Display options
Cite
Farajzadeh-Sheikh A, Jolodar A, Ghaemmaghami S. Sequence characterization of cDNA sequence of encoding of an antimicrobial Peptide with no disulfide bridge from the Iranian mesobuthus eupeus venomous glands. Iran Red Crescent Med J. 2013;15(1):36-41doi: 10.5812/ircmj.4024.
Farajzadeh-Sheikh, A., Jolodar, A., & Ghaemmaghami, S. (2013). Sequence characterization of cDNA sequence of encoding of an antimicrobial Peptide with no disulfide bridge from the Iranian mesobuthus eupeus venomous glands. Iranian Red Crescent medical journal, 15(1), 36-41. https://doi.org/10.5812/ircmj.4024
Farajzadeh-Sheikh, Ahmad, et al. "Sequence characterization of cDNA sequence of encoding of an antimicrobial Peptide with no disulfide bridge from the Iranian mesobuthus eupeus venomous glands." Iranian Red Crescent medical journal vol. 15,1 (2013): 36-41. doi: https://doi.org/10.5812/ircmj.4024
Farajzadeh-Sheikh A, Jolodar A, Ghaemmaghami S. Sequence characterization of cDNA sequence of encoding of an antimicrobial Peptide with no disulfide bridge from the Iranian mesobuthus eupeus venomous glands. Iran Red Crescent Med J. 2013 Jan;15(1):36-41. doi: 10.5812/ircmj.4024. Epub 2013 Jan 05. PMID: 23486842; PMCID: PMC3589777.
Copy Download .nbib Format: NLM
Share it on

Iran Red Crescent Med J. 2013 Jan;15(1):36-41. doi: 10.5812/ircmj.4024. Epub 2013 Jan 05.

Sequence characterization of cDNA sequence of encoding of an antimicrobial Peptide with no disulfide bridge from the Iranian mesobuthus eupeus venomous glands.

Iranian Red Crescent medical journal

Ahmad Farajzadeh-Sheikh, Abbas Jolodar, Shamsedin Ghaemmaghami

Affiliations

  1. Department of Microbiology, School of Medicine, Ahvaz Jundishapur University of Medical Sciences, Ahvaz, IR Iran.

PMID: 23486842 PMCID: PMC3589777 DOI: 10.5812/ircmj.4024

Abstract

BACKGROUND: Scorpion venom glands produce some antimicrobial peptides (AMP) that can rapidly kill a broad range of microbes and have additional activities that impact on the quality and effectiveness of innate responses and inflammation.

OBJECTIVES: In this study, we reported the identification of a cDNA sequence encoding cysteine-free antimicrobial peptides isolated from venomous glands of this species.

MATERIALS AND METHODS: Total RNA was extracted from the Iranian mesobuthus eupeus venom glands, and cDNA was synthesized by using the modified oligo (dT). The cDNA was used as the template for applying Semi-nested RT- PCR technique. PCR Products were used for direct nucleotide sequencing and the results were compared with Gen Bank database.

RESULTS: A 213 BP cDNA fragment encoding the entire coding region of an antimicrobial toxin from the Iranian scorpion M. Eupeus venom glands were isolated. The full-length sequence of the coding region was 210 BP contained an open reading frame of 70 amino with a predicted molecular mass of 7970.48 Da and theoretical Pi of 9.10. The open reading frame consists of 210 BP encoding a precursor of 70 amino acid residues, including a signal peptide of 23 residues a propertied of 7 residues, and a mature peptide of 34 residues with no disulfide bridge. The peptide has detectable sequence identity to the Lesser Asian mesobuthus eupeus MeVAMP-2 (98%), MeVAMP-9 (60%) and several previously described AMPs from other scorpion venoms including mesobuthus martensii (94%) and buthus occitanus Israelis (82%).

CONCLUSIONS: The secondary structure of the peptide mainly consisted of α-helical structure which was generally conserved by previously reported scorpion counterparts. The phylogenetic analysis showed that the Iranian MeAMP-like toxin was similar but not identical with that of venom antimicrobial peptides from lesser Asian scorpion mesobuthus eupeus.

Keywords: Antimicrobial Peptide Pharbitis; Meucin-25, Mesobuthus Eupeus; Reverse Transcriptase Polymerase Chain Reaction; Scorpions; Venoms

References

  1. Eur J Biochem. 2002 Oct;269(19):4799-810 - PubMed
  2. FEBS Lett. 1992 May 18;302(3):220-2 - PubMed
  3. J Biol Chem. 1998 Jan 23;273(4):2059-66 - PubMed
  4. J Membr Biol. 1985;87(1):35-44 - PubMed
  5. Biopolymers. 2000;55(1):4-30 - PubMed
  6. Toxicon. 2009 Sep 1;54(3):252-61 - PubMed
  7. Toxicon. 2008 Jun 15;51(8):1499-508 - PubMed
  8. Antimicrob Agents Chemother. 2000 Aug;44(8):2086-92 - PubMed
  9. Nat Rev Microbiol. 2005 Mar;3(3):238-50 - PubMed
  10. Biochim Biophys Acta. 1999 Dec 15;1462(1-2):55-70 - PubMed
  11. Eur J Surg Oncol. 2007 May;33(4):459-62 - PubMed
  12. Nucleic Acids Res. 1986 Jun 11;14(11):4683-90 - PubMed
  13. Curr Opin Immunol. 1998 Feb;10(1):41-4 - PubMed
  14. J Biol Chem. 1988 May 15;263(14):6491-4 - PubMed
  15. Biochim Biophys Acta. 1999 Dec 15;1462(1-2):29-54 - PubMed
  16. Eur J Biochem. 2000 Aug;267(16):5023-31 - PubMed
  17. J Biol Chem. 1996 Nov 22;271(47):29537-44 - PubMed
  18. Curr Top Microbiol Immunol. 2006;306:27-66 - PubMed
  19. Biochem Biophys Res Commun. 1993 Jul 15;194(1):17-22 - PubMed
  20. Peptides. 2004 Feb;25(2):143-50 - PubMed
  21. Biochem J. 2001 Oct 1;359(Pt 1):35-45 - PubMed
  22. Biochem Biophys Res Commun. 2002 May 24;293(5):1514-22 - PubMed
  23. Cell Mol Life Sci. 2004 Jul;61(14):1751-63 - PubMed
  24. Eur J Biochem. 1999 Sep;264(2):287-300 - PubMed

Publication Types