocytes and arrested oocyte maturation. However, silencing one of these two genes did not affect the transcript level of the other. These results demonstrate the role of SfVgR in transporting SfVg into oocytes. Both SfVg and SfVgR are essential for oocyte maturation in S. furcifera and both genes could potentially be targeted as means of controlling this pest.

30 September 2019 in Insect Molecular Biology
Verified
Journal Article
Closed access
PDF file
YTY. Tang
Y. Tang
HHH. He
H. He
XQX. Qu
X. Qu
YCY. Cai
Y. Cai
WDW. Ding
W. Ding
YLYouzhi Li
Youzhi Li

1 June 2020 in Comparative Biochemistry and Physiology Part D: Genomics and Proteomics
Verified
Journal Article
Closed access
LQLin Qiu
Lin Qiu
LHLi He
Li He
XTXiaoping Tan
Xiaoping Tan
ZZZhengbing Zhang
Zhengbing Zhang
YWYong Wang
Yong Wang
YLYouzhi Li
Youzhi Li

7 March 2019 in PeerJ
Verified
Journal Article
Open access
PDF file
KHKui Hu
Kui Hu
SLSheng Liu
Sheng Liu
LQLin Qiu
Lin Qiu
YLYouzhi Li
Youzhi Li
Plant volatiles play an important role in regulating insect behavior. Odorant binding proteins (OBPs) are involved in the first step of the olfactory signal transduction pathway and plant volatiles recognition. Sogatella furcifera is one of the most destructive pests of rice crops. Understanding the functions of S. furcifera OBPs (SfurOBPs) in the host plant location and the behavioral responses of S. furcifera to rice plant volatiles could lead to improved, more environmentally-friendly, methods for controlling this pest. We found that SfurOBP1 displayed only weak binding with all the tested volatiles. SfurOBP2, SfurOBP3 and SfurOBP11 had different binding affinities to β-ionone. SfurOBP2 and SfurOBP11 had strong binding affinities to β-caryophyllene (Ki = 2.23 µM) and plant alcohol (Ki = 2.98 µM), respectively. The results of Y-olfactometer experiments indicate that S. furcifera was significantly repelled by octanal and n-octane but strongly attracted by (+)-limonene, acetophenone, 2-heptanone, n-hendecane, α-farnesene and β-ionone. Furthermore, the dsRNA-mediated gene silencing of SfurOBP2, SfurOBP3 and SfurOBP11 shifted the olfactory behavior of S. furcifera for β-ionone, α-farnesene and plant alcohol, respectively. These results suggest that the SfurOBPs are involved in the recognition of rice plant volatiles, and several potential repellants and lures for controlling this pest.

29 November 2019 in Molecular Biology Reports
Verified
Journal Article
Closed access
PDF file
KHKui Hu
Kui Hu
PTPing Tian
Ping Tian
LYLu Yang
Lu Yang
YTYan Tang
Yan Tang
LQLin Qiu
Lin Qiu
YLYouzhi Li
Youzhi Li

7 April 2021 in Journal of Pest Science
Verified
Journal Article
Closed access
PDF file
HHHualiang He
Hualiang He
AZAilin Zhou
Ailin Zhou
LHLi He
Li He
LQLin Qiu
Lin Qiu
WDWenbing Ding
Wenbing Ding
YLYouzhi Li
Youzhi Li