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Int J Parasitol

Title:		"Functional characterization of a novel gene, Hc-dhs-28 and its role in protecting the host after Haemonchus contortus infection through regulation of diapause formation"
Author(s):		Yang Y; Guo X; Chen X; Zhou J; Wu F; Huang Y; Shi H; Du A;
Address:		"College of Animal Sciences, Zhejiang Provincial Key Laboratory of Preventive Veterinary Medicine, Institute of Preventive Veterinary Medicine, Zhejiang University, Hangzhou 310058, China. Kangmeihuada Gene Technology Co., Ltd, Hangcheng Industrial Zone, Baoan District, Shenzhen 518126, China. College of Animal Sciences, Zhejiang Provincial Key Laboratory of Preventive Veterinary Medicine, Institute of Preventive Veterinary Medicine, Zhejiang University, Hangzhou 310058, China. Electronic address: afdu@zju.edu.cn"
Journal Title:		Int J Parasitol
Year:		2020
Volume:		20200825
Issue:		12
Page Number:		945 - 957
DOI:		10.1016/j.ijpara.2020.04.013
ISSN/ISBN:		1879-0135 (Electronic) 0020-7519 (Linking)
Abstract:		"Haemonchus contortus could enter the diapause stage to avoid hostile conditions, however the inducing mechanism still remains poorly understood. A similar dauer strategy exists in Caenorhabditis elegans, and dauer phenomones, which are produced through a four step cycle of peroxisomal fatty acid beta-oxidation, are essential in this stage. In this study, a novel gene, Hc-dhs-28, was identified and characterised. Hc-DHS-28 was the homologue of Ce-DHS-28, a key enzyme in the oxidation cycle, and the protein contained a short chain dehydrogenase domain and a peroxisomal targeting signal 1. The expression pattern of Hc-DHS-28 detected by quantitative real-time PCR and indirect immunofluorescence assay revealed that this protein was mainly expressed in the intestine and subdermal regions of larvae at diapause and in free-living stages. Enzyme activity analysis confirmed its 3-hydroxyacyl CoA dehydrogenase activity with 121, 149, 162 and 166 as key functional sites; meanwhile co-localization in human embryonic kidney 293 cells indicated that Hc-DHS-28 was targeted to the peroxisome of cytoplasm under the guide of peroxisomal targeting signal 1, which was consistent with the functional domain prediction of Hc-dhs-28. Overexpression, rescue and RNA interference experiments were carried out to explore the function of Hc-dhs-28. Our results showed that Hc-dhs-28 was very similar to Ce-dhs-28 and partially rescued its function in C. elegans. RNAi with Hc-dhs-28 in C. elegans led to decreased transcription of genes in the peroxisomal fatty acid beta-oxidation cycle, considerable fat accumulation and dauer formation defects. Furthermore, immunisation with recombinant Hc-DHS-28 protein in sheep was able to maintain the body weight of the host after infection and reduce the worm burden. In conclusion, Hc-DHS-28 is most likely involved in the peroxisome fatty acid beta-oxidation as the third 3-hydroxyacyl CoA dehydrogenase to regulate the production of diapause-related pheromones, and then influence the formation of diapause in H. contortus"
Keywords:		3-Hydroxyacyl CoA Dehydrogenases/*genetics Amino Acid Sequence Animals *Diapause HEK293 Cells *Haemonchus/genetics Helminth Proteins/*genetics Host-Parasite Interactions/*genetics Humans Sheep Caenorhabditis elegans Diapause Haemonchus contortus Peroxisom;
Notes:		"MedlineYang, Yi Guo, Xiaolu Chen, Xueqiu Zhou, Jingru Wu, Fei Huang, Yan Shi, Hengzhi Du, Aifang eng Research Support, Non-U.S. Gov't England 2020/08/29 Int J Parasitol. 2020 Oct; 50(12):945-957. doi: 10.1016/j.ijpara.2020.04.013. Epub 2020 Aug 25"