The immune system of earthworm is very robust despite being in a primitive invertebrate organism. The immune system confers protection against pollutants and pathogens (Ghosh in Environ Sci Pollut Res 25:6196, 2018) and the cells and molecules in the earthworm coelomic fluid are reported (Bilej et al. In: Madame Curie bioscience database [Internet]. Landes Bioscience, Austin, TX, 2000–2013) to play antibacterial, antitumoral and anti trypanosomal role and contain immune molecule including coelom cytolytic factor (CCF), lyesenin and antimicrobial peptides (AMPs). Due to their diverse and advanced roles, they find importance for study both from the point of view of basic sciences and applied biological sciences. Although the immune molecules are reported from different species of earthworm, the physiochemical proteins of AMPs are yet to be studied. Therefore, we performed an insilico study of the different AMPs reported from different species of earthworm from the NCBI. We report for the first time, diversity amongst the AMPs of different species of earthworms, despite functional similarities.
This is a preview of subscription content, log in to check access.
Buy single article
Instant access to the full article PDF.
Tax calculation will be finalised during checkout.
Subscribe to journal
Immediate online access to all issues from 2019. Subscription will auto renew annually.
Tax calculation will be finalised during checkout.
Bilej M, Procházková P, Šilerová M, Josková R (2000–2013) Earthworm immunity. In: Madame Curie bioscience database [Internet]. Landes Bioscience, Austin, TX
Blom N, Gammeltoft S, Brunak S (1999) Sequence- and structure-based prediction of eukaryotic protein phosphorylation sites. J Mol Biol 294(5):1351–1362
Blom N, Ponten T, Gupta R, Gammeltoft S, Brunak S (2004) Prediction of post-translational glycosylation and phosphorylation of proteins from the amino acid sequence. Proteomics 4(6):1633–1649 (Review 2004)
Bruno R, Maresca M, Canaan S, Cavalier J-F, Mabrouk K, Boidin-Wichlacz C, Olleik H, Zeppilli D, Brodin P, Massol F, Jollivet D, Jung S, Tasiemski A (2019) Worms’ antimicrobial peptides. Mar Drugs 17:512
Chenna R, Sugawara H, Koike T, Lopez R, Gibson TJ, Higgins DG, Thompson JD (2003) Multiple sequence alignment with the clustal series of programs. Nucleic Acids Res 31:3497–3500
Cho JH, Park CB, Yoon YG, Kim SC (1998) Lumbricin I, a novel proline-rich antimicrobial peptide from the earthworm: purification, cDNA cloning and molecular characterization. Biochim Biophys Acta 1408(1):67–76
Conti E, Uy M, Leighton L, Blobel G, Kuriyan J (1998) Crystallographic analysis of the recognition of a nuclear localization signal by the nuclear import factor karyopherin alpha. Cell 94:193–204
de Paula VS, Valente AP (2018) A dynamic overview of antimicrobial peptides and their complexes. Molecules 23(8):2040
Engelmann P, Cooper EL, Opper B, Németh P (2011) Earthworm innate immune system. In: Karaca A (ed) Biology of earthworms. Soil biology, vol 24. Springer, Berlin
Epand R, Vogel H (1999) Diversity of antimicrobial peptides and their mechanisms of action. Biochim Biophys Acta 1462:11–28
Gasteiger E, Hoogland C, Gattiker A, Duvaud S, Wilkins MR, Appel RD, Bairoch A (2005) Protein identification and analysis tools on the ExPASy server. In: Walker JM (ed) The proteomics protocols handbook. Humana Press, Totowa, pp 571–607
Ghosh S (2018) Environmental pollutants, pathogens and immune system in earthworms. Environ Sci Pollut Res 25:6196
Gomes-Neto F, Valente AP, Almeida FCL (2013) Modeling the interaction of dodecylphosphocholine micelles with anticoccidial peptide PW2 guided by NMR data. Molecules 18:10056–10080
Harel A, Forbes DJ Importin (2004) Importin beta: conducting a much larger cellular symphony. Mol Cell 16:319–330
Higgins DG (1994) CLUSTAL V: multiple alignment of DNA and protein sequences. Methods Mol Biol 25:307–318
Higgins DG, Sharp PM (1988) CLUSTAL: a package for performing multiple sequence alignment on a microcomputer. Gene 73:237–244
Higgins DG, Sharp PM (1989) Fast and sensitive multiple sequence alignments on a microcomputer. Comput Appl Biosci 5:151–153
Higgins DG, Bleasby AJ, Fuchs R (1992) CLUSTAL V: improved software for multiple sequence alignment. Comput Appl Biosci 8:189–191
Higgins DG, Thompson JD, Gibson TJ (1996) Using CLUSTAL for multiple sequence alignments. Methods Enzymol 266:383–402
Hirigoyenberry F, Lassalle F, Lassegues M (1990) Antibacterial activity of Eisenia fetida andrei coelomic fluid: transcription and translation regulation of lysozyme and proteins evidenced after bacterial infestation. Comp Biochem Physiol B 95(1):71–75
Jeanmougin F, Thompson JD, Gouy M, Higgins DG, Gibson TJ (1998) Multiple sequence alignment with Clustal X. Trends Biochem Sci 23:403–405
Kim DH, Lee IH, Nam ST, Hong J, Zhang P, Hwang JS, Seok H, Choi H, Lee DG, Kim JI, Kim H (2014) Neurotropic and neuroprotective activities of the earthworm peptide Lumbricusin. Biochem Biophys Res Commun 448(3):292–297
Kim DH, Lee IH, Nam ST, Hong J, Zhang P, Lu LF, Hwang JS, Park KC, Kim HJ (2015) Antimicrobial peptide, lumbricusin, ameliorates motor dysfunction and dopaminergic neurodegeneration in a mouse model of Parkinson’s disease. Microbiol Biotechnol 25(10):1640–1647
Kosugi S, Hasebe M, Entani T, Takayama S, Tomita M, Yanagawa H (2008a) Design of peptide inhibitors for the importin alpha/beta nuclear import pathway by activity-based profiling. Chem Biol 15:940–949
Kosugi S, Hasebe M, Tomita M, Yanagawa H (2008b) Nuclear export signal consensus sequences defined using a localization-based yeast selection system. Traffic 9:2053–2062
Kosugi S, Hasebe M, Tomita M, Yanagawa H (2009a) Systematic identification of yeast cell cycle-dependent nucleocytoplasmic shuttling proteins by prediction of composite motifs. Proc Natl Acad Sci USA 106:10171–10176
Kosugi S, Hasebe M, Matsumura N, Takashima H, Miyamoto-Sato E, Tomita M, Yanagawa H (2009b) J Biol Chem 284:478–485
Larkin MA, Blackshields G, Brown NP, Chenna R, McGettigan PA, McWilliam H, Valentin F, Wallace IM, Wilm A, Lopez R, Thompson JD, Gibson TJ, Higgins DG (2007) Clustal W and Clustal X version 2.0. Bioinformatics 23:2947–2948
Lee BJ, Cansizoglu AE, Suel KE, Louis TH, Zhang Z, Chook YM (2006) Rules for nuclear localization sequence recognition by karyopherin beta 2. Cell 126:543–558
Li W, Li S, Zhong J, Zhu Z, Liu J, Wang W (2011) A novel antimicrobial peptide from skin secretions of the earthworm, Pheretima guillelmi (Michaelsen). Peptides 32(6):1146–1150
Liu YQ, Sun ZJ, Wang C, Li SJ, Liu YZ (2004) Purification of a novel antibacterial short peptide in earthworm Eisenia foetida. Acta Biochim Biophys Sin (Shanghai) 36(4):297–302
Mattar EH, Almehdar HA, Yacoub HA, Uversky VN, Redwan EM (2016) Antimicrobial potentials and structural disorder of human and animal defensins. Cytokine Growth Factor Rev 28:95–111
Mo X, Qiao Y, Sun Z, Sun X, Li Y (2012) Molecular toxicity of earthworms induced by cadmium contaminated soil and biomarkers screening. J Environ Sci (China) 24(8):1504–1510
Ossareh-Nazari B, Gwizdek C, Dargemont C (2001) Protein export from the nucleus. Traffic 2:684–689
Roy A, Kucukural A, Zhang Y (2010) I-TASSER: a unified platform for automated protein structure and function prediction. Nat Protoc 5:725–738
Seo M, Lee JH, Baek M, Kim MA, Ahn MY, Kim SH, Yun EY, Hwang JS (2017) A novel role for earthworm peptide Lumbricusin as a regulator of neuroinflammation. Biochem Biophys Res Commun 490(3):1004–1010
Thompson JD, Higgins DG, Gibson TJ (1994) 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
Thompson JD, Gibson TJ, Plewniak F, Jeanmougin F, Higgins DG (1997) The CLUSTAL_X windows interface: flexible strategies for multiple sequence alignment aided by quality analysis tools. Nucleic Acids Res 25:4876–4882
Travkova OG, Moehwald H, Brezesinski G (2017) The interaction of antimicrobial peptides with membranes. Adv Colloid Interface Sci 247:521–532
Valente AP, Miyamoto C, Almeida FCL (2006) Implications of protein conformational diversity for binding and development of new biological active compounds. Curr Med Chem 13:3697–3703
Wang X, Wang X, Zhang Y, Qu X, Yang S (2003) An antimicrobial peptide of the earthworm Pheretima tschiliensis: cDNA cloning, expression and immunolocalization. Biotechnol Lett 25(16):1317–1323
Yang J, Zhang Y (2015) I-TASSER server: new development for protein structure and function predictions. Nucleic Acids Res 43:W174–W181
Yang J, Yan R, Roy A, Xu D, Poisson J, Zhang Y (2015) The I-TASSER Suite: protein structure and function prediction. Nat Methods 12:7–8
Zhang LJ, Gallo RL (2016) Antimicrobial peptides. Curr Biol 26:R14–R19
The author acknowledges the national institute of Science Education and Research (NISER) Bhubaneswar for the study.
Conflict of interest
All authors declare that they have no conflict of interest.
Springer Nature remains neutral with regard to jurisdictional claims in published maps and institutional affiliations.
About this article
Cite this article
Ghosh, S. Insilico Studies on Antimicrobial Peptides (AMPs) from Earthworm. Int J Pept Res Ther 26, 1721–1738 (2020). https://doi.org/10.1007/s10989-019-09970-9
- E. andrei
- I tasser
- L. terrestris
- P. guillelmi (Michaelsen)