Open Access Open Access  Restricted Access Subscription or Fee Access

Effect of BSF Macerative on the Quality of Spun by the Mature Larval Instars of Silkworm, Bombyx mori (L)

Aditi Yogesh Tayade, Rajkumar V. Bajolge, Vitthalrao B. Khyade

Abstract


Food quality and the health status of stages of larval instars of silkworms reflect on the quality of the silk cocoon in sericulture. The pre-pupal stages of black soldier fly (BSF) are with significant quantity and quality of the proteins including the antimicrobial proteins (AMPs). The methanol solution of BSFMeal with the strength of 100 mg/L (100 ppm) was used in the present attempt for the topical application to the fifth instar larval stages of the silkworm, Bombyx mori (L) (Double Hybrid Race). The topical application of methanol solution of BSF-Meal was made at forty-eight hours after the fourth molt. The group of larvae treated with a methanol solution of cecropin (as a standard antimicrobial peptide) with the strength of 100 mg/L (100 ppm), the untreated group of larvae, and solvent-treated group of larvae was also maintained. Treating the fifth instar larvae with a methanol solution of BSF-Meal and a methanol solution of cecropin was found to reflect the significant improvement in the economic characteristics of the cocoons and silk fiber. The weight (grams) of the cocoon (deflossed whole), weight (grams) of silk shell, pupal weight (grams), and percentage of silk shell or ratio in the group of larvae recipient of the topical application of methanol solution of BSF-Meal was recorded 2.786** (±0.719); 0.687** (±0.194); 2.099 and 24.659***, respectively. The silk fiber length (meter); silk fiber weight (gram) and denier scale of silk fiber obtained through reeling the cocoons harvested from the group of larvae treated with a methanol solution of BSF-Meal were recorded at 1358.59*(±216.64); 0.606** (±0.123) and 4.014***, respectively. The weight (grams) of the cocoon (deflossed whole), weight (grams) of silk shell, pupal weight (grams), and percentage of silk shell or ratio in the group of larvae recipient of the topical application of methanol solution of cecropin was recorded 3.189** (±0.918); 0.796** (±0.194); 2.393 and 24.960***, respectively. The silk fiber length (meter); silk fiber weight (gram) and denier scale of silk fiber obtained through reeling the cocoons of cecropin treated group were recorded at 1494.61*(±169.55); 0.796** (±0.118) and 4.793***, respectively. Efficient use of a source of antimicrobial peptides (AMPs) (BSF-Meal) in methanol solution for topical application to the silkworm larvae serves to orchestrate the fortification of health through preventing the infection of microbial pathogens and significant yield of silk product.


Full Text:

PDF

References


Reddy KVR, Yedery RD, Aranha C. Antimicrobial peptides: premises and promises. J Antimicrob Agents. 2004;24(6):536–47. doi: 10.1016/j.ijantimicag.2004.09.005.

Ageitos JM, Sánchez-Pérez A, Calo-Mata P, Villa TG. Antimicrobial peptides (AMPs): ancient

compounds that represent novel weapons in the fight against bacteria. Biochem Pharmacol. 2017;133:117–38. doi: 10.1016/j.bcp.2016.09.018.

Yeaman MR, Yount NY. Mechanisms of antimicrobial peptide action and resistance. Pharmacol Rev. 2003 Mar 1;55(1):27–55. doi: 10.1124/pr.55.1.2.

Sitaram N, Nagaraj R, hosts. Host-Defense antimicrobial peptides: importance of structure for activity. Curr Pharm Des. 2002 Apr 1;8(9):727–42. doi: 10.2174/1381612023395358.

Papagianni M. Ribosomally synthesized peptides with antimicrobial properties: biosynthesis, structure, function, and applications. Biotechnol Adv. 2003 Sep 1;21(6):465–99. doi: 10.1016/s0734–9750(03)00077–6.

Dürr UH, Sudheendra US, Ramamoorthy A. LL-37, the only human member of the cathelicidin family of antimicrobial peptides. Biochim Biophys Acta. 2006;1758(9):1408–25. doi: 10.1016/j.bbamem.2006.03.030.

Dhople V, Krukemeyer A, Ramamoorthy A. The human beta-defensin-3, an antibacterial peptide with multiple biological functions. Biochim Biophys Acta. 2006 Sep 1;1758(9):1499–512. doi: 10.1016/j.bbamem.2006.07.007.

Hancock RE, Rozek A. Role of membranes in the activities of antimicrobial cationic peptides. FEMS Microbiol Lett. 2002 Jan 1;206(2):143–9. doi: 10.1111/j.1574–6968.2002.tb11000.x.

Varkey J, Singh S, Nagaraj R. Antibacterial activity of linear peptides spanning the carboxyterminal β-sheet domain of arthropod defensins. Peptides. 2006 Nov 1;27(11):2614–23. doi:

1016/j.peptides.2006.06.010.

Choudhury A, Guha A, Yadav A, Unni BG, Roy MK. Causal organism of flacherie in the silkworm Antheraea assama Ww: isolation, characterization and its inhibition by garlic extract. Phytother Res. 2002 Mar;16;Suppl 1:S89–90. doi: 10.1002/ptr.810.

Babu SM, Gopalaswamy G, Chandramohan N. Identification of an antiviral principle in Spirulina platensis against Bombyx mori Nuclear Polyhedrosis Virus (BmNPV).

Tefera T, Pringle K. Germination, radial growth, and sporulation of Beauveria bassiana and Metarhizium anisopliae isolates and their virulence to Chilo partellus (Lepidoptera: Pyralidae) at different temperatures.

Venkatesh KR, Srivastava A. Relevance of antibiotics with reference to sericulture industry. Int J Sci Natl. 2010;1(2):97–100.

Khyade VB. Utilization of Garamycin for the control of bacterial disease: flacherrie in the larval

instars of silkworm, Bombyx mori (L) (Race: double Crossed). IJHAF. 2020;4(4):139–53. doi: 10.22161/ijhaf.4.4.2.

Hou Y, Zou Y, Wang F, Gong J, Zhong X, Xia Q, et al. Comparative analysis of proteome maps of silkworm hemolymph during different developmental stages. Proteome Sci. 2010 Dec;8(1):45. doi: 10.1186/1477–5956–8–45.

Chengxiang H, Guangxing Q, Ting L, Xinglin M, Rui Z, Pan Z, et al. Differential gene expression in silkworm in response to Beauveria bassiana infection. Gene. 2011 Sep 15;484(1–2):35–41. doi: 10.1016/j.gene.2011.05.023.

Tanaka H, Yamakawa M. Regulation of the innate immune responses in the silkworm, Bombyx mori. Invertebr Surviv J. 2011 Apr 18;8(1):59–69.

Nesa J, Sadat A, Buccini DF, Kati A, Mandal AK, Franco OL. Antimicrobial peptides from Bombyx mori: a splendid immune defense response in silkworms. RSC advances. 2020;10(1):512-23.

Kalpana S, Hatha AAM, Laksmanaperumalsamy P. Insect Sci. Its Appl. 1994;15:499–502.

Patnaik BB, Kim DH, Oh SH, Song YS, Chanh ND, Kim JS, et al. Molecular cloning and characterization of novel Morus alba germin-like protein gene which encodes for a silkworm gut digestion-resistant antimicrobial protein. PLOS ONE. 2012 Dec 19;7(12):e50900. doi: 10.1371/journal.pone.0050900.

Khyade VB. Influence of juvenoids on silkworm, Bombyx mori; 2004.

Miyashita A, Takahashi S, Ishii K, Sekimizu K, Kaito C. Primed immune responses triggered by ingested bacteria lead to systemic infection tolerance in silkworms. PLOS ONE. 2015 Jun

;10(6):e0130486. doi: 10.1371/journal.pone.0130486. 23. Chen K, Lu Z. Immune responses to bacterial and fungal infections in the silkworm, Bombyx mori.

Dev Comp Immunol. 2018 Jun 1;83:3–11. doi: 10.1016/j.dci.2017.12.024.

Hoffmann JA. The immune response of Drosophila. Nature. 2003 Nov;426(6962):33–8. doi: 10.1038/nature02021.

Taha RH. Physiological changes of diseased mulberry silkworm, Bombyx mori LM Sc ([doctoral dissertation] [Thesis]. Ain Shams University, Faculty of Science).

Acharya A, Sriram S, Sehrawat S, Rahman M, Sehgal D, Gopinathan KP. Bombyx more nucleopolyhedrovirus: molecular biology and biotechnological applications for large-scale synthesis of recombinant proteins. Curr Sci. 2002 Aug 25:455–65.

Subramanian S, Mohanraj P, Muthuswamy M. Newparadigm in silkworm disease management using probiotic application of Streptomyces noursei. Karnataka J Agric Sci. 2010 May 24;22(3).

Phillips I, Casewell M, Cox T, De Groot B, Friis C, Jones R, et al. Does the use of antibiotics in food animals pose a risk to human health? A critical review of published data. J Antimicrob

Chemother. 2004 Jan 1;53(1):28–52. doi: 10.1093/jac/dkg483.

Nesa J, Sadat A, Buccini DF, Kati A, Mandal AK, Franco OL. Antimicrobial peptides from Bombyx mori: a splendid immune defense response in silkworms. RSC Adv. 2019;10(1):512–23. doi: 10.1039/c9ra06864c.

Effect of BSF Macerative on the Quality of Spun by the Mature Larval Instars Tayade et al.

Krishnaswami S, Roy D, Mikherjee SK. Yield and nutritive value of mulberry leaves as influenced by planting season, spacing and frequency of pruning. Indian J Seric. 1970;9(1):38–42.

Krishnaswamy S. Silkworm feeding traits for evaluating the quality of mulberry leaves as influenced by variety, spacing and nitrogen fertilization. Indian J Sericult. 1971;9(1):79–89.

Vijayan K, Sangannavar P, Chattopadhyay S, Dezmirean D, Ercisli S. Cultivation of mulberry: an important genetic and economic source. In: Mulberry: Genetic Improvement in Context of Climate Change. CRC Press; 2021 Jul 25. pp. 32–44.

33Krishnaswami S. Improved method of rearing young age (chawki) silkworms. Central Silk Board, Government of India; 1986.

Khyade VB. Influence of Juvenoids on Silk worm. Bombyx mori L. 2004.

Khyade VB, Mhamane GV. Vividh vanaspati Arkancha Tuti reshim kitak Sangopanasathi Upyojana. Krishi Vdnyan. 2005;4:18–22.

Khyade VB. The activity of protease in the fifth instar silkworm, Bombyx mori (L.)(race: PM X CSR2). Biolife April-June. Vol. 2(2); 2014.

Khyade VB, Patil SB, Khyade SV, Bhawane GP. Influence of acetone maceratives of Vitis vinifera on the larval parameters of silk worm, Bombyx mori (L.). Indian J Comp Anim Physiol. 2002;20:14–8.

Khyade VB, Patil SB, Khyade SV, Bhawane GP. Influence of acetone macerative of Vitis vinifera on the economic parameters of silkworm Bombyx mori (L.). Indian J Comp Anim Physiol. 2003;21(1):28–32.

Khyade VB, Machale SS, Sarwade JP, Patil SB, Deshpande SH. Screening of plant extractives for uvenoid activity in silk worm, Bombyx mori (L.). Journal of Zoological Society of India. J Environ Dev. 2006:61–77.

Khyade VB, Hershko A. Attempt On Utilization of Aqueous Solution of Eurhodin Treated Mulberry Leaves for the Qualitative Cocoons and Silk Filament in silkworm, Bombyx mori (L) Races: Bivoltine Cross Breed [(CSR6 × CSR26) × CSR2 × CSR27)] and multivoltine crossbreed [(PM x CSR. International Journal of Green Chemistry. 2018; 4(2): 1–6.

Khyade VB, Hershko A. Attempt on Utilization of Aqueous Solution of Eurhodin Treated Mulberry Leaves for the Qualitative Cocoons and Silk Filament in silkworm, Bombyx mori (L.) Races: bivoltine Cross Breed [(CSR6 × CSR26) × CSR2 × CSR27)] and multivoltine crossbreed [(PM x

CSR. Int J Green Chem. 2018;4(2):1–6.

Khyade VB, Kulkarni JA. Effect of digoxin treated mulberry leaves on protein profiles in fifth instar

larvae of Silkworm, Bombyx mori (L.)(PM x CSR2). Res J Chem Sci. 2011;1(1):2–6.

Vitthalrao K, Doshi SS. Protein contents and activity of enzymes in the mod gut homogenate of

fifth instar larvae of silkworm, Bombyx mori (L.)(Race: PM x CSR2) fed with herbal drug (Khogo) treated mulberry leaves. Res J Recent Sci ISSN. 2012;2277:2502.

Khyade VB, Khyade VV. Plants: the source of animal hormones. Frontiers in life sciences, the book

published by Science Impact publication, Ahmedpur (Latur)–413515 (India). 2013:151–68.

Khyade VB, Gokule KD, Pawar SR, Deshmukh RB. Utilization of the retinol and Phytol for the

quality improvement of cocoon and silk fibre spinned by fifth instar larvae of silkworm, Bombyx

mori (L.)(Race: PM x CSR2). World Sci News. 2016;42:167–81.

Khyade VB, Sarwade JP. Influence of acetone extractives selected plants on the body wall chitin

of fifth instars of silkworm, Bombyx mori (L.)(Race: PM x CSR2). J Assoc Zoologists, India. 2009;2(1):39–47.

Khyade VB, Gaikawad DR. Insect juvenile hormone. World Sci News. 2016;2016; 44:216–39.

Khyade VB, Sarwade JP. Utilization of digoxin, the herbal product for treating the mulberry leaves and feeding the fifth instar larvae of silkworm, Bombyx mori (L.)(Race: PM x CSR2). Int J Multidiscip Res. 2013;I(12)(III):38–42.

Khyade VB, Sarwade JP. Utilization of retinol through the topical application to the fifth instar larvae of the silkworm, Bombyx mori (L.)(Race: PM × CSR2) for qualitative improvement of the economic parameters. Int J Adv Life Sci (IJALS). 2013;6(5):532–7.

Khyade VB, Gaikawad DR. Insect juvenile hormone. World Sci News. 2016;2016; 44:216–39.

Gohl EPG, Vilensky LD. Textile Science, an Explanation of Fiber Properties. Melbourne: Longman Cheshire; 1983.

Hemmi H, Ishibashi J, Hara S, Yamakawa M. Solution structure of moricin, an antibacterial peptide,

isolated from the silkworm Bombyx mori. FEBS Lett. 2002 May 8;518(1–3):33–8. doi: 10.1016/s0014–5793(02)02637–6.

Jarosz J. Anti–infective defence strategies and methods of escape from entomologic pathogens under immunologic control of insects. Wiad Parazytol. 1996 Jan 1;42(1):3–27.

Khurad AM, Mahulikar A, Rathod MK, Rai MM, Kanginakudru S, Nagaraju J. Vertical transmission of nucleopolyhedrovirus in the silkworm, Bombyx mori L. J Invertebr Pathol. 2004 Sep 1;87(1):8–15. doi: 10.1016/j.jip.2004.05.008.

F Brivio MF, Moro M, Mastore M. Down-regulation of antibacterial peptide synthesis in an insect model induced by the body-surface of an entomoparasite (Steinernema feltiae). Dev Comp Immunol. 2006 Jan 1;30(7):627–38. doi: 10.1016/j.dci.2005.09.008.

Yu Y, Park JW, Kwon HM, Hwang HO, Jang IH, Masuda A, et al. Diversity of innate immune recognition mechanism for bacterial polymeric meso-diaminopimelic acid-type peptidoglycan in insects. J Biol Chem. 2010 Oct 22;285(43):32937–45. doi: 10.1074/jbc.M110.144014.

Yakovlev AY. Induction of antimicrobial peptide synthesis by the fat body cells of maggots of Calliphora vicina R.-D. (Diptera, Calliphoridae). J Evol Biochem Physiol. 2011 Dec;47(6):543–51. doi: 10.1134/S0022093011060056.

Lazzaro BP. Natural selection on the Drosophila antimicrobial immune system. Curr Opin Microbiol. 2008 Jun 1;11(3):284–9. doi: 10.1016/j.mib.2008.05.001.

Gao B, Zhu S. An insect defensin-derived β-hairpin peptide with enhanced antibacterial activity. ACS Chem Biol. 2014 Feb 21;9(2):405–13. doi: 10.1021/cb400591d.

Gao B, Zhu S. Alteration of the mode of antibacterial action of a defensin by the amino-terminal

loop substitution. Biochem Biophys Res Commun. 2012 Oct 5;426(4):630–5. doi: 10.1016/j.bbrc.2012.08.143.

Hoffmann JA, Reichhart JM, Hetru C. Innate immunity in higher insects. Curr Opin Immunol. 1996

Feb 1;8(1):8–13. doi: 10.1016/s0952–7915(96)80098–7.

Wilson R, Chen C, Ratcliffe NA. Innate immunity in insects: the role of multiple, endogenous serum lectins in the recognition of foreign invaders in the cockroach, Blaberus discoidalis. J

Immunol. 1999 Feb 1;162(3):1590–6. doi: 10.4049/jimmunol.162.3.1590.

Lamberty M, Zachary D, Lanot R, Bordereau C, Robert A, Hoffmann JA, et al. Insect immunity.

Constitutive expression of a cysteine-rich antifungal and a linear antibacterial peptide in a termite

insect. J Biol Chem. 2001 Feb 9;276(6):4085–92. doi: 10.1074/jbc.M002998200.

Toke O. Antimicrobial peptides: new candidates in the fight against bacterial infections.

Biopolymers. 2005;80(6):717–35. doi: 10.1002/bip.20286.

Eleftherianos I, Marokhazi J, Millichap PJ, Hodgkinson AJ, Sriboonlert A, ffrench-Constant RH et al. Prior infection of Manduca sexta with non-pathogenic Escherichia coli elicits immunity to pathogenic Photorhabdus luminescens: roles of immune-related proteins shown by RNA interference. Insect Biochem Mol Biol. 2006 Jun 1;36(6):517–25. doi: 10.1016/j.ibmb.2006.04.001.

Eleftherianos I, Gökçen F, Felföldi G, Millichap PJ, Trenczek TE, Ffrench‐Constant RH et al. The immunoglobulin family protein hemolin mediates cellular immune responses to bacteria in the

insect Manduca sexta. Cell Microbiol. 2007 May;9(5):1137–47. doi: 10.1111/j.1462– 5822.2006.00855.x.

Dai H, Rayaprolu S, Gong Y, Huang R, Prakash O, Jiang H. Solution structure, antibacterial

activity, and expression profile of Manduca sexta moricin. J Pept Sci. 2008 Jul;14(7):855–63. doi: 10.1002/psc.1016.

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 formalininactivated Vibrio alginolyticus and Nocardia seriolae vaccine challenges. Fish Shellfish Immunol.

Dec 1;25(6):740–50. doi: 10.1016/j.fsi.2008.02.012. Effect of BSF Macerative on the Quality of Spun by the Mature Larval Instars Tayade et al.

Shen X, Ye G, Cheng X, Yu C, Altosaar I, Hu C. Characterization of an abaecin-like antimicrobial peptide identified from a Pteromalus puparum cDNA clone. J Invertebr Pathol. 2010 Sep 1;105(1):24–9. doi: 10.1016/j.jip.2010.05.006.

Bang K, Park S, Yoo JY, Cho S. Characterization and expression of attacin, an antibacterial proteinencoding gene, from the beet armyworm, Spodoptera exigua (Hübner) (Insecta: Lepidoptera:

Noctuidae). Mol Biol Rep. 2012 May;39(5):5151–9. doi: 10.1007/s11033–011–1311–3.

Ye JS, Zheng XJ, Leung KW, Chen HM, Sheu FS. Induction of transient ion channel-like pores in

a cancer cell by antibiotic peptide. J Biochem. 2004 Aug 1;136(2):255–9. doi: 10.1093/jb/mvh114.

Ha Lee J, Hee Lee I, Noda H, Mita K, Taniai K. Verification of elicitor efficacy of

lipopolysaccharides and peptidoglycans on antibacterial peptide gene expression in Bombyx mori.

Insect Biochem Mol Biol. 2007 Dec 1;37(12):1338–47. doi: 10.1016/j.ibmb.2007.08.007.

Fiolka MJ. Immunosuppressive effect of cyclosporin A on insect humoral immune response. J

Invertebr Pathol. 2008 Jul 1;98(3):287–92. doi: 10.1016/j.jip.2008.03.015.

Jomori T, Natori S. Function of the lipopolysaccharide-binding protein of Periplaneta americana as

an opsonin. FEBS Lett. 1992 Jan 27;296(3):283–6. doi: 10.1016/0014–5793(92)80305-z.

Hashimoto Y, Tabuchi Y, Sakurai K, Kutsuna M, Kurokawa K, Awasaki T et al. Identification of

lipoteichoic acid as a ligand for draper in the phagocytosis of Staphylococcus aureus by Drosophila

hemocytes. J Immunol. 2009 Dec 1;183(11):7451–60. doi: 10.4049/jimmunol.0901032.

Kim CH, Shin YP, Noh MY, Jo YH, Han YS, Seong YS et al. An insect multiligand recognition

protein functions as an opsonin for the phagocytosis of microorganisms. J Biol Chem. 2010 Aug

;285(33):25243–50. doi: 10.1074/jbc.M110.134940.

Hultmark D, Engström A, Bennich H, Kapur R, Boman HG. Insect immunity: isolation and

structure of cecropin D and four minor antibacterial components from Cecropia pupae. Eur J

Biochem. 1982 Sep;127(1):207–17. doi: 10.1111/j.1432–1033.1982.tb06857.x.

Hultmark D, Engström A, Andersson K, Steiner H, Bennich H, Boman HG. Insect immunity. Attacins, a family of antibacterial proteins from Hyalophora cecropia. EMBO J. 1983 Apr;2(4):571–6. doi: 10.1002/j.1460–2075.1983.tb01465.x.

Sawa T, Kurahashi K. Antimicrobial peptides/proteins—application to the therapy of sepsis. Masui.

Nov 1;48(11):1186–93.

Imler JL, Bulet P. Antimicrobial peptides in Drosophila: structures, activities and gene regulation.

Mech Epithelial Def. 2005;86:1–21.

Wang Y, Jin X, Zhu J, Zeng A, Chu F, Yang X, et al. Expression pattern of antibacterial genes in

the Musca domestica. Sci China C Life Sci. 2009 Sep;52(9):823–30. doi: 10.1007/s11427–009– 0121–5.




DOI: https://doi.org/10.37628/ijaba.v8i2.829

Refbacks

  • There are currently no refbacks.