Special Issue "Bacillus thuringiensis Toxins"


A special issue of Toxins (ISSN 2072-6651). This special issue belongs to the section "Bacterial Toxins".

Deadline for manuscript submissions: closed (30 April 2014)

Special Issue Editor

Guest Editor
Prof. Dr. Anne-Brit Kolstø
Laboratory for Microbial Dynamics (LaMDa), Department of Pharmaceutical Biosciences, University of Oslo, Blindern, 0316, Oslo, Norway
Website: http://www.mn.uio.no/farmasi/personer/vit/annebko/
E-Mail: a.b.kolsto@farmasi.uio.no
Phone: +47 22 85 6923

Special Issue Information

Dear Colleagues,

Bacillus thuringiensis is the most widely used biopesticide worldwide due to its production of proteinaceous crystal toxins. B. thuringiensis is part of the Bacillus cereus group, and the B. thuringiensis may be very closely related to B. cereus strains. The genes coding for these toxins are usually located on plasmids of varying sizes, ranging from a few kb to several hundred kb. The crystal toxins are most often produced during sporulation, and the toxins are regarded as specific for B. thuringiensis. Like the B. cereus strains, B. thuringiensis have the genes coding for several virulence factors, including enterotoxin genes, and these may well play a role in the pathogenic lifestyle that the B. thuringiensis display against insect larvae hosts. Still the specificity of each B. thuringiensis strain resides in the crystal toxin genes. More than 100 different crystal toxin genes have been identified, in addition to a great number of manipulated and improved toxin genes.

In this Special Issue of B. thuringiensis toxins, we seek new data on all aspects of the crystal toxins and other toxins produced by B. thuringiensis strains.  Both new data on gene regulation and toxin structure and mechanisms will be of interest, as will the importance of the toxins in the physiology of the bacteria and the hosts.

Prof. Dr. Anne-Brit Kolstø
Guest Editor


Manuscripts should be submitted online at www.mdpi.com by registering and logging in to this website. Once you are registered, click here to go to the submission form. Manuscripts can be submitted until the deadline. Papers will be published continuously (as soon as accepted) and will be listed together on the special issue website. Research articles, review articles as well as communications are invited. For planned papers, a title and short abstract (about 100 words) can be sent to the Editorial Office for announcement on this website.

Submitted manuscripts should not have been published previously, nor be under consideration for publication elsewhere (except conference proceedings papers). All manuscripts are refereed through a peer-review process. A guide for authors and other relevant information for submission of manuscripts is available on the Instructions for Authors page. Toxins is an international peer-reviewed Open Access monthly journal published by MDPI.

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  • host specificity of toxins
  • toxin gene regulation
  • modified toxins
  • non-Cry toxins
  • toxin stability
  • function of cry toxins and other toxins
  • resistance
  • toxin structure

Published Papers (12 papers)

by , , , ,  and
Toxins 2014, 6(8), 2453-2470; doi:10.3390/toxins6082453
Received: 23 April 2014; in revised form: 11 August 2014 / Accepted: 11 August 2014 / Published: 19 August 2014
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by , , , , Jr., , ,  and
Toxins 2014, 6(8), 2393-2423; doi:10.3390/toxins6082393
Received: 14 May 2014; in revised form: 23 June 2014 / Accepted: 27 June 2014 / Published: 13 August 2014
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by , ,  and
Toxins 2014, 6(8), 2239-2255; doi:10.3390/toxins6082239
Received: 29 May 2014; in revised form: 10 July 2014 / Accepted: 15 July 2014 / Published: 31 July 2014
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by , , , ,  and
Toxins 2014, 6(8), 2229-2238; doi:10.3390/toxins6082229
Received: 14 April 2014; in revised form: 16 July 2014 / Accepted: 18 July 2014 / Published: 25 July 2014
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by , ,  and
Toxins 2014, 6(7), 2194-2209; doi:10.3390/toxins6072194
Received: 3 June 2014; in revised form: 11 July 2014 / Accepted: 15 July 2014 / Published: 23 July 2014
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by , ,  and
Toxins 2014, 6(7), 2115-2126; doi:10.3390/toxins6072115
Received: 4 May 2014; in revised form: 23 June 2014 / Accepted: 8 July 2014 / Published: 16 July 2014
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by ,  and
Toxins 2014, 6(7), 2050-2063; doi:10.3390/toxins6072050
Received: 14 April 2014; in revised form: 2 June 2014 / Accepted: 27 June 2014 / Published: 14 July 2014
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by , , , , , , , , ,  and
Toxins 2014, 6(6), 1882-1895; doi:10.3390/toxins6061882
Received: 28 April 2014; in revised form: 29 May 2014 / Accepted: 9 June 2014 / Published: 18 June 2014
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by , , , , ,  and
Toxins 2014, 6(5), 1598-1614; doi:10.3390/toxins6051598
Received: 6 February 2014; in revised form: 29 April 2014 / Accepted: 12 May 2014 / Published: 20 May 2014
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by , , ,  and
Toxins 2014, 6(5), 1490-1504; doi:10.3390/toxins6051490
Received: 19 February 2014; in revised form: 21 April 2014 / Accepted: 24 April 2014 / Published: 30 April 2014
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by , , ,  and
Toxins 2014, 6(4), 1274-1294; doi:10.3390/toxins6041274
Received: 11 December 2013; in revised form: 13 March 2014 / Accepted: 26 March 2014 / Published: 3 April 2014
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Toxins 2014, 6(4), 1222-1243; doi:10.3390/toxins6041222
Received: 28 January 2014; in revised form: 10 March 2014 / Accepted: 14 March 2014 / Published: 28 March 2014
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Planned Papers

The below list represents only planned manuscripts. Some of these manuscripts have not been received by the Editorial Office yet. Papers submitted to MDPI journals are subject to peer-review.

Type of Paper: Article
Changes in Gene Expression in the Larval Gut of Ostrinia nubilalis in Response to Bacillus thuringiensis Cry1Ab Protoxin Ingestion
Jianxiu Yao 1,3, Lawrent L. Buschman 1,2, Chitvan Khajuria 1 and Kun Yan Zhu 1,*
1 Department of Entomology, 123 Waters Hall, Kansas State University, Manhattan, KS 66506, USA; E-Mail: kzhu@ksu.edu (K.Y.Z.)
Current Address: 963 Burland Dr., Bailey, CO 80421, USA
Current Address: Department of Entomology, 412 Minnie Belle Heep Building, Taxes A&M University, College Station, TX 77843, USA
bstract: The European corn borer, Ostrinia nubilalis, is the target pest for transgenic corn expressing insecticidal toxins encoded by genes derived from Bacillus thuringiensis (Bt). We developed a cDNA microarray based on 15,000 cDNA elements representing 2,895 unique transcripts derived from the O. nubilalis larval gut. This microarray was used to monitor gene expression in early third-instar larvae of Bt-susceptible O. nubilalis after 6-hr feeding on diet with or without Cry1Ab protoxin. We identified 174 transcripts for which the expression was changed more than 2-fold in the gut of the larvae fed Cry1Ab protoxin (P ≤ 0.05). These transcripts represent 80 down-regulated and 94 up-regulated genes. Among these 174 differentially expressed transcripts, 106 showed BLAST results (e value < 1.0e-3), whereas 68 did not. Thirteen of these transcripts putatively encode proteins that are considered likely to be involved in Bt toxicity, and these transcripts include eight serine proteases, three aminopeptidases, one alkaline phosphatase, and one cadherin. The expressions of trypsin-like protease and three aminopeptidase transcripts were variable (three trypsin proteases and one aminpeptidase were up-regulated and one trypsin and two aminopeptidases was down-regulated), but some encoding three potential Bt-binding proteins, one aminopeptidase, alkaline phosphatase and cadherin, were consistently up-regulated in larvae fed Cry1Ab protoxin. The significantly up and down-regulated transcripts may be involved in Cry1Ab toxicity by activation, degradation, toxin binding and other related cellular responses. This study is the first large-scale survey of Cry1Ab protoxin induced transcriptional responses in O. nubilalis gut tissue and is expected to provide a platform for functional studies of toxin-insect interactions.
Bacillus thuringiensis; European corn borer; Ostrinia nubilalis; Cry1Ab protoxin; microarray; transcriptional response

Type of Paper: Review
Bacillus thuringiensis subsp. israelensis and its Dipteran-Specific Toxins
Eitan Ben-Dov
Department of Life Sciences, Achva Academic College MP Shikmim, 79800, Israel;  E-Mail: etn@bgu.ac.il
Bacillus thuringiensis subsp. israelensis (Bti) is the first subspecies of B. thurengiensis that was found and used as an effective biological control agent against larvae of many mosquito and black fly species. The larvicidity of Bti resides in at least four major crystal pro-toxic proteins, of 134, 128, 72 and 27 kDa, encoded by cry4Aa, cry4Ba, cry11Aa and cyt1Aa respectively, and all mapped on the 128 kb plasmid known as pBtoxis. Despite the low toxicity of Cyt1Aa against exposed larvae, it is highly synergistic with the Cry toxins and their combinations and thus prevents selection of resistance in the targets. Low probability of developing resistance has been observed in field mosquito populations treated for decades with Bti-bioinsecticide.

Type of Paper: Review
Bt Toxin Modification for Enhanced Efficacy.
M.T. Fernandez-Luna, B. Deist, M. Rausch and Bryony C. Bonning
Department of Entomology, Iowa State University, Ames, IA 50011; E-Mail: bbonning@iastate.edu (B.C.B.)
Insect -specific toxins derived from Bacillus thuringiensis (Bt) provide a valuable resource for pest suppression. Here we review the different strategies that have been employed to enhance toxicity against specific target species or to modify the host range of Bt toxins. Toxin optimization provides a useful approach to extend their utility for suppression of pests that only exhibit low susceptibility to Bt toxins, and to overcome field resistance.

Type of Paper: Review
Bacillus thuringiensis Toxins: An Overview of Their Known Biocide Activity
Leopoldo Palma, Delia Muñoz, Colin Berry and Primitivo Caballero
Instituto de Agrobiotecnología, CSIC-Gobierno de Navarra, 31192 Mutilva Baja, Navarra, Spain; E-Mail: pcm92@unavarra.es
Bacillus thuringiensis (Bt) is a Gram positive, spore-forming bacterium that synthesizes parasporal crystalline inclusions containing one or more proteins (Cry and Cyt proteins) (Schnepf et al., 1998), some of which are toxic against a wide range of insects orders (Bravo et al., 2007; MacIntosh et al., 1990; Porcar et al., 2009), and nematodes (Wei et al., 2003). These toxins have been successfully developed as some of the most useful and environmental-friendly bioinsecticides in decades for herbivore insects with chewing mouthparts, such as caterpillars, beetles, and maggots, which ingest the toxins present on the plant surfaces along with their food. However, vast numbers of Bt isolates naturally present in the soil and the phylloplane synthesize Cry proteins whose biological activity is still unknown(Mizuki et al., 2000; Ohba et al., 2009). Bt also synthesizes insecticidal proteins during the vegetative growth phase, which are subsequently secreted into the growth medium. These proteins are commonly known as vegetative insecticidal proteins (Vips) and hold insecticidal activity against lepidopteran (Estruch et al., 1996), coleopteran (Warren et al., 1998) and some homopteran pests (Sattar and Maiti, 2011).  A less characterized secretory protein with no amino acid similarity to previously known Vips, has shown insecticidal activity against coleopteran pests (Donovan et al., 2006) and termed as Sip protein (secreted insecticidal protein). Mtx-like and Bin-like proteins, which share amino acid similarities with mosquitocidal Mtx and Bin toxins, respectively, from Bacillus sphaericus, are also produced by some Bt strains (Berry, 2012; Peña et al., 2006). In summary, Bt insecticidal proteins may be classified into at least five distinct protein groups according to their amino acid identity and protein structure: Bin-like, three-domain Cry toxins, Cyt, Mtx-like, Sip, and Vip proteins (Peña et al., 2006). In addition to the aforementioned toxins, Bt produces some proteins, initially termed as non-insecticidal for their lack of toxicity against lepidopterans, dipterans and coleopterans, with outstanding toxicity against human cancer cells (Ohba et al., 2009), a human-pathogenic protozoan (Kondo et al., 2002) and the Oncomelania snail (Ali et al., 2010). In this review we provide an overview of the known active Bt toxins to date, which strongly suggests the pluripotential nature of the ample repertoire of toxins produced by this bacteria.

Last update: 1 April 2014

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