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      Assessment of the Antimicrobial Activity and the Entomocidal Potential of Bacillus thuringiensis Isolates from Algeria

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          Abstract

          This work represents the first initiative to analyze the distribution of B. thuringiensis in Algeria and to evaluate the biological potential of the isolates. A total of 157 isolates were recovered, with at least one isolate in 94.4% of the samples. The highest Bt index was found in samples from rhizospheric soil (0.48) and from the Mediterranean area (0.44). Most isolates showed antifungal activity (98.5%), in contrast to the few that had antibacterial activity (29.9%). A high genetic diversity was made evident by the finding of many different crystal shapes and various combinations of shapes within a single isolate (in 58.4% of the isolates). Also, over 50% of the isolates harbored cry1, cry2, or cry9 genes, and 69.3% contained a vip3 gene. A good correlation between the presence of chitinase genes and antifungal activity was observed. More than half of the isolates with a broad spectrum of antifungal activity harbored both endochitinase and exochitinase genes. Interestingly, 15 isolates contained the two chitinase genes and all of the above cry family genes, with some of them harboring a vip3 gene as well. The combination of this large number of genes coding for entomopathogenic proteins suggests a putative wide range of entomotoxic activity.

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          Bacillus lipopeptides: versatile weapons for plant disease biocontrol.

          In the context of biocontrol of plant diseases, the three families of Bacillus lipopeptides - surfactins, iturins and fengycins were at first mostly studied for their antagonistic activity for a wide range of potential phytopathogens, including bacteria, fungi and oomycetes. Recent investigations have shed light on the fact that these lipopeptides can also influence the ecological fitness of the producing strain in terms of root colonization (and thereby persistence in the rhizosphere) and also have a key role in the beneficial interaction of Bacillus species with plants by stimulating host defence mechanisms. The different structural traits and physico-chemical properties of these effective surface- and membrane-active amphiphilic biomolecules explain their involvement in most of the mechanisms developed by bacteria for the biocontrol of different plant pathogens.
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            Bacillus thuringiensis and its pesticidal crystal proteins.

            During the past decade the pesticidal bacterium Bacillus thuringiensis has been the subject of intensive research. These efforts have yielded considerable data about the complex relationships between the structure, mechanism of action, and genetics of the organism's pesticidal crystal proteins, and a coherent picture of these relationships is beginning to emerge. Other studies have focused on the ecological role of the B. thuringiensis crystal proteins, their performance in agricultural and other natural settings, and the evolution of resistance mechanisms in target pests. Armed with this knowledge base and with the tools of modern biotechnology, researchers are now reporting promising results in engineering more-useful toxins and formulations, in creating transgenic plants that express pesticidal activity, and in constructing integrated management strategies to insure that these products are utilized with maximum efficiency and benefit.
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              Bacillus thuringiensis: A story of a successful bioinsecticide.

              Bacillus thuringiensis (Bt) bacteria are insect pathogens that rely on insecticidal pore forming proteins known as Cry and Cyt toxins to kill their insect larval hosts. At least four different non-structurally related families of proteins form the Cry toxin group of toxins. The expression of certain Cry toxins in transgenic crops has contributed to an efficient control of insect pests resulting in a significant reduction in chemical insecticide use. The mode of action of the three domain Cry toxin family involves sequential interaction of these toxins with several insect midgut proteins facilitating the formation of a pre-pore oligomer structure and subsequent membrane insertion that leads to the killing of midgut insect cells by osmotic shock. In this manuscript we review recent progress in understanding the mode of action of this family of proteins in lepidopteran, dipteran and coleopteran insects. Interestingly, similar Cry-binding proteins have been identified in the three insect orders, as cadherin, aminopeptidase-N and alkaline phosphatase suggesting a conserved mode of action. Also, recent data on insect responses to Cry toxin attack is discussed. Finally, we review the different Bt based products, including transgenic crops, that are currently used in agriculture. Copyright © 2011 Elsevier Ltd. All rights reserved.
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                Author and article information

                Contributors
                Role: Academic Editor
                Journal
                Toxins (Basel)
                Toxins (Basel)
                toxins
                Toxins
                MDPI
                2072-6651
                13 April 2017
                April 2017
                : 9
                : 4
                : 139
                Affiliations
                [1 ]Microbiology Group, Laboratory of Cellular and Molecular Biology, Faculty of Biological Sciences, University of Science and Technology Houari Boumediene (USTHB), BP 32, EL ALIA, Bab Ezzouar, 16111 Algiers, Algeria; zad@ 123456uv.es (Z.D.); fnateche@ 123456yahoo.fr (F.N.); mer.amziane@ 123456gmail.com (M.A.); fifiel07@ 123456yahoo.fr (F.E.-A.); hassibakhorf@ 123456gmail.com (H.K.)
                [2 ]ERI BIOTECMED and Department of Genetics, Universitat de València, Dr. Moliner, 50, BURJASSOT, 46100 Valencia, Spain; joaquin.gomis@ 123456uv.es
                [3 ]Department of Science and Technology, Faculty of Science, University Dr Yahia Frès, 26000 Médéa, Algeria
                Author notes
                [* ]Correspondence: juan.ferre@ 123456uv.es ; Tel.: +34-96-354-4506
                Article
                toxins-09-00139
                10.3390/toxins9040139
                5408213
                28406460
                14be877a-139f-4a55-b3fe-72f439efd8a3
                © 2017 by the authors.

                Licensee MDPI, Basel, Switzerland. This article is an open access article distributed under the terms and conditions of the Creative Commons Attribution (CC BY) license ( http://creativecommons.org/licenses/by/4.0/).

                History
                : 14 March 2017
                : 11 April 2017
                Categories
                Article

                Molecular medicine
                b. thuringiensis,antibacterial,antifungal,cry,vip3,chitinase,biocontrol
                Molecular medicine
                b. thuringiensis, antibacterial, antifungal, cry, vip3, chitinase, biocontrol

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