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      A novel bioactive peptide from wasp venom

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          Abstract

          Wasp venoms contain a number of pharmacologically active biomolecules, undertaking a wide range of functions necessary for the wasp's survival. We purified and characterized a novel bioactive peptide (vespin) from the venoms of Vespa magnifica (Smith) wasps with unique primary structure. Its amino acid sequence was determined to be CYQRRVAITAGGLKHRLMSSLIIIIIIRINYLRDNSVIILESSY. It has 44 residues including 15 leucines or isoleucines (32%) in the sequence. Vespin showed contractile activity on isolated ileum smooth muscle. The cDNA encoding vespin precursor was cloned from the cDNA library of the venomous glands. The precursor consists of 67 amino acid residues including the predicted signal peptide and mature vespin. A di-basic enzymatic processing site (-KR-) is located between the signal peptide and the mature peptide. Vespin did not show similarity with any known proteins or peptides by BLAST search, suggesting it is a novel bioactive peptide from wasp venoms.

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          Bee and wasp venoms.

          E Habermann (1972)
          Article 0 comments Cited 57 times – based on 0 reviews     Review now
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            Bee, wasp and ant venomics pave the way for a component-resolved diagnosis of sting allergy.

            Dirk C de Graaf, C Graaf, Maarten Aerts … (2009)
            With the complete sequencing of its genome, the honey bee is now a preferred model organism for Hymenoptera species, also with respect to venomic studies. Major pitfalls in proteomic profiling are: i) highly abundant proteins masking low-copy number proteins; ii) high heterogeneity in proteomes due to isoforms, protease activity and PTMs; iii) the inability for protein function assignment. If genomic information is not available, proteins still might be identified through cross-species protein identifications or MS/MS data-based de novo sequencing techniques. Venomic approaches discovered several new proteins and peptides from honey bees, bumble bees, ants and different wasp species, and some of these constituents were proven to be of immunological significance. Further digging in the proteome/peptidome will yield more so-called "venom trace elements" with only a local function in the venom duct or reservoir or released by leakage of the gland tissue. An impressive list of recombinants venom proteins has become available from a diverse range of Hymenopterans. Protein microarray allows the determination and monitoring of allergic patients' IgE reactivity profiles to disease-causing allergens using single measurements and minute amounts of serum. The information the physician will get from such a single run will largely exceed the output from current IgE capturing tools using whole venom preparations.
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              Interaction of the cyclic antimicrobial cationic peptide bactenecin with the outer and cytoplasmic membrane.

              R. Hancock, Jennifer Wu (1999)
              Bactenecin, a 12-amino acid cationic antimicrobial peptide from bovine neutrophils, has two cysteine residues, which form one disulfide bond, making it a cyclic molecule. To study the importance of the disulfide bond, a linear derivative Bac2S was made and the reduced form (linear bactenecin) was also included in this study. Circular dichroism spectroscopy showed that bactenecin existed as a type I beta-turn structure regardless of its environment, while the reduced form and linear bactenecin adopted different conformations according to the lipophilicity of the environment. Bactenecin was more active against the Gram-negative wild type bacteria Escherichia coli, Pseudomonas aeruginosa, and Salmonella typhimurium than its linear derivative and reduced form, while all three peptides were equally active against the outer membrane barrier-defective mutants of the first two bacteria. Only the two linear peptides showed activity against the Gram-positive bacteria Staphylococcus epidermidis and Enterococcus facaelis. Bactenecin interacted well with the outer membrane and its higher affinity for E. coli UB1005 lipopolysaccharide and improved ability to permeabilize the outer membrane seemed to account for its better antimicrobial activity against Gram-negative bacteria. The interaction of bactenecin with the cytoplasmic membrane was determined by its ability to dissipate the membrane potential by using the fluorescence probe 3, 3-dipropylthiacarbocyanine and an outer membrane barrier-defective mutant E. coli DC2. It was shown that the linear derivative and reduced form were able to dissipate the membrane potential at much lower concentrations than bactenecin despite the similar minimal inhibitory concentrations of all three against this barrier-defective mutant.
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                Author and article information

                Journal
                Journal ID (nlm-ta): J Venom Res
                Journal ID (publisher-id): jvr
                Title: Journal of Venom Research
                Publisher: Library Publishing Media
                ISSN (Electronic): 2044-0324
                Publication date Collection: 2010
                Publication date (Electronic): 30 September 2010
                Volume: 1
                Pages: 43-47
                Affiliations
                [α ]Kunming Institute of Zoology, Chinese Academy of Sciences, Kunming 650223, Yunnan, China
                [β ]Clinical Laboratory, the First Affiliated Hospital of Kunming Medical College, Kunming 650032, Yunnan, Chin
                [γ ]Yunnan Clinical Research Center of Breast Cancer, the Third Affiliated Hospital of Kunming Medical College, Kunming 650032 , Yunnan, China
                Author notes
                [* ]Correspondence to: Ren Lai, Email: rlai@ 123456mail.kiz.ac.cn , Tel: +86 871 5196202, Fax: +86 871 5199086
                Article
                PMC ID: 3086190
                PubMed ID: 21544181
                SO-VID: 427758d2-7b5a-4bf6-9440-f36b9a9ac465
                Copyright © ©The Authors
                License:

                This is an open access article, published under the terms of the Creative Commons Attribution Non-Commercial License ( http://creativecommons.org/licenses/by-nc/2.0/uk/). This license permits non-commercial use, distribution and reproduction of the article, provided the original work is appropriately acknowledged with correct citation details.

                History
                Date received : 09 August 2010
                Date revision received : 01 September 2010
                Date accepted : 03 September 2010
                Categories
                Subject: Research Report

                ScienceOpen disciplines: Medicine
                Keywords: smooth muscle,wasp venom,novel peptide,vespa magnifica,contraction
                Data availability:
                ScienceOpen disciplines: Medicine
                Keywords: smooth muscle, wasp venom, novel peptide, vespa magnifica, contraction

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