Your browser doesn't support javascript.
loading
Functional analysis of a peptidoglycan recognition protein involved in the immune response in the common cutworm, Spodoptera litura.
Wang, Ying; Zhang, Qin; Yu, Hai-Zhong.
Afiliación
  • Wang Y; College of Life Sciences, Gannan Normal University, Ganzhou, People's Republic of China.
  • Zhang Q; National Navel Orange Engineering Research Center, Ganzhou, People's Republic of China.
  • Yu HZ; College of Life Sciences, Gannan Normal University, Ganzhou, People's Republic of China.
Arch Insect Biochem Physiol ; 109(4): e21858, 2022 Apr.
Article en En | MEDLINE | ID: mdl-35289433
ABSTRACT
Peptidoglycan recognition proteins (GRPs) are family of pattern recognition receptors (PRRs), which can recognize the peptidoglycan and trigger the innate immune system against the microorganisms in insects. In this study, we identified a GRP-LB from Spodoptera litura genome database and named SlGRP-LB, which contained a complete open reading frame (ORF) of 639 bp, encoding a protein of 212 amino acids with a signal peptide and GRP domain. Phylogenetic tree analysis suggested that the SlGRP-LB has a close relationship with Helicoverpa armigera GRP-LB (HaGRP-LB). Tissue expression analysis revealed that SlGRP-LB had a high expression level in the fat body. The expression levels of SlGRP-LB were significantly upregulated in the hemolymph, fat body, and midgut from 3 to 12 h after injection of Escherichia coli and Staphylococcus aureus, while the expression levels were not downregulated at 24 h postinfection. Knockdown of SlGRP-LB expression by RNA interference reduced the expression of antibacterial peptide-related genes in the fat body and midgut, while their expression levels were upregulated in the hemolymph. In addition, the recombinant SlGRP-LB was expressed by using E. coli expression system, and it exhibited binding activity to E. coli. Taken together, the data suggest that S. litura GRP-LB might play a crucial role in regulating immune response in S. litura.
Asunto(s)
Palabras clave

Texto completo: 1 Base de datos: MEDLINE Asunto principal: Proteínas de Insectos / Escherichia coli Límite: Animals Idioma: En Revista: Arch Insect Biochem Physiol Asunto de la revista: BIOLOGIA / BIOQUIMICA Año: 2022 Tipo del documento: Article

Texto completo: 1 Base de datos: MEDLINE Asunto principal: Proteínas de Insectos / Escherichia coli Límite: Animals Idioma: En Revista: Arch Insect Biochem Physiol Asunto de la revista: BIOLOGIA / BIOQUIMICA Año: 2022 Tipo del documento: Article