7 research outputs found

    new caerin-like antibacterial peptide from the venom gland of the Iranian scorpion Mesobuthus eupeus: cDNA amplification and sequence analysis

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    Scorpion venom consists of different types of peptides and proteins which are encoded by individual genes. A full length cDNA consisting of 238 base pair nucleotides and encoding 74 amino acids peptide was isolated from the venom gland of the Iranian scorpion Mesobuthus eupeus (Buthidae family). This peptide named M. eupeus caerin-like antimicrobial peptide (Me-CLAP) belonging to the group of antibacterial peptide was previously described from scorpion. In this study, sequence of cDNA encoding Me-CLAP from the M. eupeus venom glands was amplified using reverse transcriptase polymerase chain reaction (RT-PCR) and was analyzed afterwards. Me-CLAP has similar molecular characteristics to antimicrobial peptides (AMPs) of same genus like Mesobuthus martensii and M. eupeus and more differences were seen with other genus.Keywords: Caerin-like antimicrobial peptide, Mesobuthus eupeus, semi-nested real-time polymerase chain reaction

    Construction and expression of aspartic protease from Onchocerca volvulus* as ompA fusion protein in a mutant strain of Salmonella typhimurium

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    Two constructions in pHS164 vector were designed to permit expression of OV7A and OV4A inserts encoding the N-terminal and C-terminal portion of an aspartic protease from Onchocerca volvulus, respectively. A novel 39 kD protein ompA-OV7A fusion protein was stably expressed as ompA fusion in a modified strain of Salmonella typhimurium strain SL5000 and E.coli strain JM109. Expression of the fusion protein in bacterial strains harboring the constructs were evaluated by western blotting. E.coli and Salmonella lysates were fractionated by 10% SDS-PAGE gel and then immobilized to nitrocellulose membrane by electroblotting. Primary polyclonal antibody generated in rats against the GST-OV7A fusion protein was used in the Western blots. It remains to be seen whether the fusion protein expressed in vivo will promote effective immune response

    Study of Methicillin resistance in Staphylococcus aureus and species of Coagulase negative Staphylococci isolated from various clinical specimens.

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    Conclusions: The rate of MRCONS was more than MRSA and vancomycin was the most effective antibiotic against those organisms. As such, this antibiotic is the drug of choice for treatment in such cases

    Comparative characterization of two galectins excreted-secreted from intestine-dwelling parasitic versus free-living females of the soil-transmitted nematode Strongyloides

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    Helminths are complex pathogens that ensure their long-term survival by influencing the immune responses of their host. Excretory/secretory products (ESP) can exert immunoregulatory effects which foster parasite survival. Galectins represent a widespread group of β-galactoside-binding proteins which are involved in a multitude of biological processes operative in parasite-host interaction. We had earlier identified seven galectins in Strongyloides ratti, four of them detected in the ESP of distinct developmental stages of the parasite. In the present report, we focused on the characterization of two of them, Sr-galectin-1 (Sr-Gal-1) and Sr-galectin-3 (Sr-Gal-3). While Sr-Gal-3 expression was strongest in parasitic females, Sr-Gal-1 was predominantly expressed in free-living females. Both proteins were cloned and recombinantly expressed in an E. coli expression system. Their glycan-binding activity was verified by haemagglutination and glycan array analysis. Furthermore, primary immunological activities of the Sr-galectins were initially investigated by the application of an in vitro mucosal 3D-culture model, comprising of mucosa-associated epithelial and dendritic cells. The Sr-galectins stimulated preferentially the release of the type 2 cytokines thymic stromal lymphopoietin and IL-22, a first indication for immunoregulatory activity. In addition, the Sr-galectins dose-dependently fostered cell migration. Our results confirm the importance of these carbohydrate-binding proteins in host-parasite-interaction by indicating possible interaction with the host mucosa-associated cells
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