Molecular cloning and expression analysis of Crustin-like gene from Chinese shrimp Fenneropenaeus chinensis

Acta Oceanologica Sinica

Volumn 27, Issue 2, 2008, Pages 81-92

  Liu, Fengsong ^a,b   Li, Fuhua ^b   Xiang, Jianhai ^b   Dong, Bo ^b   Liu, Yichen ^b   Zhang, Xiaojun ^b   Zhang, Liusuo ^b  

^a HEBEI UNIVERSITY   (China)

^b INSTITUTE OF OCEANOLOGY   (China)

Author keywords

Crustin like gene; Expression analysis; Fenneropenaeius chinensis; Microbe challenge; Molecular cloning

Indexed keywords

AMINO ACID; CLONE; GENE EXPRESSION; HOMOLOGY; PROTEIN;

BACTERIA (MICROORGANISMS); DECAPODA (CRUSTACEA); FENNEROPENAEUS CHINENSIS; LITOPENAEUS;

EID: 46649089130     PISSN: 0253505X     EISSN: None     Source Type: Journal    
DOI: None     Document Type: Article

References (28)

1. Andrä J, Lamata M, Tejada G M, et al. 2004. Cyclic antimicrobial peptides based on Limulus anti-lipopolysaccharide factor for neutralization of lipopolysaccharide. Biochemical Pharmacology, 68: 1297-1307
2. Bartlett T C, Cuthbertson B J, Shepard E F, et al. 2002. Crustins, homologues of an 11. 5-kDa antibacterial peptide, from two species of penaeid shrimp, Litopenaeus vannamei and Litopenaeus setiferus. Marine Biotechnology, 4: 278-293
3. Bulet P, Urge L, Ohresser S, et al. 1999. Enlarged scale chemical synthesis and range of activity of drosocin, an Oglycosylated antibacterial peptide of Drosophila. European Journal of Biochemistry, 23: 329-344
4. Chen J Y, Pan C Y, Kuo C M. 2004. cDNA sequence encoding an 11. 5-kDa antibacterial peptide of the shrimp Penaeus monodon. Fish Shellfish Immunology, 16: 659-664
5. Destoumieux D, Bulet P, Loew D, et al. 1997. Penaeidins, a new family of antimicrobial peptides isolated from the shrimp Penaeus vannamei (Decapoda). Journal of Biology & Chemistry, 272: 28398-28406
6. Destoumieux D, Muňoz M, Cosseau C, et al. 2000. Penaeidins, antimicrobial peptides with chitin-binding activity, are produced and stored in shrimp granulocytes and released after microbial challenge. Journal of Cell Science, 113: 461-469
7. Dong Bo, Liu Fengsong, Xiang Jianhai, et al. 2005. Expression profiles of penaeidin from Fenneropenaeus chinensis in response to WSSV and vibrio infection by real time PCR. Acta Oceanologica Sinica, 24(2): 131-140
8. Engström Y. 1998. Insect immune gene regulation. In: Brey P T, Hultmark D, eds. Molecular Mechanisms of Immune Responses in Insects. London: Chapman and Hall, 211-244
9. Epand R M, Vogel H J. 1999. Diversity of antimicrobial peptides and their mechanisms of action. Biochemistry Biophysics Acta, 1463: 11-28
10. Ganz T, Lehrer R I. 1997. Antimicrobial peptides of leukocytes. Current Opinion in Hematology, 4: 53-58
11. Gross P S, Bartlett T C, Browdy C L, et al. 2001. Immune gene discovery by expressed sequence tag analysis of hemocytes and hepatopancreas in the Pacific white shrimp, Litopenaeus vannamei, and the Atlantic white shrimp, L. setiferus. Developmental & Comparative Immunology, 25: 565-577
12. Hiemstra P S, Fernie-King B A, McMichael J, et al. 2004. Antimicrobial peptides: mediators of innate immunity as templates for the development of novel anti-infective and immune therapeutics. Current Pharmaceutical Design, 10: 2891-2905
13. Kang Cuijie, Wang Jinxing, Zhao Xiaofan, et al. 2004. Molecular cloning and expression analysis of the Ch-penaeidin, an antimicrobial peptide from Chinese shrimp, Fenneropenaeus chinensis. Fish Shellfish Immunology, 16: 513-525
14. Kanost M R. 1999. Serine proteinase inhibitors in arthropod immunity. Developmental & Comparative Immunology, 23: 291-301
15. Lee I H, Zhao C, Cho Y, et al. 1997. Clavanins, alpha-helical antimicrobial peptides from tunicate hemocytes. FEBS Letters, 400: 158-162
16. Liu Fengsong, Liu Yichen, Li Fuhua, et al. 2005. Molecular cloning and expression profile of putative anti-lipopolysaccharide factor (ALF) in Chinese shrimp Fenneropenaeus chinensis. Marine Biotechnology, 7: 600-608
17. Mitta G, Hubert F, Noël T, et al. 1999. Myticin, a novel cysteine-richantimicrobial peptide isolated from haemocytes and plasma of the mussel Mytilus gallopro incialis. European Journal of Biochemistry, 264: 1-9
18. Muñoz M, Vandenbulcke F, Garnier J, et al. 2004. Involvement of penaeidins in defense reactions of the shrimp Litopenaeus stylirostris to a pathogenic vibrio. Cellular & Molecular Life Sciences, 61: 961-972
19. Muñoz M, Vandenbulcke F, Saulnier D, et al. 2002. Expression and distribution of penaeidin antimicrobial peptides are regulated by haemocyte reactions in microbial challenged shrimp. European Journal of Biochemistry, 269: 2678-2689
20. Ouellette A J, Selsted M E. 1996. Panethcell defensins: endogeneous peptide components of intestinal host defense. FASEB Journal, 10: 1280-1289
21. Rattanachai A, Hirono I, Ohira T, et al. 2004. Cloning of kuruma prawn Marsupenaeus japonicus Crustin-like peptide cDNA and analysis of its expression. Fish Science, 70: 765-771
22. Rodriguez J, Boulo V, Mialhe E, et al. 1995. Characterization of shrimp haemocytes and plasma components by monoclonal antibodies. Journal of Cell Science, 108: 1043-1050
23. Supungul P, Klinbunga S, Pichyangkura R, et al. 2002. Identification of immune-related genes in hemocytes of black tiger shrimp (Penaeus monodon). Marine Biotechnology, 4: 487-494
24. Valerie J S, Janet H B, Chris H. 2003. Immunostimulation in crustaceans: does it really protect against infection? Fish Shellfish Immunology, 15: 71-90
25. Vargas - Albores F, Yepiz - Plascencia G, Jiménez - Vega F, et al. 2004. Structural and functional differences of Litopenaeus vannamei Crustins. Comparative Biochemistry and Physiology, 138B: 415-422
26. Wang Dongning, Liu Jiewu, Yang Guanzhen, et al. 2002. Cloning of anti-LPS factor cDNA from Tachypleus tridentatus, expression in Bombyx mori larvae and its biological activity in vitro. Molecular Biotechnology, 21: 1-7
27. Zhang Jiquan, Li Fuhua, Wang Zaizhao, et al. 2007. Expression, purification, and characterization of recombinant Chinese shrimp Crustin-like protein(CruFc) in Pichia pastoris. Biotechnol Lett, 29: 813-817
28. Zhao C, Liaw L, Lee I H, et al. 1997. cDNA cloning of three cecropin-like antimicrobial peptides (styelins) from the tunicate, Styela clava. FEBS Letters, 412: 144-148