Molecular Biology Reports

, Volume 38, Issue 6, pp 3751–3756

Molecular cloning and expression analysis of a F-type lectin gene from Japanese sea perch (Lateolabrax japonicus)

  • Lihua Qiu
  • Liansheng Lin
  • Keng Yang
  • Hanhua Zhang
  • Jianzhu Li
  • Falin Zou
  • Shigui Jiang
Article

Abstract

The techniques of homology cloning and anchored PCR were used to clone the fucose-binding lectin (F-type lectin) gene from Japanese sea perch (Lateolabrax Japonicus). The full-length cDNA of sea perch F-lectin (JspFL) contained a 5′ untranslated region (UTR) of 39 bp, an ORF of 933 bp encoding a polypeptide of 310 amino acids with an estimated molecular mass of 10.82 kDa and a 3′ UTR of 332 bp. The searches for nucleotides and protein sequence similarities with BLAST analysis indicated that the deduced amino acid sequence of JspFL was homological to the Fucose-binding lectin in other fish species. In the JspFL deduced amino acid sequence, two tandem domains that exhibit the eel carbohydrate-recognition sequence motif were found. The temporal expressions of gene in the different tissues were measured by real-time PCR. And the mRNA expressions of the gene were constitutively expressed in tissues including spleen, head-kidney, liver, gill, and heart. The JspFL expression in spleen was different during the stimulated time point, 2 h later the expression level became up-regulated, and 6 h later the expression level became down-regulated. The result indicated that JspFL was constitutive and inducible expressed and could play a critical role in the host-pathogen interaction.

Keywords

F-type lectin Cloning Expression Japanese sea perch 

References

  1. 1.
    Ewart KV, Johnson SC, Ross NW (2001) Lectins of the innate immune system and their relevance to fish health. J Mar Sci 58:380–385Google Scholar
  2. 2.
    Barondes SH (1988) Bifunctional properties of lectins: lectins redefined. Trends Biochem Sci 13:480–482PubMedCrossRefGoogle Scholar
  3. 3.
    Andersen O, Laursen SB, Svehag SE, Holmoskow U, Thiel S (1991) Mammalian lectins in defence mechanism against microorganism. Lectins Rev. 1:41–51Google Scholar
  4. 4.
    Arason GJ (1996) Lectins as defence molecules in vertebrates and invertebrates. Fish Shellfish Immunol 6:277–289CrossRefGoogle Scholar
  5. 5.
    Josh SS, Gabius HJ (1993) Measurement of intracellular calcium levels by flow cytometry following treatment of murine macrophage/mono-cytes with mistletoe lectin. In: Gabius HJ, Gabius S (eds) Lectins and glycobiology. Springer, BerlinGoogle Scholar
  6. 6.
    Sharon N, Lis H (1989) Lectins as cell recognition molecules. Science 246:227–233PubMedCrossRefGoogle Scholar
  7. 7.
    Sharon N (1993) Lectin-carbohydrate complexes of plants and animals: an atomic view. Trends Biochem Sci 18:221–226PubMedCrossRefGoogle Scholar
  8. 8.
    Drickamer K, Taylor ME (1993) Biology of animal lectins. Annu Rev Cell Biol 9:237–264PubMedCrossRefGoogle Scholar
  9. 9.
    Honda S, Kashiwagi M, Miyamoto K, Takei Y, Hirose S (2000) Multiplicity, structure and endocrine and exocrine natures of eel fucose-binding lectins. J Biol Chem 275:33151–33157PubMedCrossRefGoogle Scholar
  10. 10.
    Bianchet MA, Odom EW, Vasta GR, Amzel LM (2002) A novel fucose recognition fold involved in innate immunity. Nat Struct Biol 9:628–634PubMedGoogle Scholar
  11. 11.
    Saito T, Hatada M, Iwanaga S, Kawabata S (1997) A newly identified horseshoe crab lectin with binding specificity to O-antigen of bacterial lipopolysaccharides. J Biol Chem 272:30703–30708PubMedCrossRefGoogle Scholar
  12. 12.
    Macedo-Ribeiro S, Bode W, Huber R, Quinn-Allen MA, Kim SW, Ortel TL, Bourenkov GP, Bartunik HD, Stubbs MT, Kane WH, Fuentes-Prior P (1999) Crystal structures of the membrane-binding C2 domain of human coagulation factor V. Nature 402:434–439PubMedCrossRefGoogle Scholar
  13. 13.
    Pratt KP, Shen BW, Takeshima K, Davie EW, Fujikawa K, Stoddard BL (1999) Structure of the C2 domain of human factor VIII at 1.5 A resolution. Nature 402:439–442PubMedCrossRefGoogle Scholar
  14. 14.
    Gaskell A, Crennell S, Taylor G (1995) The three domains of a bacterial sialidase: a beta-propeller, an immunoglobulin module and a galactose-binding jelly-roll. Structure (Camb.) 3:1197–1205CrossRefGoogle Scholar
  15. 15.
    Ito N, Phillips SE, Stevens C, Ogel ZB, McPherson MJ, Keen JN, Yadav KD, Knowles PF (1991) Novel thioether bond revealed by a 1.7 A crystal structure of galactose oxidase. Nature 350:87–90PubMedCrossRefGoogle Scholar
  16. 16.
    Lee CC, Kreusch A, McMullan D, Ng K, Spraggon G (2003) Crystal structure of the human neuropilin-1 b1 domain. Structure (Camb.) 11:99–108CrossRefGoogle Scholar
  17. 17.
    Leulliot N, Quevillon-Cheruel S, Sorrel I, Graille M, Meyer P, Liger D, Blondeau K, Janin J, Tilbeurgh H (2004) Crystal structure of yeast allantoicase reveals a repeated jelly roll motif. J Biol Chem 279:23447–23452PubMedCrossRefGoogle Scholar
  18. 18.
    Shao ZT, Cong X, Yuan JD, Yang GW, Chen Y, Pan J, An LG (2009) Construction and characterization of a cDNA library from head kidney of Japanese sea bass (Lateolabrax japonicus). Mol Biol Rep 36(7):2031–2037PubMedCrossRefGoogle Scholar
  19. 19.
    Qiu L, Zhang H, Yang K, Jiang S (2009) Molecular cloning and mRNA expression analysis of interleukin-8 gene in Japanese sea perch (Lateolabrax japonicus). Mol Biol Rep 36(5):1099–1105PubMedCrossRefGoogle Scholar
  20. 20.
    Cheng HL, Sun SP, Peng YX, Shi XY, Shen X, Meng XP, Dong ZG (2009) cDNA sequence and tissues expression analysis of lipoprotein lipase from common carp (Cyprinus carpio Var. Jian). Mol Biol Rep 37(6):2665–2673PubMedCrossRefGoogle Scholar
  21. 21.
    Inagawa H, Kuroda A, Nishizawa T et al (2001) Cloning and characterization of tandem-repeat type galectin in rainbow trout (Oncorhynchus mykiss). Fish Shellfish Immunol 11:217–231PubMedCrossRefGoogle Scholar
  22. 22.
    Cammareta M, Vazzana M, Chinnici C et al (2001) A serum fucolectin isolated and characterized from sea bass Dicentrarchus labrax. Biochim Biophys Acta 1528:196–202Google Scholar
  23. 23.
    Odom EW, Vasta GR (2006) Characterization of a binary tandem domain f-type lectin from striped bass (Morone saxatilis). J Biol Chem 281(3):1698–1713PubMedCrossRefGoogle Scholar
  24. 24.
    Thiel S, Vourp Jensen T, Stover CM, Schwable W, Eggleton P, Hansen S, Holmoskov U, Reid KB, Jensunius JC (1997) A second serine protease associated with mannose-binding lectin that activates complement. Nature 386:506–510PubMedCrossRefGoogle Scholar
  25. 25.
    Ikeda K, Sannoh T, Kawasaki T, Kawasaki N, Yamashina I (1987) Serum lectin with known structure activates complement through the classical pathway. J Biol Chem 262:7451–7454PubMedGoogle Scholar
  26. 26.
    Faisal M, Chiappelli F, Ahmed II, Cooper EL, Weiner H (1989) Social confrontation ‘stress’ in aggressive fish is associated with an endogenous opioid-mediated suppression of proliferative response to mitogens and non-specific cytotoxicity. Brain Behav Immun 3:223–233PubMedCrossRefGoogle Scholar
  27. 27.
    Odom E, Vasta GR (2006) Characterization of a binary tandem domain F-type lectin from striped bass (Morone saxatilis). J Biol Chem 281:1698–1713PubMedCrossRefGoogle Scholar
  28. 28.
    Chothia C, Lesk AM (1986) The relation between the divergence of sequence and structure in proteins. EMBO J 5:823–826PubMedGoogle Scholar
  29. 29.
    Voss EW Jr, Fryer JL, Banowetz GM (1978) Isolation, purification, and partial characterization of a lectin of a Chinook salmon ova. Arch Biochem Biophys 186:25–34PubMedCrossRefGoogle Scholar
  30. 30.
    Krajhanzl A (1990) Egg lectin of invertebrates and lower vertebrates: properties and biological function. Adv Lectin Res 3:83–131Google Scholar
  31. 31.
    Salerno G, Parisi MG, Parrinello D, Benenati G, Vizzini A, Vazzana M, Vasta GR, Cammarata M (2009) F-type lectin from the sea bass (Dicentrarchus labrax): purification, cDNA cloning, tissue expression and localization, and opsonic activity. Fish Shellfish Immunol 27:143–153PubMedCrossRefGoogle Scholar
  32. 32.
    Iwama G, Nakanishi T (1996) The fish immune system—organism, pathogen, environment. Academic Press, New YorkGoogle Scholar
  33. 33.
    Ulevitch RJ, Tobias PS (1995) Receptor-dependent mechanisms of cell stimulation by bacterial endotoxin. Annu Rev Immunol 13:437–457PubMedCrossRefGoogle Scholar
  34. 34.
    Lemaitre B, Nicolas E, Michaut L, Reichhart JM, Hoffmann JA (1996) The dorsoventral regulatory gene cassette spatzle/Toll/cactus controls the potent antifungal response in Drosophila adults. Cell 86:973–983PubMedCrossRefGoogle Scholar
  35. 35.
    Ostos MA, Recalde D, Zakin MM, Scott-Algara D (2002) Implication of natural killer T cells in atherosclerosis development during a LPS induced chronic inflammation. FEBS Lett 519:23–29PubMedCrossRefGoogle Scholar
  36. 36.
    Kuhlman M, Joiner K, Ezekowitz AB (1989) The human mannose-binding protein functions as an opsonin. J Exp Med 169:1733–1745PubMedCrossRefGoogle Scholar
  37. 37.
    Cooper D, Butcher CM, Berndt MC, Vadas MA (1994) P-selectin interacts with a beta 2-integrin to enhance phagocytosis. J Immunol 153:3199–3209PubMedGoogle Scholar
  38. 38.
    Tino MJ, Wright JR (1996) Surfactant protein A stimulates phagocytosis of specific pulmonary pathogens by alveolar macrophages. Am J Physiol 270:677Google Scholar
  39. 39.
    Goldstein IJ, Huges RC, Monsigny M, Osawa T, Sharon N (1980) What should be called a lectin? Nature 285:66CrossRefGoogle Scholar
  40. 40.
    Rabinovich GA, Toscano MA, Jackson SS, Vasta GR (2007) Functions of cell surface galectin–glycoprotein lattices. Curr Opin Struct Biol 17:513–520PubMedCrossRefGoogle Scholar

Copyright information

© Springer Science+Business Media B.V. 2010

Authors and Affiliations

  • Lihua Qiu
    • 1
  • Liansheng Lin
    • 2
  • Keng Yang
    • 1
  • Hanhua Zhang
    • 1
  • Jianzhu Li
    • 1
  • Falin Zou
    • 1
  • Shigui Jiang
    • 1
  1. 1.Biotechnology and Aquiculture LaboratoryThe South China Sea Fisheries Research Institute, Chinese Academy of Fishery SciencesGuangzhouPeople’s Republic of China
  2. 2.Chinese Academy of Fishery SciencesBeijingPeople’s Republic of China

Personalised recommendations