International Journal of Industrial Entomology and Biomaterials

Korean Society of Sericultural Science (한국잠사학회)
권호 표지

Computational Analysis of Apolipophorin-III in Hyphantria cunea

  • Chandrasekar R. (Department of Biotechnology, Bharathidasan University, Division of Applied Life Science, Gyeongsang National University) ;
  • Dhanalakshmi R. (Department of Biotechnology, Bharathidasan University) ;
  • Krishnan M. (Department of Biotechnology, Bharathidasan University) ;
  • Kim H. J. (Division of Applied Life Science, Gyeongsang National University) ;
  • Jeong H. C. (Hampyeong County Insect Institute) ;
  • Seo S. J. (Division of Applied Life Science, Gyeongsang National University)
  • Published : 2005.03.01
Download PDF
⟨ Previous Next ⟩

Abstract

Recently a cDNA clone of apoLp-III from Hyphantria cunea was isolated and subjected to computational analysis to compare with other available sequences. Multiple sequence alignments were carried out using the amino acid sequences of apoLp-III from six insects. It was found that the H. cunea apoLp-III has relatively high sequence identities to Spodoptera litura ($69.5\%$), Manduca sexta ($66.8\%$), Galleria mellonella ($65.1\%$), Bombyx mori N4 ($54.3\%$) but less identity to Locusta migratoria ($18.3\%$). The amino acid composition was compared with other insects using EXPASY tools; it shows that alanine (Ala), glutamine (Gln), leucine (Leu) and lysine (Lys) are the major amino acid components of apoLp-III in H. cunea as well as other lepidopterans. Homology modeling performed using PSI-BLAST (PDB template M. sexta) reveals that the apoLp-III molecules consist of five, long amphipathic alpha helical bundles with short loops connecting the helices and shows homology with other insects. Phylogenetic analysis shows that the orthopteran apoLp-III represented by locust was most distantly related to the lepidopteran insects.

Keywords

References

  1. Altschul, S. F, W. Gish, W. Miller, E. W. yers and D. J. Lipman (1990) Basic local alignment search tool. J. Mol. Biol. 215, 403-410 https://doi.org/10.1016/S0022-2836(05)80360-2
  2. Appel, R. D., A. Bairoch and D. F Hochstrasser (1994) Some measure of comparative performance in physicochemical analysis from sequences. Trends Biochem. Sci. 19, 258-260 https://doi.org/10.1016/0968-0004(94)90153-8
  3. Benson, D. A., M. S. Boguski, D. J. Lipman, J. Ostell and B. F. Ouellette (1998) Genbank. Nucleic Acids Res. 26, 1-7 https://doi.org/10.1093/nar/26.1.1
  4. Blaber, M., X. J. Zhang and B. W. Mathews (1993) Structural basis of amino acid alpha helix propensity. Science 262, 917-918
  5. Boguski, M. S., M. Freeman, N. A. Elshourbagy, J. M. Taylor and J. I. Gordon (1986) Structure of apoLp-III in insects. J. Lipid Res. 27, 1011-1034
  6. Breiter, D. R., M. R. Kanost, N. N. Benning, G. Wesenberg and H. Law (1991) Molecular structure of an apolipoprotein determined at 2.5 A resolution. Biochemistry 30, 603-608 https://doi.org/10.1021/bi00217a002
  7. Brenner, S. E., C. Chothia and T. J. P. Hubbard (1997) Population statistic of protein structures: lessons from structural classification. Curr. Opin. Struct. Biol. 7, 369-376 https://doi.org/10.1016/S0959-440X(97)80054-1
  8. Estela, L. A., L. E. Canavoso, Z. E. Jouni, J. E. Pennington, K. Tsuchida and M. A. Wells (2001) Lipid storage and mobilization in insects: current status and future directions. Insect Biochem. Mol. Biol. 31, 7-17 https://doi.org/10.1016/S0965-1748(00)00102-8
  9. Fredji, T.(2000) Biocomputing in nutshell. Developer IQ, 2, 37
  10. Halwani, A. E., D. F. Niven and G. B. Dunphy (2001) Apolipophorin-III in the greater wax moth, Galleria mellonella (Lepidopteran: Phyralidae). Arch. Insect Biochem. Physiol. 48, 135-143 https://doi.org/10.1002/arch.1066
  11. Henikoff, S. (1996) Scores for sequence searches and align ments. Curr. Opin. Struct. Biol. 6, 353-360 https://doi.org/10.1016/S0959-440X(96)80055-8
  12. Kanost, M. R., M. S. Boguski, M. Freeman, J. I. Gordon, G. R. Wyatt and M. A. Wells (1988) Primary structure of apolipophorin-III from the migratory locust, Locusta migratoria. J Biol. Chem. 26, 10568-10573
  13. Kim, H. J., H. J. Je, S. Y. Park, J. H. Lee, B. R. Jin, H. K. Yun, C. Y. Yun, Y. S. Han, Y. J. Kang and S. J. Seo (2004) Immune activation of apolipophorin-III and its distribution in hemocyte from Hyphantria cunea. Insect Biochem. Mol. Biol. 34, 1011-1023 https://doi.org/10.1016/j.ibmb.2004.05.005
  14. Kim, H. J., S. D. Lee and S. J. Seo (2001) Molecular characterization of apolipophorin-III in the fall webworm Hyphantria cunea Drury. Int. J. Indust. Entomol. 3, 163-168
  15. Kim, E. S., S. H. Kim, C. S. Choi, U. I. Park and H. R. Kim (1998) Cloning and expression of apolipophorin-III from the common cutworm, Spodoptera litura. Arch. Insect Biochem. Physiol. 39, 116-173
  16. Kiss, R. S., M. W. Paul, V. Narayanaswami, J. Cohen and R. O. Ryan (2003) Structure-guided protein engineering modulates helix bundle exchangeable apolipoprotein properties. J. Biochem. 278, 21952-21959
  17. Kyte, J. and R. F. Doolittle (1996) A simple method of displaying the hydropathic character of a protein. J. Mol. Biol.157, 105-132
  18. Mathew J. W. and D. H. Jonathan (2004) Prediction protein secondary structure by cascade-correlation neural networks. Bioinformatics Application Note 20, 419-420 https://doi.org/10.1093/bioinformatics/btg423
  19. Narayanaswami, V., J. Wang, D. Schieve, C. M. Kary and R. O. Ryan (1999) A molecular trigger of lipid binding induced opening of a helix bundle exchangeable apolipoprotein. Proc. Natl. Aced. Sci. 96, 4366-4371 https://doi.org/10.1073/pnas.96.8.4366
  20. Narayanaswami, V. and R. O. Ryan (2000) Molecular basis of exchangeable apolipopretein function. Biochem. Biophys. Acta 1483, 15-36 https://doi.org/10.1016/S1388-1981(99)00176-6
  21. Niere, M., M. Dettloff, T. Maier, M. Ziegler and A. Wiesner (2001) Insect immune activation by apolipophorin- III is correlated with the lipid binding properties of this protein, Biochemistry 40, 11503-11508
  22. Niere, M., C. Meibitzer, M. Dettloff, C. Weise, M. Ziegler and A. Wiesner (1999) Insect immune activation by recombinant Gallleria mellonella apolipophorin-III. Biochim. Biophys. Acta 1433, 16-26 https://doi.org/10.1016/S0167-4838(99)00148-X
  23. Rost, B. and C. Sander (1993) Prediction of protein secondary structure at better than 70% accuracy. J. Mol. Biol. 232, 584-599 https://doi.org/10.1006/jmbi.1993.1413
  24. Ryan, R. O. (1990) Dynamics in insect lipophorin metabolism. J. Lipid Res. 31, 1725-1739
  25. Sahoo, D., V. Narayanaswami, K. Oikawa, C. M. Kay and R. O. Ryan (1998) Fluorescence studies of exchangeable apolipoprotein lipid interactions. Superficial association of apolipoprotein-III with lipoprotein surfaces, J. Biol. Chem. 237, 1403-1408
  26. Segrest, J. P., M. K. Jones, H. Dc Loof and N. Dashti (2001) Structure of apolipoprotein B-100 in low density lipoproteins. J. Lipid Res. 42, 1346-1367
  27. Smith, A. F., L. M. Owen, L. M. Strobel, H. Chen, M. R. Kanost, E. Hanneman and M. A. Wells (1994) Exchangeable apolipoproteins of insects share a common structural motif. J. Lipid Res. 35, 1976-1984
  28. Soulages, J. L., J. Pennington, O. Bendavid and Wells, M. A., (1998) Role of glycosylation in the lipid binding activity of the exchangeable apolipoprotein, apolipophorin-III. Biochem. Biophys. Res. Commun. 243, 372-376 https://doi.org/10.1006/bbrc.1998.8099
  29. Soulages, J. L. and M. A. Wells (1994) Lipophorin: the structure of an insect lipoprotein and its role in lipid transport in insects. Adv. Protein Chem. 45, 371-415 https://doi.org/10.1016/S0065-3233(08)60644-0
  30. Thompson, J. D., T. J. Gibson, F. Plewniak, F. Jeanmougin and D. G. Higgins (1997) The CLUSTAL-X windows interface: flexible strategies for multiple sequence alignment aided by quality analysis tools. Nucleic Acids Res. 25, 4876-4882 https://doi.org/10.1093/nar/25.24.4876
  31. Van der Horst, D .J., D. Hoof, W. J. van Marrewijik and K. W. Rodenburg (2002) Alternative lipid mobilization: The insect shuttle system. Mol. Cell. Biochem. 239, 113-119 https://doi.org/10.1023/A:1020541010547
  32. Van der Horst, D. J., W. J. van Marrewijik and J. H. B. Diederen (2001) Adipokinetic hormone of insect: release, signal transduction and responses. Int. Rev. Cytol. 211, 179-240 https://doi.org/10.1016/S0074-7696(01)11019-3
  33. Van der Horst, D. J., R. O. Ryan, M. C. V. Heusden, T. K. Suchulz, J. M. V. Doorn, J. H. Law and A. M. Been Akkers (1988) An insect lipoprotein hybrid helps to define the role of apolipophorin III. J. Biol. Chem. 263, 2027-2033
  34. Wang, J., S. Gagne, B. D. Sykes and R. O. Ryan (1997) Insight into lipid surface recognition and reversible conformational adaptations of an exchangeable apolipoprotein by multidimensional NMR techniques. J. Biol. Chem. 272, 17912-17921 https://doi.org/10.1074/jbc.272.29.17912
  35. Weers, P. M. M., V. Narayanaswami, C. M. Kay and R. O. Ryan (1999) Interaction of an exchangeable apolipoprotein with phospholipids vesicles and lipoprotein particles. Role of leucines 32, 34 and 95 in Locusta migratoria apolipophorin-III. J. Biol. Chem. 274, 21804-21810 https://doi.org/10.1074/jbc.274.31.21804
  36. Weise, C., P. Franke and A. Wiesner (1998) Primary structure of apolipophorin-III from the greater wax moth, Galleria mellonella. J. Protein Chem. 17, 633-640 https://doi.org/10.1007/BF02780964
  37. Wells, M. A., R. O. Ryan, J. K. Kawooya and J. H. Law (1987) Role of apolipoprotein-III in vivo lipoprotein inter conversions in adult Manduca sexta. J. Biol. Chem. 262, 4172-4176
  38. Wiesner, A., Y. Fukunishi, L. R. Murphy, A. Fadel and R. M. Levy (2000) Ietrative sequence/secondary structure search for protein homologs: comparison with amino acid sequence alignments and application to fold recognition in genome databases. Biolryformatics 16, 988-1002
  39. Wiesner, A., S. Losen, P. Kopacek and P. Gotz (1997) Isolated apolipophorin-III from Galleria mellonella stimulates the immune reactions of this insect. J. Insect Physiol. 43, 383-391 https://doi.org/10.1016/S0022-1910(96)00113-8
  40. Wilson, C., M. R. Wardell, K. H. Weisgraber, R. W. Mahley and D. A. Agard (1991) Three dimensional structure of the LDL receptor-binding domain of human apolipoprotein E. Science 252, 1817-1822 https://doi.org/10.1126/science.2063194
  41. Yamauchi, Y., C. Hoeffer, A. Yamamoto, H. Takeda, R. Ishihara, H. Maekawa, R. Sato, S. I. Seong, M. Sumida, M. A. Wells and K. Tsuchida (2000) cDNA and deduced amino acid sequences of apolipophorin-III from Bombyx mori and Bomyx mandarina. Arch. Insect Biochem. Physiol. 43, 16-21 https://doi.org/10.1002/(SICI)1520-6327(200001)43:1<16::AID-ARCH3>3.0.CO;2-W
  42. Zakarian, R. J., G. B. Dunphy and J. M. Quiot (2002) Growth of an ovarian cell line of Galleria mellonella and its response to immune-inducing factors. In Vitro Cell Dev. Biol. Anim. 38, 572-581 https://doi.org/10.1290/1543-706X(2002)38<572:GOAOCL>2.0.CO;2