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A small heat shock protein 21 (sHSP21) mediates immune responses in Chinese oak silkworm Antheraea pernyi

Author:
Liu, Qiu-Ning, Liu, Yu, Xin, Zhao-Zhe, Zhu, Xiao-Yu, Ge, Bao-Ming, Li, Chao-Feng, Wang, Dong, Bian, Xun-Guang, Yang, Li, Chen, Li, Tian, Ji-Wu, Zhou, Chun-Lin, Tang, Bo-Ping
Source:
International journal of biological macromolecules 2018 v.111 pp. 1027-1031
ISSN:
0141-8130
Subject:
Antheraea pernyi, Baculoviridae, abiotic stress, amino acid sequences, binding sites, embryogenesis, genes, glucans, heat shock proteins, immune response, innate immunity, lipopolysaccharides, metamorphosis, molecular weight, moths, non-specific serine/threonine protein kinase, pathogen-associated molecular patterns, pathogens, peptidoglycans, phosphorylation, phylogeny, polypeptides, protein kinase C, quantitative polymerase chain reaction, reverse transcriptase polymerase chain reaction, silkworms, temperature, tyrosine
Abstract:
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. The deduced ApsHSP21 protein sequence consists of 186 residues with a calculated molecular mass of 21.0 kDa and an isoelectronic point (pI) of 6.63. The protein contains a conserved α-crystallin domain (ACD), and includes two casein kinase II phosphorylation sites, a protein kinase C phosphorylation site, two tyrosine kinase phosphorylation sites, and various polypeptide binding sites. Phylogenetic analysis revealed that ApsHSP21 is closely related to homologs from other insects. Real-time quantitative reverse transcription PCR (qRT-PCR) analysis revealed that expression of ApsHSP21 was significantly up-regulated at different timepoints following simulated pathogen challenge with lipopolysaccharide (LPS), peptidoglycan (PGN), glucan, and NPV. The results suggest sHSP21 is involved in innate immune responses in A. pernyi.
Agid:
5917228