title: Assessment of immunogenic characteristics of Hemiscorpius lepturus venom and its cross-reactivity with venoms from Androctonus crassicauda and Mesobuthus eupeus.
abstract: Hemiscorpius lepturus (H. lepturus), one of the most venomous scorpions in tropical and sub-tropical areas, belongs to the Hemiscorpiidae family. Studies of antibodies in sera against the protein component of the venom from this organism can be of great use for the development of engineered variants of proteins for eventual use in the diagnosis/treatment of, and prevention of reactions to, stings. In the present in vitro study, the proteins of H. lepturus venom, which could specifically activate the production of immunoglobulin G (IgG) in victims accidently exposed to the venom from this scorpion, were evaluated and their cross-reactivity with venoms from two other important scorpion species including Androctonus crassicauda and Mesobuthus eupeus assessed. H. lepturus venom was analyzed with respect to its protein composition and its antigenic properties against antibodies found in sera collected from victims exposed to the venom of this scorpion within a previous 2-month period. The cross-reactivity of the H. lepturus venom with those from A. crassicauda and M. eupeus was assessed using ELISA and immunoblotting. Electrophoretic analysis of the venom of H. lepturus revealed several protein bands with weights of 8-116 KDa. The most frequent IgG-reactive bands in the test sera had weights of 34, 50, and 116 kDa. A weak cross-reactivity H. lepturus of venom with venoms from A. crassicauda and M. eupeus was detected. The results of immunoblotting and ELISA experiments revealed that H. lepturus venom activated the host immune response, leading to the production of a high titer of antibodies. Clearly, a determination of the major immunogenic components of H. lepturus venom could be valuable for future studies and ultimately of great importance for the potential production of recombinant or hypo-venom variants of these proteins.
authors.affiliation: Toxicology Research Center .
authors.forename: Shahin
authors.initials: S
authors.lastname: Khanbashi
authors.forename: Ali
authors.initials: A
authors.lastname: Khodadadi
authors.forename: Mohammad-Ali
authors.initials: MA
authors.lastname: Assarehzadegan
authors.forename: Mohammad Hassan
authors.initials: MH
authors.lastname: Pipelzadeh
authors.forename: Babak
authors.initials: B
authors.lastname: Vazirianzadeh
authors.forename: Mohsen
authors.initials: M
authors.lastname: Hosseinzadeh
authors.forename: Ali Hassan
authors.initials: AH
authors.lastname: Rahmani
authors.forename: Akbar
authors.initials: A
authors.lastname: Asmar
mesh_terms: D000293:Adolescent; D000328:Adult; D000818:Animals; D000997:Antivenins / Q000627:therapeutic use; D002648:Child; D003429:Cross Reactions; D005260:Female; D006801:Humans; D007106:Immune Sera / Q000378:metabolism; D015151:Immunoblotting; D007074:Immunoglobulin G / Q000378:metabolism; D019476:Insect Proteins / Q000276:immunology / Q000378:metabolism*; D008297:Male; D065008:Scorpion Stings / Q000175:diagnosis / Q000276:immunology* / Q000628:therapy; D012604:Scorpion Venoms / Q000276:immunology / Q000378:metabolism*; D012605:Scorpions / Q000276:immunology*; D013045:Species Specificity; D055815:Young Adult
chemical_list: D000997:Antivenins; D007106:Immune Sera; D007074:Immunoglobulin G; D019476:Insect Proteins; D012604:Scorpion Venoms
keywords: Cross-reactivity; hemiscorpius lepturus; immunogenic; venom