Evolution of plant ribosome-inactivating proteins

This contribution presents an updated analysis of the evolution of ribosome-inactivating proteins (RIPs) in plants. All evidence suggests that an ancestor of modern seed plants developed the RIP domain at least 300 million years ago. This ancestral RIP domain gave rise to a direct lineage of type 1 RIPs (i.e. primary type 1 RIPs) still present today in many monocots and at least one dicot. In a later stage a plant succeeded in fusing the RIP domain to a duplicated ricin-B domain acquired from a bacterium. The resulting ancestral type 2 RIP gave rise to all modern type 2 RIPs and by domain deletion to different lines of ‘secondary’ type 1 RIPs and ricin-B type lectins. In a more recent past at least three other domain fusions took place in the family Poaceae whereby type AC1 (type 3), type AC2 and type AD chimeric forms were generated

Ligand-induced perturbations in Urtica dioica agglutinin

AbstractThe binding of the trisaccharide, N,N′,N″-triacetylchitotriose, to Urtica dioica agglutinin (UDA) was investigated using 1H NMR spectroscopy. UDA is a small antiviral plant lectin containing two homologous 43-amino acid domains. Carbohydrate-induced perturbations occur in one domain of UDA at trisaccharide concentrations below equimolar. Residues in the second domain are shifted at higher carbohydrate concentrations. This data confirms the presence of two binding sites of non-identical affinities per UDA monomer. Qualitative analysis of the 2D NOESY spectra indicates that UDA contains two short stretches of antiparallel β-sheet. The 1H resonance assignments for both antiparallel β-sheet sequences have been completed and there is one β-stretch per domain. A number of these β-sheet residues are perturbed in the presence of carbohydrate

Crystal structure of the GalNAc/Gal-specific agglutinin from the phytopathogenic ascomycete Sclerotinia sclerotiorum reveals novel adaptation of a beta-trefoil domain

International audienceA lectin from the phytopathogenic ascomycete Sclerotinia sclerotiorum that shares only weak sequence similarity with characterized fungal lectins has recently been identified. S. sclerotiorum agglutinin (SSA) is a homodimeric protein consisting of two identical subunits of ∼ 17 kDa and displays specificity primarily towards Gal/GalNAc. Glycan array screening indicates that SSA readily interacts with Gal/GalNAc-bearing glycan chains. The crystal structures of SSA in the ligand-free form and in complex with the Gal-β1,3-GalNAc (T-antigen) disaccharide have been determined at 1.6 and 1.97 Å resolution, respectively. SSA adopts a β-trefoil domain as previously identified for other carbohydrate-binding proteins of the ricin B-like lectin superfamily and accommodates terminal non-reducing galactosyl and N-acetylgalactosaminyl glycans. Unlike other structurally related lectins, SSA contains a single carbohydrate-binding site at site α. SSA reveals a novel dimeric assembly markedly dissimilar to those described earlier for ricin-type lectins. The present structure exemplifies the adaptability of the β-trefoil domain in the evolution of fungal lectins

Isolation and characterization of a second lectin (SNA-II) present in elderberry (Sambucus nigra L.) bark

A second lectin (SNA-II) has been isolated from elderberry (Sambucus nigra L.) bark by affinity chromatography on immobilized asialo-glycophorin. This lectin is a blood group nonspecific glycoprotein containing 7.8% carbohydrate and which is rich in asparagine/aspartic acid, glutamine/glutamic acid, glycine, valine, and leucine. Gel filtration on Superose 12 gave a single symmetrical peak corresponding to Mr, 51,000; SDS-acrylamide electrophoresis gave a single polypeptide, Mr, 30,000. Hence SNA-II appears to be a homodimer. The lectin is a Gal/GalNAc-specific lectin which is precipitated by glycoproteins containing GalNAc-terminated oligosaccharide chains (e.g., asialo-ovine submaxillary and hog gastric mucins), and by glycoproteins and polysaccharides having multiple terminal nonreducing -galactosyl groups as occur in asialoglycophorin, asialo-laminin and Type 14 pneumococcal polysaccharide. The carbohydrate binding specificity of SNA-II was studied by sugar hapten inhibition of the asialo-glycophorin precipitation reaction. The lectin's binding site appears to be most complementary to GalNAc linked [alpha] to the C-2, C-3, or C-6 hydroxyl group of galactose. These disaccharide units are approximately 100 times more potent than melibiose, 60 times more potent than N-acetyllactosamine, and 30 times more potent than lactose. Interestingly, the blood group A-active trisaccharide containing an -fucosyl group linked [alpha]1-2 to galactose was 10-fold poorer as an inhibitor than the parent oligosaccharide (GalNAc[alpha]1-3Gal), suggesting steric hindrance to binding by the [alpha]--fucosyl group; this explains the failure of the lectin to exhibit blood group A specificity.Peer Reviewedhttp://deepblue.lib.umich.edu/bitstream/2027.42/28711/1/0000532.pd

Proteins with an Euonymus lectin-like domain are ubiquitous in Embryophyta

<p>Abstract</p> <p>Background</p> <p>Cloning of the <it>Euonymus </it>lectin led to the discovery of a novel domain that also occurs in some stress-induced plant proteins. The distribution and the diversity of proteins with an <it>Euonymus </it>lectin (EUL) domain were investigated using detailed analysis of sequences in publicly accessible genome and transcriptome databases.</p> <p>Results</p> <p>Comprehensive in silico analyses indicate that the recently identified <it>Euonymus europaeus </it>lectin domain represents a conserved structural unit of a novel family of putative carbohydrate-binding proteins, which will further be referred to as the <it>Euonymus </it>lectin (EUL) family. The EUL domain is widespread among plants. Analysis of retrieved sequences revealed that some sequences consist of a single EUL domain linked to an unrelated N-terminal domain whereas others comprise two in tandem arrayed EUL domains. A new classification system for these lectins is proposed based on the overall domain architecture. Evolutionary relationships among the sequences with EUL domains are discussed.</p> <p>Conclusion</p> <p>The identification of the EUL family provides the first evidence for the occurrence in terrestrial plants of a highly conserved plant specific domain. The widespread distribution of the EUL domain strikingly contrasts the more limited or even narrow distribution of most other lectin domains found in plants. The apparent omnipresence of the EUL domain is indicative for a universal role of this lectin domain in plants. Although there is unambiguous evidence that several EUL domains possess carbohydrate-binding activity further research is required to corroborate the carbohydrate-binding properties of different members of the EUL family.</p

A comparative study of mannose-binding lectins from the amaryllidaceae and alliaceae

A comparative study of the lectins from the families Amaryllidaceae and Alliaceae reveals many common features: all bind-mannose exclusively and have similar molecular structures and amino acid compositions. All these lectins contain subunits of Mr 11 500-14 000 which are not linked by disulphide bonds and occur as dimers (in Allium sativum, A. vineale, A. ursinum, A. moly, Narcissus pseudonarcissus and Clivia miniata) or tetramers (in Galanthus nivalis, Hippeastrum hybrid, Allium cepa and A. porrum. Most of these lectins were shown to occur as complex mixtures of isolectins. In general, the lectin concentration in Amaryllidaceae bulbs is higher than in Alliaceae bulbs. Antisera raised in rabbits against the Galanthus nivalis and the Narcissus cv Carlton lectins gave, upon double immunodiffusion, single precipitation bands and lines of identity with purified lectins from all Amaryllidaceae species, A. cepa and A. porrum. Similar single lines of identity were obtained between purified lectins from other Allium species and Amaryllidaceae lectins when challenged with rabbit anti-daffodil antiserum. However, two immunoprecipitin bands were obtained when the same assay was carried out with antiserum against Galanthus nivalis lectin, one line cross-reacting with the Amaryllidaceae lectins with the formation of a spur. Cross-reactions were also observed between Allium cepa and A. porrum lectins and the lectins from A. moly, A. vineale, A. ursinum and A. sativum. Although all lectins are serologically related, there are differences in their reaction with various antisera.Peer Reviewedhttp://deepblue.lib.umich.edu/bitstream/2027.42/29508/1/0000595.pd

Hevein: an antifungal protein from rubber-tree ( Hevea brasiliensis ) latex

Several chitin-binding proteins were isolated from the “bottom fraction” of Hevea brasiliensis (Müll.) Arg. latex. One of these chitin-binding proteins is hevein, a small monomeric protein which strongly resembles the lectin from stinging nettle ( Urtica dioica L.). Like the latter, hevein showed strong antifungal activity against several fungi in vitro. The possible involvement of this protein in the defense against invasion by potentially pathogenic fungi is discussed.Peer Reviewedhttp://deepblue.lib.umich.edu/bitstream/2027.42/47477/1/425_2004_Article_BF00197797.pd