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      The Cuban scorpion Rhopalurus junceus (Scorpiones, Buthidae): component variations in venom samples collected in different geographical areas

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          Abstract

          Backgound

          The venom of the Cuban scorpion Rhopalurus junceus is poorly study from the point of view of their components at molecular level and the functions associated. The purpose of this article was to conduct a proteomic analysis of venom components from scorpions collected in different geographical areas of the country.

          Results

          Venom from the blue scorpion, as it is called, was collected separately from specimens of five distinct Cuban towns (Moa, La Poa, Limonar, El Chote and Farallones) of the Nipe-Sagua-Baracoa mountain massif and fractionated by high performance liquid chromatography (HPLC); the molecular masses of each fraction were ascertained by mass spectrometry analysis. At least 153 different molecular mass components were identified among the five samples analyzed. Molecular masses varied from 466 to 19755 Da. Scorpion HPLC profiles differed among these different geographical locations and the predominant molecular masses of their components. The most evident differences are in the relative concentration of the venom components. The most abundant components presented molecular weights around 4 kDa, known to be K +-channel specific peptides, and 7 kDa, known to be Na +-channel specific peptides, but with small molecular weight differences. Approximately 30 peptides found in venom samples from the different geographical areas are identical, supporting the idea that they all probably belong to the same species, with some interpopulational variations. Differences were also found in the presence of phospholipase, found in venoms from the Poa area (molecular weights on the order of 14 to 19 kDa). The only ubiquitous enzyme identified in the venoms from all five localities studied (hyaluronidase) presented the same 45 kD molecular mass, identified by gel electrophoresis analysis.

          Conclusions

          The venom of these scorpions from different geographical areas seem to be similar, and are rich in peptides that have of the same molecular masses of the peptides purified from other scorpions that affect ion-channel functions.

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          Most cited references 80

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          Cleavage of structural proteins during the assembly of the head of bacteriophage T4.

           U K Laemmli (1970)
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            Current views on scorpion toxins specific for K+-channels.

            Much of our knowledge on K+-channels was elucidated using specific peptide ligands isolated from a number of venomous organisms. Recently, this field received a strong support and increased interest due to the solution of the three-dimensional structure of a couple of K+-channels. At the same time, several new subfamilies of specific toxins for K+-channels were isolated from scorpion venoms, enhancing the availability and diversity of such useful molecular tools. It opened new lines of research for the better understanding of K+-channel biophysics and pharmacology. In this review, we listed 120 amino acid sequences of peptides isolated from scorpion venoms. They were demonstrated or assumed to be specific for K+-channels. These sequences were aligned and used to generate a rooted phylogenetic tree. The evolutionary tree indicates that several clusters of divergent peptides show preference for specific subtypes of channels. The three-dimensional structures of representative examples of these peptides were drawn and analysed concerning the molecular fitness of their interactions with the channel targets. Four different interacting modes were identified to exist between scorpion toxins and the various subtypes of K+-channels. Copyright 2004 Elsevier Ltd.
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              Overview of scorpion toxins specific for Na+ channels and related peptides: biodiversity, structure-function relationships and evolution.

              Scorpion venoms contain a large number of bioactive components. Several of the long-chain peptides were shown to be responsible for neurotoxic effects, due to their ability to recognize Na(+) channels and to cause impairment of channel functions. Here, we revisited the basic paradigms in the study of these peptides in the light of recent data concerning their structure-function relationships, their functional divergence and extant biodiversity. The reviewed topics include: the criteria for classification of long-chain peptides according to their function, and a revision of the state-of-the-art knowledge concerning the surface areas of contact of these peptides with known Na(+) channels. Additionally, we compiled a comprehensive list encompassing 191 different amino acid sequences from long-chain peptides purified from scorpion venoms. With this dataset, a phylogenetic tree was constructed and discussed taking into consideration their documented functional divergence. A critical view on problems associated with the study of these scorpion peptides is presented, drawing special attention to the points that need revision and to the subjects under intensive research at this moment, regarding scorpion toxins specific for Na(+) channels and the other related long-chain peptides recently described.
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                Author and article information

                Contributors
                Journal
                J Venom Anim Toxins Incl Trop Dis
                J Venom Anim Toxins Incl Trop Dis
                The Journal of Venomous Animals and Toxins Including Tropical Diseases
                BioMed Central
                1678-9199
                2013
                20 May 2013
                : 19
                : 13
                Affiliations
                [1 ]Center for Mountain Development, Ministry of Science, Technology and Environment, Limonar de Monte Roux, El Salvador Guantánamo, Cuba
                [2 ]Department of Molecular Medicine and Bioprocesses, Biotechnology Institute, National Autonomous University of Mexico, Cuernavaca, Mexico
                [3 ]Department of Biochemistry, School of Biology, University of Havana, Havana, Cuba
                [4 ]Center of Marine Research, University of Havana, Havana, Cuba
                Article
                1678-9199-19-13
                10.1186/1678-9199-19-13
                3710086
                23849540
                Copyright © 2013 Rodríguez-Ravelo et al.; licensee BioMed Central Ltd.

                This is an Open Access article distributed under the terms of the Creative Commons Attribution License ( http://creativecommons.org/licenses/by/2.0), which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited.

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                Research

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