Molecular identification and expression analysis of bactericidal permeability-increasing protein/ LPS-binding protein (BPI/LBP) from Black rockfish Sebastes schlegeli

  • Kwon, Mun-Gyeong (Pathology Division, National Fisheries Research and Development Institute) ;
  • Kim, Ju-Won (Department of Marine Biology & Aquaculture, Institute of Marine Industry, College of Marine Science, Gyeongsang National University) ;
  • Park, Myoung-Ae (Pathology Division, National Fisheries Research and Development Institute) ;
  • Hwang, Jee-Youn (Pathology Division, National Fisheries Research and Development Institute) ;
  • Park, Hyung-Jun (Department of Marine Biology & Aquaculture, Institute of Marine Industry, College of Marine Science, Gyeongsang National University) ;
  • Baeck, Gun-Wook (Department of Marine Biology & Aquaculture, Institute of Marine Industry, College of Marine Science, Gyeongsang National University) ;
  • Park, Chan-Il (Department of Marine Biology & Aquaculture, Institute of Marine Industry, College of Marine Science, Gyeongsang National University)
  • 투고 : 2010.08.26
  • 심사 : 2010.11.27
  • 발행 : 2010.12.31

초록

Bactericidal/permeability-increasing protein (BPI) and lipopolysaccharide-binding protein (LBP) are important components of the mammalian innate defence system against Gram-negative infections. The BPI/LBP cDNA was identified from the black rockfish ConA/PMA or LPS stimulated leukocyte cDNA library. The full-length BR-BPI/LBP cDNA was 2118 bp long and contained an open reading frame (ORF) of 1422 bp that encoded 473 amino-acid residues. The 5' UTR had a length of 57 bp, and the 3' UTR 639 bp. The molecular weight and theoretical isoelectric point (pI) values were calculated 51.4 kDa and 9.72, respectively. Compared with other known BPI or BPI/LBP peptide sequences, the most conserved regions of the black rockfish BPI/LBP peptide were found to be the BPI1 N-terminal, BPI2 C-terminal domains and a LPS binding domain. Phylogenetic analysis based on the deduced amino acid sequence revealed a homologous relationship between the BPI/LBP sequence of black rockfish and that of other teleosts. The black rockfish BPI/LBP gene was predominantly expressed in the PBLs, head kidney, trunk kidney and spleen. The expression of the black rockfish BPI/LBP molecule was induced in the peripheral blood leukocytes (PBLs) from 1 to 24 h following LPS stimulation, with a peak at 12 h post-stimulation.

키워드

참고문헌

  1. Alexander, C., Rietschel, E.T.: Bacterial lipopolysaccharides and innate immunity. J Endotoxin Res., 7:167-202, 2001.
  2. Baeck, G.W., Kim, J.W., Park, C.I.: Identification and expression analysis of an interferon stimulated gene 15 (ISG15) from black rockfish, Sebastes schlegeli. Fish Shellfish Immunol., 25:679-81, 2008. https://doi.org/10.1016/j.fsi.2008.08.005
  3. Beamer, L.J., Carrol, S.E., Eisenberg, D.: The BPI/LBP family of proteins: a structural analysis of conserved regions. Prot. Sci., 7: 906-914, 1998.
  4. Bingle, C.D., Craven, C.J.: Meet the relatives: a family of BPI- and LBP-related proteins. Trends Immunol., 25:53-55, 2004. https://doi.org/10.1016/j.it.2003.11.007
  5. Dempsey, P.W., Vaidya, S.A., Cheng, G.: The art of war: innate and adaptive immune responses. Cell Mol Life Sci., 60:2604-2621, 2003. https://doi.org/10.1007/s00018-003-3180-y
  6. Gallay, P., Carrel, S., Glauser, M.P., Barras, C., Ulevitch, R.J., Tobias, P.S.: Purification and characterization of murine lipopolysaccharidebinding protein. Infect Immun., 61:378-383, 1993.
  7. Gish, W., David, J.S.: Identification of protein coding regions by database similarity search. Nature Genetics, 3:266-272, 1993. https://doi.org/10.1038/ng0393-266
  8. Gonzalez, M., Gueguen, Y., Destoumieux-Garzon, D., Romestand, B., Fievet, J., Pugniere, M., Roquet, F., Escoubas, J.M., Vandenbulche, F., Levy, O., Saune, L., Bulet, P., Bachere, E.: Evidence of a bactericidal permeability increasing protein in an invertebrate, the Crassostrea gigas Cg-BPI. Proc. Natl. Acad. Sci. U.S.A., 104:17759-17764, 2007. https://doi.org/10.1073/pnas.0702281104
  9. Gray, P.W., Flaggs, G., Leong, S.R., Gumina, R.J., Weiss, J., Ooi, C.E.: Cloning of the cDNA of a human neutrophil bactericidal protein. Structural and functional correlations. J Biol Chem., 264:9505-9509, 1989.
  10. Huang, Y., Lou, H., Wu, X., Chen, Y.: Characterization of the BPI-like gene from a subtracted cDNA library of large yellow croaker (Pseudosciaena crocea) and induced expression by formalin-inactivated Vibrio alginolyticus and Nocardia seriolae vaccine challenges. Fish Shellfish Immunol., 25:740-750, 2008. https://doi.org/10.1016/j.fsi.2008.02.012
  11. Inagawa, H., Honda, T., Kohchi, C., Nishzawa, T., Yoshiura, Y., Nakanishi, T., Yokomizo, Y., Soma, G.: Cloning and characterization of the homolog of mammalian lipopolysaccharide binding protein and bactericidal permeability-increasing protein in rainbow trout Oncorhynchus mykiss. J. Immunol., 168:5638-5644, 2002.
  12. Iovine, N., Elsbach, P., Weiss, J.: An opsonic function of the neutrophil bactericidal/permeability-increasing protein depends on both its N- and C-terminal domains. Proc. Natl. Acad. Sci. U.S.A., 94:10973-10978, 1997. https://doi.org/10.1073/pnas.94.20.10973
  13. Kono, T., Sakai, M.: Molecular cloning of a novel bactericidal permeability-increasing protein/lip opolysacc har ide-binding protein (BPI/LBP) from comment carp Cyprinus carpio L. and its expression. Mol. Immunol., 40:269-278, 2003. https://doi.org/10.1016/S0161-5890(03)00103-2
  14. Lamping, N., Hoess, A., Yu, B., Park, T.C., Kirschning, C.J., Pfeil, D., Reuter, D., Wright, S.D., Herrmann, F., Schumann, R.R.: Effects of site-directed mutagenesis of basic residues (Arg 94, Lys 95, Lys 99) of lipopolysaccharide (LPS)-binding protein on binding and transfer of LPS and subsequent immune cell activation. J Immunol., 157(10):4648-4656, 1996.
  15. Lengacher, S., Jongeneel, C.V., LeRoy, D., Lee, J.D., Kravchenko, V., Ulevitch, R.J., Glauser, M.P., Heumann, D.: Reactivity of murine and human recombinant LPS-binding protein (LBP) within LPS and gram negative bacteria. J Inflamm., 47(4):165-172, 1995.
  16. Leong, S.R., Camerato, T.: Nucleotide sequence of the bovine bactericidal permeability increasing protein (BPI). Nucleic Acids Res., 18:3052, 1990. https://doi.org/10.1093/nar/18.10.3052
  17. Medzhitov, R., Janeway, Jr C.A.: Decoding the patterns of self and nonself by the innate immune system. Science 296:298-300, 2002. https://doi.org/10.1126/science.1068883
  18. Nam, B.H., Ahn, K.J., Kim, Y.O., Kong, H.J., Kim, W.J., Kim, H.S., Lee, S.J., Kim, K.K.: Molecular cloning and characterization of LPS-binding protein/bactericidal permeability-increasing protein (LBP/BPI) from olive flounder, Paralichthys olivaceus. Vet. Immunol. Immunopathol., 133:256-263, 2010. https://doi.org/10.1016/j.vetimm.2009.07.010
  19. Schumann, R.R., Leong, S.R., Flaggs, G.W., Gray, P.W., Wright, S.D., Mathison, J.C.: Structure and function of lipopolysaccharide binding protein. Science, 249:1429-1431, 1990. https://doi.org/10.1126/science.2402637
  20. Stenvik, J., Soltrad, T., Strand, C., Leiros, I., Jorgensen, T.: Cloning and analyses of BPI/LBP cDNA of the Atlantic cod (Gadus morhua L.). Dev. Comp. Immunol., 28:307-323, 2004. https://doi.org/10.1016/j.dci.2003.09.002
  21. Su, G.L., Freeswick, P.D., Geller, D.A., Wang, Q., Shapiro, R.A., Wan, Y.H., Billiar, T.R., Tweardy, D.J., Simmons, R.L., Wang, S.C.: Molecular cloning, characterization, and tissue distribution of rat lipopolysaccharide binding protein. Evidence for extrahepatic expression. J Immunol, 153(2):743-752, 1994.
  22. Suzuki, K., Izumi, S., Tanaka, H., Katagiri, T.: Molecular cloning and expression analysis of the BPI/LBP cDNA and its gene from ayu Plecoglossus altivelis altivelis. J. Fish. Sci., 75:673-681, 2009. https://doi.org/10.1007/s12562-009-0072-6
  23. Thompson, J.D., Higgis, D.G., Gibson, T.J.: CLUSTAL W: improving the sensitivity of progressive multiple sequence alignment through sequence weighting, position specific gap penalties and weight matrix choice. Nucleic Acids Res., 22: 4673-4680, 1994. https://doi.org/10.1093/nar/22.22.4673
  24. Tobias, P.S., Mathison, J.C., Ulevitch, R.J.: A family of lipopolysaccharide binding proteins involved in responses to gramnegative sepsis. J Biol Chem., 263:13479-13481, 1988.
  25. Tobias, P.S., Soldau, K., Iovine, N.M., Elsbach, P., Weiss, J.: Lipopolysaccharide (LPS)-binding proteins BPI and LBP form different types of complexes with LPS. J Biol Chem., 272:18682-18685, 1997. https://doi.org/10.1074/jbc.272.30.18682
  26. Xu, P., Bao, B., He, Q., Peatman, E., He, C., Liu, Z.: Characterization and expression analysis of bactericidal permeability-increasing protein (BPI) antimicrobial peptide gene from channel catfish Ictalurus punctatus. Dev. Comp. Immunol., 29:865-878, 2005. https://doi.org/10.1016/j.dci.2005.03.004
  27. Zarember, K., Elsbach, P., Shin-Kim, K.,Weiss, J.: p15s (15-kD antimicrobial proteins) are stored in the secondary granules of rabbit granulocytes: implications for antibacterial synergy with the bactericidal/perm eability-increasing protein in inflammatory fluids. Blood, 89:672-679, 1997.