XU Jingxiang, RUAN Lingwei, LI Zhen, YU Xiaoman, LI Sedong, SHI Hong, XU Xun. Characterization of four hemocyanin isoforms in Litopenaeus vannamei[J]. Acta Oceanologica Sinica, 2015, 34(2): 36-44. doi: 10.1007/s13131-015-0588-9
Citation: XU Jingxiang, RUAN Lingwei, LI Zhen, YU Xiaoman, LI Sedong, SHI Hong, XU Xun. Characterization of four hemocyanin isoforms in Litopenaeus vannamei[J]. Acta Oceanologica Sinica, 2015, 34(2): 36-44. doi: 10.1007/s13131-015-0588-9

Characterization of four hemocyanin isoforms in Litopenaeus vannamei

doi: 10.1007/s13131-015-0588-9
  • Received Date: 2013-11-04
  • Rev Recd Date: 2014-02-27
  • In this study, the gene encoding hemocyanin subunit L, LvHcL, was cloned from Litopenaeus vannamei and the genomic organization was characterized. This gene was diverse with many SNPs and also had at least four isoforms, while one of them (LvHcL4) only had two exons and the exon2 was missed. Transcription analysis showed that these isoforms of LvHcL were up-regulated after WSSV challenge in WSSV-resistant shrimp, while the transcriptions were decreased constantly in WSSV-susceptible shrimp. It is suggested that the hemocyanin had rich polymorphism and was involved in the antiviral response. These results could extend our previous findings and provide insights into the immune feature of hemocyanin, which would be helpful for further studies aimed at antiviral mechanism in inver-tebrate.
  • loading
  • Adachi K, Endo H, Watanabe T, et al. 2005. Hemocyanin in the exosk-eleton of crustaceans: enzymatic properties and immunolocaliz-ation. Pigment Cell Research, 18(2): 136-143
    Adema C M, Hertel L A, Miller R D, et al. 1997. A family of fibrinogen-related proteins that precipitates parasite-derived molecules is produced by an invertebrate after infection. Proceedings of the National Academy of Sciences of the United States of America,94(16): 8691-8696
    Amparyup P, Kondo H, Hirono I, et al. 2008. Molecular cloning, geno-mic organization and recombinant expression of a crustin-like antimicrobial peptide from black tiger shrimp Penaeus monodon. Molecular Immunology, 45(4): 1085-1093
    Bourchookarn A, Havanapan P-O, Thongboonkerd V, et al. 2008. Proteomic analysis of altered proteins in lymphoid organ of yellow head virus infected Penaeus monodon. Biochimica et Bio-physica Acta (BBA)-Proteins & Proteomics, 1784(3): 504-511
    Chongsatja P O, Bourchookarn A, Lo C F, et al. 2007. Proteomic analysis of differentially expressed proteins in Penaeus vannamei hemocytes upon Taura syndrome virus infection. Proteomics, 7(19): 3592-3601
    Cuthbertson B J, Deterding L J, Williams J G, et al. 2008. Diversity in penaeidin antimicrobial peptide form and function. Develop-mental & Comparative Immunology, 32(3): 167-181
    Cuthbertson B J, Yang Y, Bachère E, et al. 2005. Solution structure of synthetic penaeidin-4 with structural and functional compari-sons with penaeidin-3. Journal of Biological Chemistry, 280(16): 16009-16018
    Decker H, Jaenicke E. 2004. Recent findings on phenoloxidase activity and antimicrobial activity of hemocyanins. Developmental and Comparative Immunology, 28(7-8): 673-687
    Decker H, Rimke T. 1998. Tarantula hemocyanin shows phenoloxi-dase activity. Journal of Biological Chemistry, 273(40): 25889-25892
    Decker H, Ryan M, Jaenicke E, et al. 2001. SDS-induced phenoloxida-e activity of hemocyanins fromLimulus polyphemus, Eurypelma californicum, and Cancer magister. Journal of Biological Chemi-stry, 276(21): 17796-17799
    Destoumieux-Garzón D, Saulnier D, Garnier J, et al. 2001. Crustacean immunity: antifungal peptides are generated from the c terminus of shrimp hemocyanin in response to microbial challenge. Journal of Biological Chemistry, 276(50): 47070-47077
    Duda T F, Vanhoye D, Nicolas P. 2002. Roles of diversifying selection and coordinated evolution in the evolution of amphibian antimi-crobial peptides. Molecular Biology and Evolution, 19(6): 858-864
    Engel D W, Brouwer M, Mercaldo-Allen R. 2001. Effects of molting and environmental factors on trace metal body-burdens and hemocyanin concentrations in the American lobster, Homarus americanus. Marine Environmental Research, 52(3): 257-269
    Ghosh J, Lun C M, Majeske A J, et al. 2011. Invertebrate immune diversity. Developmental & Comparative Immunology, 35(9): 959-974
    Guo Lingling, Zhao Xianliang, Zhang Yueling, et al. 2013. Evidences of SNPs in the variable region of hemocyanin Ig-like domain in shr-imp Litopenaeus vannamei. Fish & Shellfish Immunology, 35(5): 1532-1538
    Hazes B, Kalk K H, Hol W G J, et al. 1993. Crystal structure of deoxy-genated Limulus polyphemus subunit II hemocyanin at 2.18 Å resolution: clues for a mechanism for allosteric regulation. Pro-tein Science, 2(4): 597-619
    Herberts C, De Frescheville J. 1981. Occurrence of haemocyanin in the rhizocephalan crustacea sacculina carcini thompson. Com-parative Biochemistry and Physiology Part B: Comparative Bio-chemistry, 70(3): 657-659
    Jaenicke E, Föll R, Decker H. 1999. Spider hemocyanin binds ec-dysone and 20-OH-ecdysone. Journal of Biological Chemistry, 274(48): 34267-34271
    Jiang Naxin, Tan N S, Ho B, et al. 2007. Respiratory protein-generated reactive oxygen species as an antimicrobial strategy. Nature Immunology, 8(10): 1114-1122
    Léonard P M, Adema C M, Zhang S-M, et al. 2001. Structure of two FREP genes that combine IgSF and fibrinogen domains, with comments on diversity of the FREP gene family in the snail Biomphalaria glabrata. Gene, 269(1-2): 155-165
    Lang W H, van Holde K E. 1991. Cloning and sequencing of Octopus dofleini hemocyanin cDNA: derived sequences of functional units Ode and Odf. Proceedings of the National Academy of Scie-nces of the United States of America, 88(1): 244-248
    Lee S Y, Lee B L, Söderhäll K. 2003. Processing of an antibacterial peptide from hemocyanin of the freshwater crayfish Pacifastacus leniusculus. Journal of Biological Chemistry, 278(10): 7927-7933
    Lee S Y, Lee B L, Söderhäll K. 2004. Processing of crayfish hemocyanin subunits into phenoloxidase. Biochemical and Biophysical Res-earch Communications, 322(2): 490-496
    Lei Kaiyu, Li Fang, Zhang Mingchang, et al. 2008. Difference between hemocyanin subunits from shrimp Penaeus japonicus in anti-WSSV defense. Developmental & Comparative Immunology, 32(7): 808-813
    Magnus K A, Hazes B, Ton-That H, et al. 1994. Crystallographic anal-ysis of oxygenated and deoxygenated states of arthropod hem-ocyanin shows unusual differences. Proteins: Structure, Function, and Bioinformatics, 19(4): 302-309
    Nagai T, Kawabata S-I. 2000. A link between blood coagulation and prophenol oxidase activation in arthropod host defense. Journal of Biological Chemistry, 275(38): 29264-29267
    Nagai T, Osaki T, Kawabata S-I. 2001. Functional conversion of hemocyanin to phenoloxidase by horseshoe crab antimicrobial peptides. Journal of Biological Chemistry, 276(29): 27166-27170
    O'Leary N A, Gross P S. 2006. Genomic structure and transcriptional regulation of the penaeidin gene family from Litopenaeus vann-amei. Gene, 371(1): 75-83
    Pan Deng, He Nanhai, Yang Zhiyuan, et al. 2005. Differential gene expression profile in hepatopancreas of WSSV-resistant shrimp (Penaeus japonicus) by suppression subtractive hybridization. Developmental & Comparative Immunology, 29(2): 103-112
    Paul R, Pirow R. 1998. The physiological significance of respiratory proteins in invertebrates. Zoology, 100(4): 298-306
    Perdomo-Morales R, Montero-Alejo V, Perera E, et al. 2007. Phenol-oxidase activity in the hemolymph of the spiny lobster Panulirus argus. Fish & Shellfish Immunology, 23(6): 1187-1195
    Redmond J R. 1955. The respiratory function of hemocyanin in Crustacea. Journal of Cellular and Comparative Physiology, 46(2): 209-247
    Sambrook J, Russell D W. 2001. Molecular Cloning: A Laboratory Manual. v 1-3. Cold Spring Harbor, New York: Cold Spring Har-bor Laboratory Press
    Sellos D, Lemoine S, van Wormhoudt A. 1997. Molecular cloning of hemocyanin cDNA from Penaeus vannamei (Crustacea, Dec-apoda): structure, evolution and physiological aspects. FEBS Letters, 407(2): 153-158
    Senkbeil E G, Wriston J C. 1981. Hemocyanin synthesis in the American lobster, Homarus americanus. Comparative Bioche-mistry and Physiology Part B: Comparative Biochemistry, 68(1): 163-171
    Somboonwiwat K, Chaikeeratisak V, Wang H-C, et al. 2010. Proteomic analysis of differentially expressed proteins in Penaeus monodon hemocytes after Vibrio harveyi infection. Proteome Science, 8(1): 39-39
    Tassanakajon A, Vatanavicharn T, Supungul P, et al. 2008. Biotechno-logy of marine invertebrates —recent advances in shrimp and shellfish. In: Memorial book of the 5th World Fisheries Congress. Tokyo: TERRAPUB, 221-239
    van Holde K E, Miller K I, Decker H. 2001. Hemocyanins and invertebrate evolution. Journal of Biological Chemistry, 276(19): 15563-15566
    Yang Y, Poncet J, Garnier J, et al. 2003. Solution structure of the recombinant penaeidin-3, a shrimp antimicrobial peptide. Jour-nal of Biological Chemistry, 278(38): 36859-36867
    Zhang Xiaobo, Huang Canhua, Qin Qiwei. 2004. Antiviral properties of hemocyanin isolated from shrimpPenaeus monodon. Antiviral Research, 61(2): 93-99
    Zhao Xianliang, Guo Lingling, Zhang Yueling, et al. 2012. SNPs of hemocyanin C-terminal fragment in shrimp Litopenaeus vann-amei. FEBS Letters, 586(4): 403-410
    Zhao Zhiying, Yin Zhixin, Weng Shaopeng, et al. 2007. Profiling of differentially expressed genes in hepatopancreas of white spot syndrome virus-resistant shrimp (Litopenaeus vannamei) by suppression subtractive hybridisation. Fish & Shellfish Immun-ology, 22(5): 520-534
  • 加载中

Catalog

    通讯作者: 陈斌, bchen63@163.com
    • 1. 

      沈阳化工大学材料科学与工程学院 沈阳 110142

    1. 本站搜索
    2. 百度学术搜索
    3. 万方数据库搜索
    4. CNKI搜索

    Article Metrics

    Article views (1456) PDF downloads(1220) Cited by()
    Proportional views
    Related

    /

    DownLoad:  Full-Size Img  PowerPoint
    Return
    Return