생명과학회지 (Journal of Life Science)

  • 제18권3호
  • /
  • Pages.409-413
  • /
  • 2008
  • /
  • 1225-9918(pISSN)
  • /
  • 2287-3406(eISSN)
한국생명과학회 (Korean Society of Life Science)
권호 표지
DOI QR코드

DOI QR Code

작잠(Antheraea pernyi) arylphorin의 항체를 이용한 수종의 나비목 야생 견사곤충들 간의 면역학적 비교

Comparison of Arylphorin of Antheraea pernyi with Those of Several Lepidopteran Wild Silkmoths by Western Blot Analysis.

  • 박남숙 (부산대학교 생명자원과학대학 생명환경화학과) ;
  • 김미애 (부산대학교 생명자원과학대학 생명환경화학과) ;
  • 박현철 (부산대학교 생명자원과학대학 생명환경화학과) ;
  • 김근기 (부산대학교 생명자원과학대학 생명환경화학과) ;
  • 진병래 (동아대학교 생명자원과학대학 응용생명공학과) ;
  • 이상몽 (부산대학교 생명자원과학대학 생명환경화학과)
  • Park, Nam-Sook (Dept. of Life Science & Environmental Biochemistry, College of Natural Resources & Life Science, Pusan National University) ;
  • Kim, Mi-Ae (Dept. of Life Science & Environmental Biochemistry, College of Natural Resources & Life Science, Pusan National University) ;
  • Park, Hyun-Chul (Dept. of Life Science & Environmental Biochemistry, College of Natural Resources & Life Science, Pusan National University) ;
  • Kim, Keun-Ki (Dept. of Life Science & Environmental Biochemistry, College of Natural Resources & Life Science, Pusan National University) ;
  • Jin, Byung-Rae (College of Natural Resources and Life Science, Dong-A University) ;
  • Lee, Sang-Mong (Dept. of Life Science & Environmental Biochemistry, College of Natural Resources & Life Science, Pusan National University)
  • 발행 : 2008.03.31
PDF 다운로드
⟨ 이전 논문 다음 논문 ⟩

초록

작잠 arylphorin 항 혈청을 사용하여 천잠, 가중나무 산누에 나방 및 옥색긴꼬리 산누에나방의 5령 유충의 혈림프, 피부, 지방체, 중장 및 실샘에 대한 종(species) 공통항원의 존재 여부를 비교${\cdot}$검토하였다. 4개종은 혈림프, 피부, 지방체, 중장 실샘 등 종별 조직에 따라 다소간 검출유무의 차이는 있으나 작잠 arylphorin 항 혈청에 대한 공통항원의 존재는 4종의 야생곤충 모두에서 확인되었으며, 특히 혈림프에서 가장 강력한 항원-항체 반응이 관찰되었다. 이상의 결과에서 A. pernyi arylphorin은 천잠 등 4개의 공시곤충들의 공통 조상유전자로부터 유래한 단백질일 가능성이 높은 것으로 사료된다.

The occurences of proteins relating to Antheraea pernyi arylphorin in haemolymph, fat body, integument, midgut and silkgland of the wild silkmoths, Antheraea yamamai, Antheraea pernyi, Samia cynthia pryeri and Actias gnoma in the 5th larval instar were investigated by immunoblot analysis using mouse polyclonal antibody against A. pernyi arylphorin as probe. In A. yamamai, A. pernyi, S. cynthia pryeri and A. gnoma, the major immunoreactive antigenic proteins with a molecular weight of 80 KDa against the antisera of the A. pernyi arylphorin were clearly observed in the haemolymph, but in the integument, fat body, midgut and silkgland of the corresponding wild silkmoths the presence of the immunoreactive proteins were very variable. These results suggest that the A. pernyi arylphorin has almost same immunological identity with those of the wild silkmoths, A. yamamai, S. cynthia pryeri and A. gnoma though the distribution of the corresponding antigenic arylphorins is different according to the tissues of the wild silkmoths.

키워드

참고문헌

  1. Bean, D. W. and D. L. Silhack. 1989. Changes in titer of the female-predominant storage protein (81k) during larval and pupal development of the wax moth, Galleria mellonella. Arch. Insect. Biochem. Physiol. 10, 333-348. https://doi.org/10.1002/arch.940100408
  2. DeKort, C. A. D. and A. B. Koopmanschap. 1987. Isolation and characterization of a larval hemolymph protein in Locusta migratoria. Arch. Insect Biochem. Physiol. 4, 191-203. https://doi.org/10.1002/arch.940040305
  3. Haunerland, N. H. and W. S. Bowers. 1986. Arylphorin from the corn earworm. Heliothis zea. Insect Biochem. 16, 617-625. https://doi.org/10.1016/0020-1790(86)90004-1
  4. Hwang, J. S., J. S. Lee, T. W. Goo, S. M. Lee and O. Y. Kwon. 1999. Comparative analysis of nucleotide sequence and codon usage of arylphorin gene cloned from four silk-producing insects and their molecular phylogenetics. J. Life Science 9, 84-89.
  5. Kim, B. Y., Y. W. Choi, N. S. Park and S. M. Lee. 2001. Collection and characteristics of the wild silkmoth, Samia cynthia pryeri, in Korea, Int. J. Indust. Entomol. 3, 101-103.
  6. Kim, S. H., S. K. Hwang, R. A. Dwek, P. M. Rudd, Y. H. Ahn, E. H. Kim, C. J. Cheong, S. I. Kim,, N. S. Park and S. M. Lee. 2003. Structural determination of the N-glycans of a lepidopteran arylphorin reveals the presence of a monoglucosylated oligosaccharide in the storage protein. Glycobiology 13, 147-157. https://doi.org/10.1093/glycob/cwg023
  7. Laemmli, U. K. 1970. Cleavage off structure during the assembly of the head of bacteriophage T4. Nature 277, 680-685.
  8. Park, N. S., S. M. Lee, J. Y. Moon and S. I. Seong. 1999. Purification and partial characterization of the storage protein- like protein from the 5th Instar larval haemolymph of the Chinese oak silkworm, Antheraea pernyi. Korean J. Seric. Sci. 41, 75-81.
  9. Palli, S. R. and M. Locke. 1987. Purification and characterization of three major hemolymph proteins of an insect Calpodes ethlius (Lepidoptera, Hesperiidae). Arch. Insect Biochem. Physiol. 5, 233-244. https://doi.org/10.1002/arch.940050403
  10. Park, N. S. 2001. Purification and characterization of arylphorin from larval Hemolymph of the Chinese oak silkworm, Antheraea pernyi. Thesis for the Degree of Master of Science. Miryang National University.
  11. Park, S. B., J. W. Kim, S. H. Kim, N. S. Park, B. R. Jin, J. S. Hwang, S. I. Seong, B. H. Lee, E. J. Park and S. M. Lee. 2003. Purification and characterization of arylphorin of the chinese oak silkmoth, Antheraea pernyi. Int. Indust. Entomol. 6, 33-44.
  12. Roberts. D. B. 1983. The evolution of larval serum protein genes in Drosophila, pp. 86-101, In Scheller, K. (ed.), The Larval Serum Proteins of Insects Thieme, Stuttgart.
  13. Ryan, R. O., J. O. Schmidt and J. H. Law. 1984. Arylphorin from the haemolymph of the larval honeybee, Apis. mellifera. Insect Biochem. 14, 515-520. https://doi.org/10.1016/0020-1790(84)90005-2
  14. Ryan, R. O., D. R. Anderson. W. J. Grimes and J. H. Law. 1985. Arylphorin from Manduca sexta; carbohydrate structure and immunological studies. Arch. Biochem. Biophys. 243, 115-124. https://doi.org/10.1016/0003-9861(85)90779-9
  15. Ryan. R. O., S. V. Prasad, E. J. Henriksen, M. A. Wells and J. H. Law. 1986. Lipoprotein interconversions in an insect, Manduca sexta. Evidence for a lipid transfer factor in the hemolymph. J. Biol. Chem. 261, 563-568.
  16. Ryu, C. W., M. A. Kim, N. S. Park, H. D. Sohn, S. B. Park, H. O. Lee, J. Y. Moon, S. I. Seong and S. M. Lee. 2002. Developmental and morphological characterization of the wild silkmoth, Actias gnoma, in Korea. Int. J. Indust. Entomol. 5, 79-83.
  17. Scheller, K., H. P. Zimmerman and C. E. Sekeris. 1980. Calliphorin, a protein involoved in cuticle formation of the blowfly, Calliphara vicina. Z. Naturforsch. 35, 387-389.
  18. Sekeris, C. E. and K. M. Scheller. 1977. Calliphorin, a protein of the blowfly; correlation between the amount of protein, its biosynthesis, and the titer of translatable calliphorin- mRNA during development. Dev. Biol. 59, 12-23. https://doi.org/10.1016/0012-1606(77)90236-6
  19. Telfer, W. H. and H. C. Jr. Massey. 1987. A storage hexamer from Hyalophora that binds riboflavin and resembles the apoprotein of hemocyanin, pp. 305-314, In Law, J. H. (ed.), Molecular Entomology, Alar, R. Liss, New York.
  20. Telfer, W. H., P. S. Keim and J. H. Law. 1983. Arylphorin, a new protein from Hyalophora cecropia : Comparisons with calliphorin and manducin. Insect Biochem. 13, 301-613.
  21. Tojo, S., T. Betchaku, V. J. Ziccardi and G. R. Wyatt. 1978. Fat body protein granules and storage proteins in the silkmoth, Hyalophora cecropia, J. Cell Biol. 78, 823-838. https://doi.org/10.1083/jcb.78.3.823
  22. Tojo, S., M. Nagata and M. Kobayashi. 1980. Storage proteins in the silkworm, Bombyx mori. Insect Biochem. 10, 289-303. https://doi.org/10.1016/0020-1790(80)90024-4
  23. Yoon, H. J., P. D. Kang, S. M. Lee, S. E. Kim and K. Y. Kim. 2007. Improvement of occasional artificial hatching and incubation method in diapause egg of the wild silkmoth, Antheraea yamamai. Korean J. Appl. Entomol. 46, 295-302. https://doi.org/10.5656/KSAE.2007.46.2.295

피인용 문헌

  1. cDNA Cloning and Stage-Dependant Expression of Arylphorin Gene from Chinese Oak Silkworm, Antheraea pernyi vol.20, pp.8, 2010, https://doi.org/10.5352/JLS.2010.20.8.1193