Expression of cDNA for a bark lectin of <i>Robinia</i> in transgenic tobacco plants

Tazaki, Kiyoshi; Yoshida, Kazumasa; Shinohara, Kenji; Koshiba, Tomokazu; Yamamoto, Naoki

doi:10.1016/0014-5793(95)01254-0

“…As lectins have insecticidal properties, their genes are currently being used for plant trans-formation. The pea and bark lectins have been successfully expressed into tobacco plants (Tazaki et al, 1995, de Pater et al, 1996 and this expression caused a reduction of insect biomass correlated to a reduction of leaf damage (Boulter et al, 1990). The snowdrop lectin has also been expressed in different plants such as tobacco or rice where it protects against several insects, the moth, Lacanobia oleracea, the aphid, Myzus persicae, or the rice brown planthopper, respectively (Gatehouse et al, 1997;Rao et al, 1998;Zhou et al, 1998).…”

Section: Introductionmentioning

confidence: 99%

Modulation of a lectin insecticidal activity by carbohydrates

Triguéros

¹

,

Wang

²

,

Père

³

et al. 2000

Arch. Insect Biochem. Physiol.

View full text Add to dashboard Cite

Lectins from plants present an insecticidal activity most probably through their carbohydrate binding properties; as a consequence, their toxicity should vary with the presence of a competitive sugar in the ingested food. In order to test this hypothesis, we performed competition experiments between insecticidal activity and carbohydrate binding. For this purpose, we used a lectin from Lathyrus ochrus and the specific carbohydrate for this protein, glucose. In toxicological tests with Drosophila melanogaster, we observed a decrease of lectin toxicity when glucose was added to the larva-rearing medium. This result suggests that the toxicity of the lectin is correlated to its ability to bind sugar in the insect digestive tract and stresses the importance of sugar composition of the nutriment used for toxicological testing of lectins or in genetically modified plants.

show abstract

“…The pea and bark lectins have been successfully expressed into tobacco plants (Tazaki et al, 1995, de Pater et al, 1996 and this expression caused a reduction of insect biomass correlated to a reduction of leaf damage (Boulter et al, 1990). The pea and bark lectins have been successfully expressed into tobacco plants (Tazaki et al, 1995, de Pater et al, 1996 and this expression caused a reduction of insect biomass correlated to a reduction of leaf damage (Boulter et al, 1990).…”

Section: Introductionmentioning

confidence: 99%

Modulation of a lectin insecticidal activity by carbohydrates

Triguéros

¹

,

Wang

²

,

Père

³

et al. 2000

Arch. Insect Biochem. Physiol.

1

0

View full text Add to dashboard Cite

Lectins from plants present an insecticidal activity most probably through their carbohydrate binding properties; as a consequence, their toxicity should vary with the presence of a competitive sugar in the ingested food. In order to test this hypothesis, we performed competition experiments between insecticidal activity and carbohydrate binding. For this purpose, we used a lectin from Lathyrus ochrus and the specific carbohydrate for this protein, glucose. In toxicological tests with Drosophila melanogaster, we observed a decrease of lectin toxicity when glucose was added to the larva-rearing medium. This result suggests that the toxicity of the lectin is correlated to its ability to bind sugar in the insect digestive tract and stresses the importance of sugar composition of the nutriment used for toxicological testing of lectins or in genetically modified plants.

show abstract

“…In addition, evidence was presented that suggests the formation of protein oligomers. The final yield was 1 mg of lectin per 50 g of fresh leaves [ 2 ].…”

Section: Production Of Recombinant Lectinsmentioning

confidence: 99%

“…Lectins are proteins that include at least one non-catalytic domain with the ability of binding in a reversible and specific way to carbohydrates that are free or bound to cell membranes, such as glycoproteins, glycolipids or polysaccharides [ 1 , 2 , 3 ]. The recognition of these carbohydrates is highly specific and allows these proteins to differentially bind to certain molecules and cells [ 4 , 5 ].…”

Section: Introductionmentioning

confidence: 99%

Expression of Lectins in Heterologous Systems

Martínez-Alarcón¹,

Blanco‐Labra²,

García-Gasca

³

2018

IJMS

View full text Add to dashboard Cite

Lectins are proteins that have the ability to recognize and bind in a reversible and specific way to free carbohydrates or glycoconjugates of cell membranes. For these reasons, they have been extensively used in a wide range of industrial and pharmacological applications. Currently, there is great interest in their production on a large scale. Unfortunately, conventional techniques do not provide the appropriate platform for this purpose and therefore, the heterologous production of lectins in different organisms has become the preferred method in many cases. Such systems have the advantage of providing better yields as well as more homogeneous and better-defined properties for the resultant products. However, an inappropriate choice of the expression system can cause important structural alterations that have repercussions on their biological activity since the specificity may lay in their post-translational processing, which depends largely on the producing organism. The present review aims to examine the most representative studies in the area, exposing the four most frequently used systems (bacteria, yeasts, plants and animal cells), with the intention of providing the necessary information to determine the strategy to follow in each case as well as their respective advantages and disadvantages.

show abstract

Expression of cDNA for a bark lectin of Robinia in transgenic tobacco plants

Cited by 8 publications

References 33 publications

Modulation of a lectin insecticidal activity by carbohydrates

Modulation of a lectin insecticidal activity by carbohydrates

Modulation of a lectin insecticidal activity by carbohydrates

Expression of Lectins in Heterologous Systems

Contact Info

Product

Resources

About