Lipids of brush border membrane vesicles (BBMV) from Plutella xylostella resistant and susceptible to Cry1Ac δ-endotoxin of Bacillus thuringiensis

Kumaraswami, N. Selvamuthu; Maruyama, Takeshi; Kurabe, Sakiko; Kishimoto, Tadashi; Mitsui, Toshiaki; Hori, Hidetaka

doi:10.1016/s1096-4959(01)00327-x

Cited by 26 publications

(23 citation statements)

References 39 publications

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“…Significantly, Cry14A has been reported to be toxic to coleopteran insects (23), suggesting that insects could use the same receptor. In addition, some insect resistance to Cry toxin has been has been correlated with changes in complex carbohydrate structures (24,25). Along with the striking conservation of the bre-3-bre-5 pathway with the egh-brn pathway in insects, these observations suggest our results may be relevant to Cry toxin resistance in insects as well.…”

Section: Bre-3 Encodes the C Elegans Homologue Of Drosophila Eggheadsupporting

confidence: 57%

Resistance to a Bacterial Toxin Is Mediated by Removal of a Conserved Glycosylation Pathway Required for Toxin-Host Interactions

Griffitts

Huffman

Whitacre

et al. 2003

Journal of Biological Chemistry

122

104

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Crystal (Cry) proteins made by the bacterium Bacillus thuringiensis are pore-forming toxins that specifically target insects and nematodes and are used around the world to kill insect pests. To better understand how pore-forming toxins interact with their host, we have screened for Caenorhabditis elegans mutants that resist Cry protein intoxication. We find that Cry toxin resistance involves the loss of two glycosyltransferase genes, bre-2 and bre-4. These glycosyltransferases function in the intestine to confer susceptibility to toxin. Furthermore, they are required for the interaction of active toxin with intestinal cells, suggesting they make an oligosaccharide receptor for toxin. Similarly, the bre-3 resistance gene is also required for toxin interaction with intestinal cells. Cloning of the bre-3 gene indicates it is the C. elegans homologue of the Drosophila egghead (egh) gene. This identification is striking given that the previously identified bre-5 has homology to Drosophila brainiac (brn) and that egh-brn likely function as consecutive glycosyltransferases in Drosophila epithelial cells. We find that, like in Drosophila, bre-3 and bre-5 act in a single pathway in C. elegans. bre-2 and bre-4 are also part of this pathway, thereby extending it. Consistent with its homology to brn, we demonstrate that C. elegans bre-5 rescues the Drosophila brn mutant and that BRE-5 encodes the dominant UDP-GlcNAc:Man GlcNAc transferase activity in C. elegans. Resistance to Cry toxins has uncovered a four component glycosylation pathway that is functionally conserved between nematodes and insects and that provides the basis of the dominant mechanism of resistance in C. elegans.

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Section: Bre-3 Encodes the C Elegans Homologue Of Drosophila Eggheadsupporting

confidence: 57%

Resistance to a Bacterial Toxin Is Mediated by Removal of a Conserved Glycosylation Pathway Required for Toxin-Host Interactions

Griffitts

Huffman

Whitacre

et al. 2003

Journal of Biological Chemistry

122

104

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“…Since esterases had previously been implicated in Bt resistance mechanisms [12] it was reasonable to speculate that this observation could indicate an esterase-mediated mechanism, although as with the above examples other explanations -such as an indirect effect of altering the host's physiology -could exist. As well as proteases and esterases, lipids have also been implicated in Bt-resistance [13]. In this study differences were found in the lipid composition of Brush Border Membrane Vesicles between a resistant and susceptible population which the authors speculated could influence the activity of the toxin, despite the fact that no causal link was determined.…”

Section: Alternative Resistance Mechanisms and The Casual Vs Causal Pmentioning

confidence: 75%

Bacillus thuringiensis resistance in Plutella — too many trees?

Crickmore

2016

Current Opinion in Insect Science

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“…Recently, our laboratory reported that Cry1Ac-resistant P. xylostella, which was not killed by Cry1Ac, had half the amount of neutral glycolipids compared to susceptible insects (Kumaraswami et al, 2001). Furthermore, we found that the sugar portion of oligosaccharylceramide seemed to stop elongation during pentasaccharide synthesis in resistant strains.…”

Section: Introductionmentioning

confidence: 76%

“…Midgut was prepared from the last instars of P. xylostella, which were susceptible and resistant to Cry1Ac (Kumaraswami et al, 2001). Midguts were homogenized with a Polytron homogenizer (DIAX-900; Heidolph Instruments, Schwabach, Germany) at 11,000 rpm for 4 min at 2-min intervals to cool down to 4°C in 50 mM Hepes-NaOH, pH 7.4, containing the same volume of Protease Inhibitor Cocktail for general use (Sigma-Aldrich, St. Louis, MO, USA), 0.02 mM CDP-choline, 2 mM ATP, 0.2 mM BAL and 0.02 mM galactonolactone.…”

Section: Methodsmentioning

confidence: 99%

“…5). Kumaraswami et al (2001) and Griffitts et al (2005) suggested that Cry toxin-resistant P. xylostella and C. elegans had an abnormal oligosaccharide structure and sugar transferase activity, respectively. In Cry1Ac-resistant PXR, the oligosaccharylceramide content of BBM was almost half that of PXS, and the length of the oligosaccharide was significantly shorter in the PXR oligomer compared to PXS.…”

Section: Analysis Of Radioactive Sugar Lipid By Tlcmentioning

confidence: 99%

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Incorporation of UDP-Galactose and UDP-GalNAc into midgut tissue of Plutella xylostella (Lepidoptera: Yponomeutidae), which are susceptible and highly resistant to Bacillus thuringiensis Cry1Ac

Tomimoto

Katagiri

Higuchi

et al. 2007

Appl. Entomol. Zool.

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Midguts from Plutella xylostella, which are susceptible (PXS) and highly resistant (PXR) to Bacillus thuringiensis Cry1Ac, were homogenized and reacted with UDP-6-3 H-galactose (Gal) or UDP-6-3 H-N-acetylgalactosamine (GalNAc) in a bid to find a resistance mechanism. Gal was incorporated into both chloroform/methanol (C/M) soluble and insoluble fractions but GalNAc was incorporated into only the C/M insoluble fraction. PXS demonstrated a significantly higher level of incorporation; in particular, GalNAc was incorporated into the C/M insoluble fraction 1.5 times more in PXS than in PXR. The incorporation of Gal and GalNAc was enhanced with Mn 2ϩ 2-and 4-fold, respectively. The tissue homogenate was fractionated after the incorporation of sugars and the cytosol fraction rich in microsome (Micro/Cyto) had the highest radioactivity. Although the incorporation of these two sugars was higher in PXS, the level of incorporation was at best 2-fold higher. Mutation in fundamental steps of oligosaccharide synthesis must be lethal, thus, the mutation must be strictly limited to that bringing the different sugar residue(s) to the outer region of the oligosaccharide. This must be the reason why the lower sugar transferase activity in PXR could not explain the substantially higher resistance in PXR. We briefly discuss the mechanism of resistance in P. xylostella against Cry1Ac.

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Lipids of brush border membrane vesicles (BBMV) from Plutella xylostella resistant and susceptible to Cry1Ac δ-endotoxin of Bacillus thuringiensis

Cited by 26 publications

References 39 publications

Resistance to a Bacterial Toxin Is Mediated by Removal of a Conserved Glycosylation Pathway Required for Toxin-Host Interactions

Resistance to a Bacterial Toxin Is Mediated by Removal of a Conserved Glycosylation Pathway Required for Toxin-Host Interactions

Bacillus thuringiensis resistance in Plutella — too many trees?

Incorporation of UDP-Galactose and UDP-GalNAc into midgut tissue of Plutella xylostella (Lepidoptera: Yponomeutidae), which are susceptible and highly resistant to Bacillus thuringiensis Cry1Ac

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