Literature DB >> 31793737

Identification of four caspase genes from Spodoptera exigua (Lepidoptera: Noctuidae) and their regulations toward different apoptotic stimulations.

Huan Yu1,2, Zi-Qi Li1,2, Yi-Yi Ou-Yang1,2, Guo-Hua Huang1,2.   

Abstract

Apoptosis plays critical roles in multiple biological processes in multicellular organisms. Caspases are known as important participators and regulators of apoptosis. Here, four novel caspase genes of Spodoptera exigua were cloned and characterized, which were designated as SeCasp-1, SeCasp-6, SeCasp-7 and SeCasp-8. Analysis of the putative encoded protein sequences of these SeCasps indicated that SeCasp-1 and SeCasp-7 were possible homologs of executor caspases; SeCasp-8 was a possible homolog of initiator caspases; and SeCasp-6 was a unique caspase of S. exigua that shares low similarity with all the identified insect caspases. Based on baculovirus expression system analyses, SeCasp-1 exhibited similar caspase activity to human caspase-1, -3, -4, -6, -8 and -9; SeCasp-6 presented similar caspase activity to human caspase-2, -3, -4, -6, -8 and -9; SeCasp-7 exhibited similar caspase activity to human caspase-2, -3 and -6; and SeCasp-8 presented similar caspase activity only to human caspase-8. Induction with different chemicals revealed that SeCasp-1 showed extreme upregulation after 24 h in the treated fat body cell line (IOZCAS-Spex-II) of S. exigua. Developmental expression analysis revealed that SeCasp-1 was highly transcribed in the larval stages, while SeCasp-6, SeCasp-7, SeCasp-8 were down-regulated. The in vivo detection of the relative expression levels of SeCasps in S. eixgua larvae inoculated with different pathogens suggested that SeCasp-1 was sensitive to Bacillus thuringiensis infection and that SeCasp-6 was sensitive to baculovirus infection. SeCasp-7 and SeCasp-8 showed slight changes under either in vitro chemical apoptosis induction or in vivo pathogen infection.
© 2019 Institute of Zoology, Chinese Academy of Sciences.

Entities:  

Keywords:  SeCasp; Spodoptera exigua; apoptosis; apoptotic inducing; insect caspase

Mesh:

Substances:

Year:  2020        PMID: 31793737     DOI: 10.1111/1744-7917.12741

Source DB:  PubMed          Journal:  Insect Sci        ISSN: 1672-9609            Impact factor:   3.262


  4 in total

1.  3H-31, A Non-structural Protein of Heliothis virescens ascovirus 3h, Inhibits the Host Larval Cathepsin and Chitinase Activities.

Authors:  Huan Yu; Yi-Yi Ou-Yang; Chang-Jin Yang; Ni Li; Madoka Nakai; Guo-Hua Huang
Journal:  Virol Sin       Date:  2021-04-08       Impact factor: 4.327

2.  Pro-Apoptotic Function Analysis of the Reaper Homologue IBM1 in Spodoptera frugiperda.

Authors:  Benshui Shu; Jingjing Zhang; Sethuraman Veeran; Guohua Zhong
Journal:  Int J Mol Sci       Date:  2020-04-15       Impact factor: 5.923

3.  Regulation of Chitinase in Spodoptera exigua (Hübner) (Lepidoptera: Noctuidae) During Infection by Heliothis virescens ascovirus 3h (HvAV-3h).

Authors:  Lei He; Yi-Yi Ou-Yang; Ni Li; Ying Chen; Shuang-Qing Liu; Guo-Hua Huang
Journal:  Front Physiol       Date:  2020-03-10       Impact factor: 4.566

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

Authors:  Yuanyuan Zhang; Gang Xu; Yu Jiang; Chao Ma; Guoqing Yang
Journal:  Insects       Date:  2021-12-17       Impact factor: 2.769

  4 in total

北京卡尤迪生物科技股份有限公司 © 2022-2023.