Structure and Function of Leguminosae Lectins

Driessche, Edilbert Van

doi:10.1007/978-3-662-11057-7_3

Cited by 38 publications

(20 citation statements)

References 228 publications

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“…As judged from its location (the tips of emerging and growing root hairs), the cross-reactive material possibly represented trifoliin A, the white clover root lectin (Dazzo et al, 1978;Truchet et al, 1986). If so, cross-reactivity could be explained by the extensive homology at the DNA and amino acid levels and by the similarity (Van Driessche, 1988;Sharon and Lis, 1990;Shaanan et al, 1991;Rini et al, 1993). It should be noted, however, that white clover (root) lectin has not yet been characterized in detail and still awaits its assignment to the family of legume lectins.…”

Section: Cross-reactive Proteins Hinder the Demonstration Of Psl On Rmentioning

confidence: 99%

Sugar-Binding Activity of Pea Lectin Expressed in White Clover Hairy Roots

et al. 1995

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Dénarié et al., 1992). Nodulation is regulated by a two-way exchange of plant and bacterial signal molecules (Fisher and Long, 1992;Spaink et al., 1993). Signal exchange begins in the rhizosphere. Rhizobia sense flavonoids secreted by seeds and by the host plant root, which activate the constitutively expressed nodD gene product (reviewed by Schlaman et al., 1992). This step is a determinant of host plant specificity in some Rhizobium-host plant combinations (Horvath et al., 1987; Spaink et al., 1987). Transcription of structural nod genes is under the control of NodD and results in production and secretion of specific lipochitin oligosaccharides (Nod factors), which act as host plant-specific inducers of nodule morphogenesis (reviewed by Dénarié and Cullimore, 1993;Spaink et al., 1993). Most probably, Nod factors constitute the primary determinants of host-plant specificity of nodulation.Root lectins are plant factors involved in nodulation. Lectins are nonenzymatic sugar-binding (g1yco)proteins characterized by sugar-binding specificity. For example, root PSL is Glc/Man specific (Díaz et al., 1990) and white clover root lectin is 2-deoxyglucose specific (Sherwood et al., 1984). In general, the interaction between RI uiciae and white clover does not proceed beyond root hair curling, and these bacteria are not able to penetrate host plant cells by infection thread formation (Yao and Vincent, 1969;Djordjevic et al., 1986;Huang et al., 1993). However, RI viciae is able to induce infection thread formation and nodulation in a significant percentage of white clover plants with roots transformed with the psl gene, as reported by Díaz et al. (1989Díaz et al. ( , 1995. This heterologous nodulation does not take place when a psl mutant, which encodes a non-sugar-binding protein, is used for transformation of white clover roots (Van Eijsden et al., 1992. These results strongly suggest that (a) PSL is functionally expressed in transgenic white clover roots, (b) conservation of the sugar-binding activity of PSL is necessary for infection of white clover by RI viciae, and (c) root lectin helps to break a host plant-specific barrier for nodulation. The relationship between Nod factor recognition by host plants and Rhizobium recognition by host lectin is not yet clear.PSL is an ellipsoidal, nonglycosylated dimeric lectin with two sugar-binding sites, each located near the top of two identical monomers (Einspahr et al., 1988). PSL is encoded by a single gene (Gatehouse et al., 1987;Kaminski et al., 1987) and is synthesized as a single translation product, a prolectin with a molecular mass of 28 kD. Posttranslational modifications result in a protein that dissociates into two p subunits (18 kD each) and two 01 subunits (6 kD each, Higgins et al., 1983)

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Section: Cross-reactive Proteins Hinder the Demonstration Of Psl On Rmentioning

confidence: 99%

Sugar-Binding Activity of Pea Lectin Expressed in White Clover Hairy Roots

et al. 1995

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“…the lectins from Artocarpus integrifolia seeds (Sankaranarayanan et al, 1996) and Calystogia sepium rhizomes (Van Damme, Barre, Verhaert, Roug6 & Peumans, 1996) appear to form a fifth family. Examples from three of these families: the chitinbinding cereal and grass lectins (Raikhel, Lee & Broekaert, 1993), the legume lectins (Van Driessche, 1988;Sharon & Lis, 1990) and the type II ribosome-inactivating proteins (Barbieri, Batelli & Stirpe, 1993) have been extensively characterized over the last 25 years. More recently the fourth well defined family, the monocot mannose-specific lectins from the bulbs, corms, rhizomes and tubers of perennial plants, have been studied in some detail with respect to their biochemical properties, carbohydrate-binding specificity and chemical structure (Cammue, Peeters & Peumans, 1986;Van Damme, Allen & Peumans, 1987;Kaku, Goldstein & Oscarson, 1991;Kaku & Goldstein, 1992;Van Damme, Smeets & Peumans, 1995).…”

Section: Introductionmentioning

confidence: 99%

Crystallization and preliminary structural studies of Scilla campanulata lectin complexed with α1–6 mannobiose

Wright

Wood

Reynolds

et al. 1998

Acta Crystallogr D Biol Cryst

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Recent work has shown that Scilla campanulata agglutinin from bluebell bulbs has a strong affinity for oe(1,3)-and ot(1,6)-linked mannosyl residues and possesses moderate antiretroviral activity. This lectin has been crystallized by the hanging-drop method of vapour diffusion complexed with the disaccharide mannose-crl,6-D-mannose. The crystals are in the space group P21212 with unit-cell dimensions a = 70.63, b = 92.79 and c = 47.25 A, and with a dimer in the asymmetric unit. The crystals diffract X-rays to beyond 1.5 A resolution at 277 K and are stable in an X-ray beam. Data to 1.6 A resolution have been collected using a MAR image-plate system at a synchrotron source and the structure of the complex has been solved by the molecular replacement method.

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“…PSL is encoded by a small gene family, of which only one gene (Psl) appears to be functional (Gatehouse et al, 1987). This gene is strongly expressed in developing seeds (Van Driessche, 1988). There is also weak expression of Psl in roots, and some lectin is secreted into the rhizosphere.…”

mentioning

confidence: 99%

Immunolocalization of PsNLEC-1, a Lectin-Like Glycoprotein Expressed in Developing Pea Nodules

1997

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The pea (Pisum sativum) nodule lectin gene PsNlecl is a member of the legume lectin gene family that is strongly expressed in infected pea nodule tissue. A full-length cDNA sequence of PsNlecl was expressed in Escherichia coli and a specific antiserum was generated from the purified protein. lmmunoblotting of material from isolated symbiosomes revealed that the glycoprotein was present in two antigenic isoforms, PsNLEC-IA and PsNLEC-1 B. The N-terminal sequence of isoform A showed homology to an eightamino acid propeptide sequence previously identified from the cDNA sequence of isoform B. In nodule homogenates the antiserum recognized an additional fast-migrating band, PsNLEC-1 C. Fractionation studies indicated that PsNLEC-1 C was associated with a 100,OOOg nodule membrane fraction, suggesting an association with cytoplasmic membrane or vesicles. lmmunogold localization in pea nodule tissue sections demonstrated that the PsNLEC-1 antigen was present in the symbiosome compartment and also in the vacuole but revealed differences in distribution between infected host cells in different parts of the nodule. These data suggest that PsNLEC-1 is subject to posttranslational modification and that the various antigenic isoforms can be used to monitor membrane and vesicle targeting during symbiosome development.

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Structure and Function of Leguminosae Lectins

Cited by 38 publications

References 228 publications

Sugar-Binding Activity of Pea Lectin Expressed in White Clover Hairy Roots

Sugar-Binding Activity of Pea Lectin Expressed in White Clover Hairy Roots

Crystallization and preliminary structural studies of Scilla campanulata lectin complexed with α1–6 mannobiose

Immunolocalization of PsNLEC-1, a Lectin-Like Glycoprotein Expressed in Developing Pea Nodules

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