Genome-wide identification of heat shock protein gene family and their responses to pathogen challenge in Trachinotus ovatus
文献类型： 外文期刊
作者： Sun, Yi-Yao 1 ; Guo, Hua-Yang 2 ; Liu, Bao-Suo 2 ; Zhang, Nan 2 ; Zhu, Ke-Cheng 2 ; Xian, Lin 2 ; Zhao, Peng-Hai 2 ; Yang, Hui-Yuan 1 ; Zhang, Dian-Chang 2 ;
作者机构： 1.Hebei Agr Univ, Ocean Coll, Qinhuangdao 066000, Peoples R China
2.Chinese Acad Fishery Sci, South China Sea Fisheries Res Inst, Key Lab South China Sea Fishery Resources Exploita, Minist Agr & Rural Affairs, Guangzhou 510300, Guangdong, Peoples R China
3.Sanya Trop Fisheries Res Inst, Sanya 572018, Peoples R China
4.Marine Biol Seed Ind, Guangdong Prov Engineer Technol Res Ctr, Guangzhou, Guangdong, Peoples R China
5.231 Xingang Rd West, Guangzhou 510300, Peoples R China
关键词： Heat shock proteins; T.ovatus; Phylogenetic analysis; Expression analysis
期刊名称：FISH & SHELLFISH IMMUNOLOGY （ 2022影响因子：4.7； 五年影响因子：4.7 ）
ISSN： 1050-4648
年卷期： 2024 年 145 卷
收录情况： SCI
摘要： Heat Shock Proteins (HSPs) are a widely distributed family of proteins produced in response to heat and other stresses. To develop a deeper understanding of the mechanisms governing expression of HSPs in the bony fish Trachinotus ovatus, we carried out a whole genome analysis and identified 43 HSP genes. Based on their phylogenetic relationships with Danio rerio, Seriola dumerili, and Seriola lalandi, they were divided into four subfamilies: HSP20, HSP60, HSP70, and HSP90. We performed an analysis of the predicted physicochemical properties and subcellular localization of proteins encoded by these genes. The chromosomal localization results showed that the HSP genes are distributed across 20 chromosomes of T. ovatus.These genes were found to be expressed in different tissues, and they showed differential expression in the immune response against Streptococcus agalactiae. However, there was no significant differential expression in the different skin tissue locations of T. ovatus after infection by Cryptocaryon irritans Brown. This study provides basic information for further research on the evolution and structure and function of HSPs in teleosts.
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