Total views : 391
A Mini Review of Functional Proteins in Silkworm Bombyx mori L Haemolymph
This review focuses on the state of the art on haemolymph proteins in lepidopteron insect silkworm Bombyx mori L. Insects are most successful animals in the world. Their success is mostly attributed to their physiological well being and adaptability to most of the environmental conditions is an important reason to be considered evaluating their success. Proteins in insect especially the ones circulating in the blood are seen to be the major contributors for the insects successful survive, owing to their open type circulatory system the haemolymph in insects soaks all the major organs systems in the body and thus making it an important body fluid for regulation of homeostasis. This calls for an detailed study on proteomics of the haemolymph of Bombyx mori which along with being an economical insect, it is being considered as model organism for most frontier sciences like biomaterials, biomedical applications and pharmacokinetic studies, Research on lepidopteron insects has been instrumental in the discovery and the biochemical understanding of many haemolymph plasma proteins. In the present review we analyzed the haemolymph proteins based on their function and molecular characterization. We also could deduce the role of these proteins in insect physiology by comparative analysis with earlier reported proteins.
Heamolymph Proteins, Hypothetical Proteins, Immune Proteins, Silkworm.
- Zhou Z, Yang, H, Zhong B. From genome to proteome: great progress in the domesticated silkworm (Bombyx mori L.). Biochimistry and Biophysics Sinica Act. 2008; 40: 601–11.
- Krishnan M, Konig, S. Progress of proteomic analysis in silkworm Bombyx mori. Biomacromoleculs and Mass Spectroscopy. 2011; 2:179–87.
- Sumino T, Masao N. Masahiko K. Storage proteins in the silkworm Bombyx mori. Insect Biochemistry. 1980; 10:289–303.
- Kanost MR, Kawooya JK, Law JH, Ryan RO, Van Heusden MC, Ziegler R. Insect haemolymph proteins. Advanced Insect Physiology. 1990; 22:299–396.
- Biron DG, Brun C, Lefevre T, Lebarbenchon C, Loxdale HD, Chevenet F, Brizard JP, Thomas F. The pitfalls of proteomics experiments without the correct use of bioinformatics tools. Proteomics. 2006; 6(20):5577–96.
- Wyatt GR. The biochemistry of insect heamolymph. Anneal Review of Entomology. 1961; 6:75–102.
- Gillespie JP, Kanost MR, Trenczek T. Biological mediators of insect immunity. Anneal Review of Entomology. 1997; 42:611–43.
- Omenetto FG, Kaplan DL. New opportunities for an ancient material. Science. 2010; 329:528–31.
- Telfer WH, Kunkel JG. The function and evolution of insect storage hexamers. Anneal Review of Entomology. 1991; 36:205–28.
- Haunerland NH. Insect storage proteins: Gene families and receptors. Insect Biochemistry and Molecular Biology. 1996; 26:755–65.
- Lisbin MJ, Gordon M, Yannoni YM, White K. Function of RRM domains of Drosophila melanogaster ELAV: Rnp1 mutations and rrm domain replacements with ELAV family proteins and SXL. Genetics. 2000; 155:1789–98.
- Galperin MY. Conserved ‘hypothetical’ proteins: new hints and new puzzles. Comparative Functional Genomics. 2001; 2(1):14–18.
- Gert L, Leila AS, Yang JW, Julius PPJ. Searching for hypothetical proteins: Theory and practice based upon original data and literature. Progress in Neurobiology. 2005; 77:90–127.
- Gamo T. Low molecular weight lipoprotein in the haemolymph of silkworm, Bombyx mori. Inheritance, isolation and some properties. Insect Biochemistry. 1978; 8:457–70.
- Agnieszka JP, Anna B, Jochen MD, Malgorzata L, Mariusz J, Grzegorz B. Two crystal structures of Bombyx mori Lipoprotein 3 – structural characterization of a new 30-kDa Lipoprotein family member. PLOSONE. 2013:1–10. DOI: 10.1371/journal.pone.0061303.
- Zhang Y. Iratni R, Erdjument-Bromage H, Tempst P, Reinberg D. Histone deacetylases and SAP18, a novel polypeptide, are components of human sin3 complex. Cell. 1997; 89:357–64.
- Wu M, Sun LV, Vamathevan J, Riegler M, Deboy R. Phylogenomics of the reproductive parasite Wolbachia pipientis wMel: A streamlined genome overrun by mobile genetic elements. PLoS Biology. 2004; 2:327–41.
- Feng-Qian L, Guan-Cheng S, Hitoshi U, Susumu H. Sequences of two cDNAs encoding silkworm homologues of Drosophila melanogaster squid gene. Gene. 1995; 154:295–6.
- Kanost MR, Zhao L. Insect heamolymph proteins from the Ig superfamily. Advances in Comparative and Environmental Physiology. 1996; 23:185–97.
- David C, Neil F, Luis B, Marek K, Wilson C, Lori P, Mei-Ling H. A novel immunoglobulin superfamily receptor for cellular and viral MHC Class I. Molecules Immunity. 1997; 7:273–82.
- Angela P, Vincenzo S, Giosue S, Mose R, Carlo AR, Luciana E. Biochemical and structural characterization of recombinant short-chain NAD(H)-dependent dehydrogenase/reductase from Sulfolobus acidocaldarius highly enantioselective on diaryl diketone benzyl. Applied Microbiology and Biotechnolology. 2013; 97:3949–64.
- Angel V, Elvira J, Borje E, Hans J. The primary structure of alcohol dehydrogenase from Drosophila lebanonensis extensive variation within insect 'short-chain' alcohol dehydrogenase lacking zinc. Europian Journal of Biochemistry. 1989; 180:191–7.
- Wei Y, Meihui W, Hanming Z, Yanping Q, Yaozhou Z. Expression and functional analysis of storage protein 2 in the silkworm Bombyx mori. International Journal of Genomics. 2013.
- Chino H, Downer RG. Insect hemolymph lipophorin: a mechanism of lipid transport in insects. Advanced Biophysics. 1982; 15:67–92.
- Kumar V, Butcher SJ, Oorni K, Engelhardt P, Heikkonen J, Kaski K, Ala-Korpela M, Kovanen PT, Schulz C. Three-Dimensional crvoEM reconstruction of native LDL particles to 16A resolution at physiological body temparature. PLOSONE. 2011; 6(5).
- Elizabeth W, Xiao-Yu W, Michael AW. cDNA and gene sequence of manduca sexta arylphorin, an aromatic amino acid-rich larval serum protein homology to arthropod hemocyanins. Journal of Biological Chemistry. 1989; 264(32):19052–9.
- Ryan RO, Anderson DR, Grimes WJ, Law JH. Arylphorin from Manduca sexta: carbohydrate structure and immunological studies. Archive of Biochemistry and Biophysics. 1985; 243(1):115–24.
- Flore PH, Burand JP, Gettig R, Wood HA. Characterization of DNA polymerase activity in trichoplusia ni cells infected with autographa californica nuclear polyhedrosis virus. Journal of General Virology. 1987; 68:2025–31.
- Howard MT, Satoshi M. Viral RNA-dependent DNA polymerase: RNA-dependent DNA polymerase in virions of rous sarcoma virus. Nature. 1970; 226:1211–13.
- Rivett AJ, Bose S, Brooks P, Broadfoot KI. Regulation of proteasome complexes by gamma-interferon and phosphorylation. Biochemie. 2001; 83(3–4):363–6.
- Brunet A, Kanai F, Stehn J, Xu J, Sarbassova D, Frangioni JV, Dalal SN, DeCaprio JA, Greenberg ME, Yaffe MB. 14-3-3 transits to the nucleus and participates in dynamic nucleocytoplasmic transport. Journal of Cellular Biology. 2002; 156:817–28.
- Efrat PY, Iiana CB, Oded M. Isolation and characterization of four mouse ribosomal-protein-L18 genes that appear to be processed pseudogenes. Gene. 1984; 29:157–66.
- Michael SP, Renu S, Ambikaipakan B, Floyd RS, Edwards AP, Steven LP. On the expansion of ribosomal proteins and RNAs in eukaryotes. Amino Acids. 2014; 46(7):1589–604.
- Annilo T, Laan M, Stahl J, Metspalu A. The human ribosomal protein S7-encoding gene: isolation, structure and localization in 2p25. Gene. 1996; 165(2):297–302.
- John HL, Brian ML, Peter EW. Zinc finger proteins: New insights into structural and functional diversity. Current Opinion in Structural Biology. 2001; 11(1):39–46.
- Decker H, Hellmann N, Jaenicke E, Lieb B, Meissner U, Markl J. Recent progress in hemocyanin research,” Integrated Comparative Biology. 2007; 47:631–44.
- Kaito C, Akimitsu N, Watanabe H, Sekimizu K. Silkworm larvae as an animal model of bacterial infection pathogenic to humans. Microbiology and Pathology. 2002; 32:183–90.
- Fujiyuki T, Imamura K, Hamamoto H, Sekimizu K. Evaluation of therapeutic effects and pharmacokinetics of antibacterial chromogenic agents in a silkworm model of Staphylococcus aureus infection. Drug Discovery and Theory. 2010; 4:349–54.
- Hamamoto H, Tonoike A, Narushima K, Horie R, Sekimizu K. Silkworm as a model animal to evaluate drug candidate toxicity and metabolism. Comparative Biochemistry and Physiology. 2009; 149:334–9.
- Etebari K, Bizhannia AR, Sorati R, Matindoost L. Biochemical changes in haemolymph of silkworm larvae due to pyriproxyfen residue. Pesticides Biochemistry and Physiology. 2007; 88:14–19.
- Nath BS, Suresh A, Varma BM, Kumar RP. Changes in protein metabolism in haemolymph and fat body of the silkworm, Bombyx mori L., in response to organophosphorus insecticides toxicity. Ecotoxicology and Environmental Safety. 1997; 36:169–73.
- Niimi S, Sakurai S. Development changes in juvenile hormone and juvenile hormone acid titers in the hemolymph and in vitro juvenile hormone synthesis by corpora allata of the silkworm, Bombyx mori. Journal of Insect Physiology. 1997; 43:875–84.
- Gu SH, Lin JL, Lin PL, Chen CH. Insulin stimulates ecdysteroidogenesis by prothoracic glands in the silkworm, Bombyx mori. Insect Biochemistry and Molecular Biology. 2009; 39:171–9.
- Ueno Y, Takao M, He N, Yamamoto K, Banno Y, Fujii H. Genetic analysis of basic chymotrypsin inhibitors in the hemolymph of the silkworm, Bombyx mori. Journal of Insect Biotechnology and Sericology. 2006; 75:65–9.
- Kim EJ, Park HJ, Park TH. Inhibition of apoptosis by recombinant 30K protein originating from silkworm haemolymph. Biochemistry and Biophysics Research Communication. 2003; 308:523–8.
- Kim EJ, Rhee WJ, Park TH. Isolation and characterization of an apoptosis inhibiting component from the haemolymph of Bombyx mori. Biochemistry and Biophysics Research Communication. 2001; 285:224–8.
- There are currently no refbacks.
This work is licensed under a Creative Commons Attribution 3.0 License.