Citation

Abdel-Rahman MA, Quintero-Hernández V, Possani LD. Toxicon 2013; 74: 193-207.

Affiliation

Zoology Department, Faculty of Science, Suez Canal University, Ismailia 41522, Egypt. Electronic address: mohamed_hassanain@science.suez.edu.eg.

Copyright

(Copyright © 2013, Elsevier Publishing)

DOI

10.1016/j.toxicon.2013.08.064

PMID

23998939

Abstract

Proteomic analysis of the scorpion venom Scorpio maurus palmatus was performed using reverse-phase HPLC separation followed by mass spectrometry determination. Sixty five components were identified with molecular masses varying from 413 to 14009 Da. The high percentage of peptides (41.5%) was from 3-5 KDa which may represent linear antimicrobial peptides and KScTxs. Also, 155 expressed sequence tags (ESTs) were analyzed through construction the cDNA library prepared from a pair of venomous gland. About 77% of the ESTs correspond to toxin-like peptides and proteins with definite open reading frames. The cDNA sequencing results also show the presence of sequences whose putative products have sequence similarity with antimicrobial peptides (24%), insecticidal toxins, β-NaScTxs, κ-KScTxs, α-KScTxs, calcines and La1-like peptides. Also, we have obtained 23 atypical types of venom molecules not recorded in other scorpion species. Moreover, 9 % of the total ESTs revealed significant similarities with proteins involved in the cellular processes of these scorpion venomous glands. This is the first set of molecular masses and transcripts described from this species, in which various venom molecules have been identified. They belong to either known or unassigned types of scorpion venom peptides and proteins, and provide valuable information for evolutionary analysis and venomics.

Language: en