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Paper Information

Journal:   IRANIAN RED CRESCENT MEDICAL JOURNAL (IRCMJ)   2013 , Volume 15 , Number 1; Page(s) 31 To 46.
 
Paper: 

SEQUENCE CHARACTERIZATION OF CDNA SEQUENCE OF ENCODING OF AN ANTIMICROBIAL PEPTIDE WITH NO DISULFIDE BRIDGE FROM THE IRANIAN MESOBUTHUS EUPEUS VENOMOUS GLANDS

 
 
Author(s):  FARAJZADEH SHEIKH AHMAD, JOLODAR ABBAS*, GHAEMMAGHAMI SHAMSEDIN
 
* DEPARTMENT OF BASIC SCIENCES, FACULTY OF VETERINARY MEDICINE, SHAHID CHAMRAN UNIVERSITY OF AHVAZ, AHVAZ, IR IRAN
 
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 ?-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.

 
Keyword(s): SCORPIONS, VENOMS, ANTIMICROBIAL PEPTIDE PHARBITIS, REVERSE TRANSCRIPTASE POLYMERASE CHAIN REACTION, MEUCIN-25, MESOBUTHUS EUPEUS
 
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