Cloning and functional analysis of the calreticulin gene from the scleractinian coral <i>Galaxea astreata</i>

Yuanjia Huang; Yanping Zhang; Huipai Peng; Jigui Yuan; Li Liu

doi:10.1007/s13131-020-1590-4

Volume 39 Issue 6

Jun. 2020

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Yuanjia Huang, Yanping Zhang, Huipai Peng, Jigui Yuan, Li Liu. Cloning and functional analysis of the calreticulin gene from the scleractinian coral Galaxea astreata[J]. Acta Oceanologica Sinica, 2020, 39(6): 58-64. doi: 10.1007/s13131-020-1590-4

Citation:

Yuanjia Huang, Yanping Zhang, Huipai Peng, Jigui Yuan, Li Liu. Cloning and functional analysis of the calreticulin gene from the scleractinian coral Galaxea astreata[J]. Acta Oceanologica Sinica, 2020, 39(6): 58-64. doi: 10.1007/s13131-020-1590-4

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Cloning and functional analysis of the calreticulin gene from the scleractinian coral Galaxea astreata

doi: 10.1007/s13131-020-1590-4

Key Laboratory of Aquaculture in South China Sea for Aquatic Economic Animal of Guangdong Higher Education Institutes, Fisheries College, Guangdong Ocean University, Zhanjiang 524025, China

Funds: The National Marine Welfare Industry Research Project under contract No. 201105012; the Guangdong Provincial Natural Science Foundation under contract No. S2011010000269; the Guangdong Marine Fishery Science and Technology Extension Project under contract No. A201308E02; the Guangdong Ocean University Scientific Research Start-up Fund for the Doctoral Program under contract No. R17066.

More Information

Corresponding author: E-mail: zjouliuli@163.com
Received Date: 2019-05-09
Accepted Date: 2019-06-17

Available Online: 2020-12-28

Publish Date: 2020-06-25

Abstract

Abstract

Calreticulin (CRT) is a highly conserved Ca²⁺-binding protein and chaperone in the endoplasmic reticulum, which mainly participates in adjusting calcium level and directing proper conformation of proteins. Here, we cloned the crt gene of the scleractinian coral Galaxea astreata, named Gacrt, and analysed its ability to drive bacterial agglutination. The full-length Gacrt cDNA consisted of 1 792 nucleotides and contained a 77 bp 5’ untranslated region (UTR), a 380 bp 3’ UTR and a 1 335 bp open reading frame (ORF) that encoded a 444 amino acid protein. The deduced peptide possessed a signal peptide domain, an endoplasmic reticulum retrieval signal sequence (KDEL), two potential calreticulin family signature motifs and a set of triplicate repeats. We also found that the recombinant GaCRT protein could promote agglutination of both the Gram-positive bacterium Micrococcus luteus and the Gram-negative bacterium Escherichia coli. These results show that the GaCRT protein can enhance bacterial agglutination, hinting that GaCRT is an immune-relevant molecule involved in host defense against bacterium.
- Galaxea astreata,
- calreticulin,
- bacterial agglutination

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References(24)

References

[1]	Baksh S, Michalak M. 1991. Expression of calreticulin in Escherichia coli and identification of its Ca²⁺ binding domains. The Journal of Biological Chemistry, 266(32): 21458–21465. doi: 10.1007/BF00006813
[2]	Corbett E F, Oikawa K, Francois P, et al. 1999. Ca²⁺ regulation of interactions between endoplasmic reticulum chaperones. The Journal of Biological Chemistry, 274(10): 6203–6211. doi: 10.1074/jbc.274.10.6203
[3]	Duan Yafei, Liu Ping, Li Jitao, et al. 2014. Molecular responses of calreticulin gene to Vibrio anguillarum and WSSV challenge in the ridgetail white prawn Exopalaemon carinicauda. Fish & Shellfish Immunology, 36(1): 164–171. doi: 10.1016/j.fsi.2013.10.024
[4]	Dunlap W C, Starcevic A, Baranasic D, et al. 2013. KEGG orthology-based annotation of the predicted proteome of Acropora digitifera: zoophyteBase-an open access and searchable database of a coral genome. BMC Genomics, 14: 509. doi: 10.1186/1471-2164-14-509
[5]	Fischer C R, Mikami M, Minematsu H, et al. 2017. Calreticulin inhibits inflammation-induced osteoclastogenesis and bone resorption. Journal of Orthopaedic Research, 35(12): 2658–2666. doi: 10.1002/jor.23587
[6]	Gold L I, Eggleton P, Sweetwyne M T, et al. 2010. Calreticulin: non-endoplasmic reticulum functions in physiology and disease. The FASEB Journal, 24(3): 665–683. doi: 10.1096/fj.09-145482
[7]	Gu V Y, Wong M H, Stevenson J L, et al. 2008. Calreticulin in human pregnancy and pre-eclampsia. Molecular Human Reproduction, 14(5): 309–315. doi: 10.1093/molehr/gan017
[8]	Hayward D C, Hetherington S, Behm C A, et al. 2011. Differential gene expression at coral settlement and metamorphosis—a subtractive hybridization study. PLoS One, 6(10): e26411. doi: 10.1371/journal.pone.0026411
[9]	Jia Xiaoyun, Xu Chongyi, Jing Ruilian, et al. 2008. Molecular cloning and characterization of wheat calreticulin (CRT) gene involved in drought-stressed responses. Journal of Experimental Botany, 59(4): 739–751. doi: 10.1093/jxb/erm369
[10]	Kenkel C D, Bay L K. 2017. Novel transcriptome resources for three scleractinian coral species from the Indo-Pacific. Gigascience, 6(9): 1–4. doi: 10.1093/gigascience/gix074
[11]	Kobylewski S E, Henderson K A, Yamada K E, et al. 2017. Activation of the EIF2α/ATF4 and ATF6 pathways in du-145 cells by boric acid at the concentration reported in men at the US mean boron intake. Biological Trace Element Research, 176(2): 278–293. doi: 10.1007/s12011-016-0824-y
[12]	Li Shuo, Xie Liping, Meng Qingxiong, et al. 2006. Significance of the extra C-terminal tail of CaLP, a novel calmodulin-like protein involved in oyster calcium metabolism. Comparative Biochemistry and Physiology Part B: Biochemistry and Molecular Biology, 144(4): 463–471. doi: 10.1016/j.cbpb.2006.04.010
[13]	Liu Xuemei, Xu Na, Zhang Shicui. 2013. Calreticulin is a microbial-binding molecule with phagocytosis-enhancing capacity. Fish & Shellfish Immunology, 35(3): 776–784. doi: 10.1016/j.fsi.2013.06.013
[14]	Michalak M, Corbett E F, Mesaeli N, et al. 1999. Calreticulin: one protein, one gene, many functions. Biochemical Journal, 344(2): 281–292. doi: 10.1042/bj3440281
[15]	Ostwald T J, MacLennan D H. 1974. Isolation of a high affinity calcium-binding protein from sarcoplasmic reticulum. The Journal of Biological Chemistry, 249(3): 974–979. doi: 10.1007/BF01520862
[16]	Peatman E, Baoprasertkul P, Terhune J, et al. 2007. Expression analysis of the acute phase response in channel catfish (Ictalurus punctatus) after infection with a Gram-negative bacterium. Developmental & Comparative Immunology, 31(11): 1183–1196. doi: 10.1016/j.dci.2007.03.003
[17]	Qiu Yuanyuan, Michalak M. 2009. Transcriptional control of the calreticulin gene in health and disease. The International Journal of Biochemistry & Cell Biology, 41(3): 531–538. doi: 10.1016/j.biocel.2008.06.020
[18]	Smith M J, Koch G L. 1989. Multiple zones in the sequence of calreticulin (CRP55, calregulin, HACBP): a major calcium binding ER/SR protein. The EMBO Journal, 8(12): 3581–3586. doi: 10.1002/j.1460-2075.1989.tb08530.x
[19]	Wang F I, Chen J C. 2006. Effect of salinity on the immune response of tiger shrimp Penaeus monodon and its susceptibility to Photobacterium damselae subsp. damselae. Fish & Shellfish Immunology, 20(5): 671–681. doi: 10.1016/j.fsi.2005.08.003
[20]	Wang Yan, Zhou Jianjiang, Xie Yuan, et al. 2013. Expressions of calmodulin, calreticulin and cyclin-dependent kinase 1 genes in gastric cancer tissues. Cancer Research on Prevention and Treatment (in Chinese), 40(2): 151–154
[21]	Xia Xiulin, Wang Guiling, Bai Zhiyi, et al. 2013. Molecular characterization and expression analysis of calreticulin cDNA from Hyriopsis cumingii. Journal of Fisheries of China (in Chinese), 37(5): 679–687. doi: 10.3724/SP.J.1231.2013.38454
[22]	Yuyama I, Ito Y, Watanabe T, et al. 2012. Differential gene expression in juvenile polyps of the coral Acropora tenuis exposed to thermal and chemical stresses. Journal of Experimental Marine Biology and Ecology, 430–431: 17–24. doi: 10.1016/j.jembe.2012.06.020
[23]	Zhang Guangming, Schmidt O, Asgari S. 2006. A calreticulin-like protein from endoparasitoid venom fluid is involved in host hemocyte inactivation. Developmental & Comparative Immunology, 30(9): 756–764. doi: 10.1016/j.dci.2005.11.001
[24]	Zhuo Ruiqun, Zhou Tingting, Yang Shiping, et al. 2017. Characterization of a molt-related myostatin gene (FmMstn) from the banana shrimp Fenneropenaeus merguiensis. General and Comparative Endocrinology, 248: 55–68. doi: 10.1016/j.ygcen.2017.03.010