Functional identification of C-type lectin in the diamondback moth, Plutella xylostella (L.) innate immunity
| Autor: | Jin-yang Li, Minsheng You, Junhan Lin, Xiao-feng Xia, Jia-yu Zhang, G. Mandela Fernández-Grandon |
|---|---|
| Jazyk: | angličtina |
| Rok vydání: | 2021 |
| Předmět: |
Signal peptide
Cellular immunity S1 Agriculture (General) Plant Science medicine.disease_cause Biochemistry S1-972 Pichia pastoris Microbiology Food Animals C-type lectin medicine diamondback moth Escherichia coli QL Innate immune system Ecology biology pattern recognition receptors Pattern recognition receptor biology.organism_classification carbohydrate-recognition domain humoral and cellular immunity Serratia marcescens Animal Science and Zoology Agronomy and Crop Science Food Science |
| Zdroj: | Journal of Integrative Agriculture, Vol 20, Iss 12, Pp 3240-3255 (2021) |
| ISSN: | 2095-3119 |
| Popis: | C-type lectins (CTLs) are a superfamily of Ca2+-dependent carbohydrate-recognition proteins, and an important pattern recognition receptor (PRR) in insect innate immunity which can mediate humoral and cellular immunity in insects. In this study, we report a novel dual carbohydrate-recognition domain (CRD) CTL from Plutella xylostella which we designate PxIML. PxIML is a protein with a 969 bp open reading frame (ORF) encoding 322 amino acids, containing a signal peptide and a dual-CRD with EPN (Glu124-Pro125-Asn126) and QPD (Gln274-Pro275-Asp276) motifs. The expression of PxIML mRNA in the fat body was significantly higher than in hemocytes and midgut. The relative expression levels of PxIML in the whole insect and the fat body were significantly inhibited after infection with Bacillus thuringiensis 8010 (Bt8010) at 18 h, while they were significantly upregulated after infection with Serratia marcescens IAE6 or Pichia pastoris. The recombinant PxIML (rPxIML) protein could bind to the tested pathogen-associated molecular patterns (PAMPs), and the bacteria of Enterobacter sp. IAE5, S. marcescens IAE6, Staphylococcus aureus, Escherichia coli BL21, and Bt8010 in a Ca2+-dependent manner, however, it showed limited binding to the fungus, P. pastoris. The rPxIML exhibited strong activity in the presence of Ca2+ to agglutinate Bt8010, Enterobacter sp. IAE5 and S. aureus, but it only weakly agglutinated with E. coli BL21, and could not agglutinate with S. marcescens IAE6 or P. pastoris. Furthermore, the rPxIML could bind to hemocytes, promote the adsorption of hemocytes to beads, and enhance the phenoloxidase (PO) activity and melanization of P. xylostella. Our results suggest that PxIML plays an important role in pathogen recognition and in mediating subsequent humoral and cellular immunity of P. xylostella. |
| Databáze: | OpenAIRE |
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