Publications by authors named "Jiwu Tian"

Antimicrobial peptides (AMPs) play important roles in the insect innate immune response. To investigate the role of a lebocin-like protein in the oak silkworm, Antheraea pernyi, in response to immune challenge, an Ap-lebocin-like gene with an open reading frame of 489 bp was identified. This gene encodes a protein of 162 amino acid residues and belongs to a family of proline-rich antimicrobial peptides.

View Article and Find Full Text PDF

Small heat shock proteins (sHSPs) are a class of highly conserved proteins that are ubiquitously found in all types of organisms, from prokaryotes to eukaryotes. In the current study, we identified and characterized the full-length cDNA encoding sHSP 19.1 from the oak silkworm, Antheraea pernyi.

View Article and Find Full Text PDF

Antheraea pernyi is not only an important economic insect, it is increasingly employed as a model organism due to a variety of advantages, including ease of rearing and experimental manipulation compared with other Lepidoptera. Peptidoglycan (PGN) is a major component of the bacterial cell wall, and interactions between PGN and A. pernyi cause a series of physiological changes in the insect.

View Article and Find Full Text PDF

Small heat shock proteins (sHSPs) are conserved among insects and play an important role in the regulation of many biological processes, including temperature stress, abiotic stress, immune responses, metamorphosis, and embryo development. Antheraea pernyi is an economically valuable silk-producing moth and source of insect food containing high-quality protein. The aim of this study was to quantify expression of the ApsHSP21 gene in response to pathogen-associated molecular patterns (PAMPs) and nucleopolyhedrovirus (NPV) challenge.

View Article and Find Full Text PDF

Cyclic AMP response element binding (CREB) proteins participate in the regulation of many biological processes. However, little is known about their role in immune regulation in the Oak silkworm (Antheraea pernyi). In this study, a CREB gene was identified in A.

View Article and Find Full Text PDF

Cathepsins are a group of protease, located in lysosome and play a vital role in physiological process. Here, we reported cathepsin L-like protease (Ap-cathL), which contained an open reading frame of 1155 bp and encoding 385 amino acid residues protein. The I29 inhibitor domain and peptidase C1A (clan CA of cysteine proteases, papain family C1 subfamily) putative conserved domains were detected in Ap-cathL.

View Article and Find Full Text PDF