Characterization of four hemocyanin isoforms in Litopenaeus vannamei
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Characterization of four hemocyanin isoforms in Litopenaeus
vannamei XU Jingxiang1, 2, RUAN Lingwei2*, LI Zhen5, YU Xiaoman4, LI Sedong3, 5, SHI Hong2, XU Xun2 1
School of Life Science, Xiamen University, Xiamen 361005, China
2
Key Laboratory of Marine Biogenetic Resources, Third Institute of Oceanography, State Oceanic Administration, Xiamen 361005, China
3
Zhanjiang Ocean and Fishery Development Research Center, Zhanjiang 524000, China
4
School of Life Sciences, Sun Yat-Sen University, Guangzhou 510275, China
5
Zhanjiang Evergreen South Ocean Science & Technology Company Limited, Zhanjiang 524094, China
Received 4 November 2013; accepted 27 February 2014 ©The Chinese Society of Oceanography and Springer-Verlag Berlin Heidelberg 2015 Abstract 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 invertebrate. Key words: hemocyanin, SNPs, isoforms, Litopenaeus vannamei, WSSV Citation: Xu Jingxiang, Ruan Lingwei, Li Zhen, Yu Xiaoman, Li Sedong, Shi Hong, Xu Xun. 2015. Characterization of four hemocyanin isoforms in Litopenaeus vannamei. Acta Oceanologica Sinica, 34(2): 36–44, doi: 10.1007/s13131-015-0588-9
1 Introduction Hemocyanins are copper-containing respiratory proteins in the hemolymph of many arthopods and mollusks. They are colorless when de-oxygenate, but appearing light blue when oxygenated. As the main protein component of hemolymph, it typically represents up to 95% of the total amount protein in penaeid shrimp (Herberts and De Frescheville, 1981; Lang and van Holde, 1991; Sellos et al., 1997). As the respiratory proteins (Redmond, 1955), its well-known role is transport and storage of molecular oxygen. Subsequently, it was demonstrated that hemocyanin is a multifunctional protein involved in several physiological processes, such as protein storage, osmoregulation, molt cycle, exoskeleton formation and so on (Paul and Pirow, 1998; Jaenicke et al., 1999; Engel et al., 2001; Adachi et al., 2005) . And recently more reports revealed that hemocyanin may be an important molecule of non-specific innate immune defense, and possessed some important immunological functions, including phenoloxidase activity, antimicrobial properties and antiviral properties (Decker and Rimke, 1998; Nagai and Kawabata, 2000; Decker et al., 2001; Destoumieux-Garzón et al., 2001; Nagai et al., 2001; Lee et al.
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