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  • 1
    Electronic Resource
    Electronic Resource
    Recognition of muramic acid and N-acetylmuramic acid by Leguminosae lectins: possible role in plant-bacteria interactions (1992)
    Oxford, UK : Blackwell Publishing Ltd
    FEMS microbiology letters 92 (1992), S. 0 
    Details
    ISSN: 1574-6968
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Biology
    Notes: Abstract Interaction of 24 different seed lectins/ isolectins from the Leguminosae with muramic acid (MurAc), N-acetylmuramic acid (MurNAc) and muramyl-dipeptides (MDP), was studied by hapten-inhibition of haemagglutination. Although many lectins were shown to interact, irrespective of their monosaccharide-specificity or systematic position, glucose/mannose-specific lectins from the tribe Vicieae exhibited the best affinity for these components of the bacterial cell wall. The discrepancies observed in the binding of the muramyl-dipeptide diastereo-isomers to lectins suggest that the binding is somewhat conformation-dependent. These interactions could be possibly involved in the recognition of bacteria by plants.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1574-6968.1992.tb05232.x
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  • 2
    Electronic Resource
    Electronic Resource
    Identification of the sugars involved in mycobacterial cell aggregation (1996)
    Oxford, UK : Blackwell Publishing Ltd
    FEMS microbiology letters 144 (1996), S. 0 
    Details
    ISSN: 1574-6968
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Biology
    Notes: Abstract Incubation of Mycobacterium tuberculosis and M. smegmatis cells with the sugar components of their surface-exposed glycans demonstrated that d-arabinose, but not α-d-glucose or d-mannose, led to the dispersion of the large clumps formed by the bacilli in stationary liquid cultures. These results confirm the presence of arabinose-containing glycans on the mycobacterial cell surface and demonstrate the implication of selective sugars in cell aggregation, suggesting that the clumping of mycobacterial cells is probably mediated by lectin-carbohydrate interactions.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1574-6968.1996.tb08525.x
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  • 3
    Electronic Resource
    Electronic Resource
    Isolation and characterization of a jacalin-related mannose-binding lectin from salt-stressed rice (Oryza sativa) plants (2000)
    Springer
    Planta 210 (2000), S. 970-978 
    Details
    ISSN: 1432-2048
    Keywords: Key words: Jacalin – Lectin –Oryza (salt stress) – Salt stress – Stress protein
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract. A novel plant lectin was isolated from salt-stressed rice (Oryzasativa L.) plants and partially characterized. The lectin occurs as a natural mixture of two closely related isoforms consisting of two identical non-covalently linked subunits of 15 kDa. Both isoforms are best inhibited by mannose and exhibit potent mitogenic activity towards T-lymphocytes. Biochemical analyses and sequence comparisons further revealed that the rice lectins belong to the subgroup of mannose-binding jacalin-related lectins. In addition, it could be demonstrated that the lectins described here correspond to the protein products of previously described salt-stress-induced genes. Our results not only identify the rice lectin as a stress protein but also highlight the possible importance of protein-carbohydrate interactions in stress responses in plants.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/s004250050705
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  • 4
    Electronic Resource
    Electronic Resource
    Purification and structural analysis of an abundant thaumatin-like protein from ripe banana fruit (2000)
    Springer
    Planta 211 (2000), S. 791-799 
    Details
    ISSN: 1432-2048
    Keywords: Key words: Fruit (protein) –Musa (banana, plantain) – Pathogenesis-related protein – Protein structure – Thaumatin-like protein
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract.  The pulp of ripe bananas (Musa acuminata) contains an abundant thaumatin-like protein (TLP). Characterization of the protein and molecular cloning of the corresponding gene from banana demonstrated that the native protein consists of a single polypeptide chain of 200 amino acid residues. Molecular modelling further revealed that the banana thaumatin-like protein (Ban-TLP) adopts an overall fold similar to that of thaumatin and thaumatin-like PR-5 proteins. Although the banana protein exhibits an electrostatically polarized surface, which is believed to be essential for the antifungal properties of TLPs, it is apparently devoid of antifungal activity towards pathogenic fungi. It exhibits a low but detectable in vitro endo-β-1,3-glucanase (EC 3.2.1.x) activity. As well as being present in fruits, Ban-TLP also occurs in root tips where its accumulation is enhanced by methyl jasmonate treatment of plants. Pulp of plantains (Musa acuminata) also contains a very similar TLP, which is even more abundant than its banana homologue. Our results demonstrate for the first time that fruit-specific (abundant) TLPs are not confined to dicots but occur also in fruits of monocot species. The possible role of the apparent widespread accumulation of fruit-specific TLPs is discussed.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/s004250000354
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  • 5
    Electronic Resource
    Electronic Resource
    Fruit-specific lectins from banana and plantain (2000)
    Springer
    Planta 211 (2000), S. 546-554 
    Details
    ISSN: 1432-2048
    Keywords: Key words: Fruit lectins – Jacalin – Lectin – Mannose –Musa– Plantain
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract.  One of the predominant proteins in the pulp of ripe bananas (Musa acuminata L.) and plantains (Musa spp.) has been identified as a lectin. The banana and plantain agglutinins (called BanLec and PlanLec, respectively) were purified in reasonable quantities using a novel isolation procedure, which prevented adsorption of the lectins onto insoluble endogenous polysaccharides. Both BanLec and PlanLec are dimeric proteins composed of two identical subunits of 15 kDa. They readily agglutinate rabbit erythrocytes and exhibit specificity towards mannose. Molecular cloning revealed that BanLec has sequence similarity to previously described lectins of the family of jacalin-related lectins, and according to molecular modelling studies has the same overall fold and three-dimensional structure. The identification of BanLec and PlanLec demonstrates the occurrence of jacalin-related lectins in monocot species, suggesting that these lectins are more widespread among higher plants than is actually believed. The banana and plantain lectins are also the first documented examples of jacalin-related lectins, which are abundantly present in the pulp of mature fruits but are apparently absent from other tissues. However, after treatment of intact plants with methyl jasmonate, BanLec is also clearly induced in leaves. The banana lectin is a powerful murine T-cell mitogen. The relevance of the mitogenicity of the banana lectin is discussed in terms of both the physiological role of the lectin and the impact on food safety.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/s004250000307
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  • 6
    Electronic Resource
    Electronic Resource
    A plant-seed inhibitor of two classes of α-amylases: X-ray analysis of Tenebrio molitor larvae α-amylase in complex with the bean Phaseolus vulgaris inhibitor (1999)
    Copenhagen : International Union of Crystallography (IUCr)
    Acta crystallographica 55 (1999), S. 360-362 
    Details
    ISSN: 1399-0047
    Source: Crystallography Journals Online : IUCR Backfile Archive 1948-2001
    Topics: Chemistry and Pharmacology , Geosciences , Physics
    Notes: The α-amylase from Tenebrio molitor larvae (TMA) has been crystallized in complex with the α-amylase inhibitor (α-AI) from the bean Phaseolus vulgaris. A molecular-replacement solution of the structure was obtained using the refined pig pancreatic α-amylase (PPA) and α-AI atomic coordinates as starting models. The structural analysis showed that although TMA has the typical structure common to α-amylases, large deviations from the mammalian α-amylase models occur in the loops. Despite these differences in the interacting loops, the bean inhibitor is still able to inhibit both the insect and mammalian α-amylase.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1107/S0907444998010701
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  • 7
    Electronic Resource
    Electronic Resource
    Characterization of the Arabidopsis lecRK-a genes: members of a superfamily encoding putative receptors with an extracellular domain homologous to legume lectins (1999)
    Springer
    Plant molecular biology 39 (1999), S. 671-682 
    Details
    ISSN: 1573-5028
    Keywords: Arabidopsis ; genome ; kinase ; lectin ; receptor
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract An Arabidopsis cDNA clone that defines a new class of plant serine/threonine receptor kinases was found to be a member of a family of four clustered genes (lecRK-a1–a4) which have been cloned, sequenced and mapped on chromosome 3. This family belongs to a large superfamily encoding putative receptors with an extracellular domain homologous to legume lectins and appears to be conserved at least among dicots. In the Columbia ecotype only the lecRK-a1 and perhaps the lecRK-a3 gene is functional, since lecRK-a2 is disrupted by a Ty-copia retroelement and lecRK-a4 contains a frameshift mutation. Structural analysis of the lecRK-a1 and lecRK-a3 deduced amino-acid sequences suggests that the lectin domain is unlikely to be involved in binding monosaccharides but could interact with complex glycans and/or with hydrophobic ligands. Immunodetection of lecRK gene products in plasma membranes purified by free-flow electrophoresis showed that the lecRK-a proteins are probably highly glycosylated integral plasma membrane components.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1023/A:1006136701595
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  • 8
    Electronic Resource
    Electronic Resource
    A lectin and a lectin-related protein are the two most prominent proteins in the bark of yellow wood (Cladrastis lutea). (1995)
    Springer
    Plant molecular biology 29 (1995), S. 579-598 
    Details
    ISSN: 1573-5028
    Keywords: bark proteins ; Cladrastis lutea ; cDNA cloning ; lectin ; lectin-related protein ; yellow wood
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract Using a combination of cDNA cloning and protein purification it is demonstrated that bark of yellow wood (Cladrastis lutea) contains two mannose/glucose binding lectins and a lectin-related protein which is devoid of agglutination activity. One of the lectins (CLAI) is the most prominent bark protein. It is built up of four 32 kDa monomers which are post-translationally cleaved into a 15 kDa and a 17 kDa polypeptide. The second lectin (CLAII) is a minor protein, which strongly resembles CLAI except that its monomers are not cleaved into smaller polypeptides. Molecular cloning of the Cladrastis lectin family revealed also the occurrence of a lectin-related protein (CLLRP) which is the second most prominent bark protein. Although CLLRP shows sequence homology to the true lectins, it is devoid of carbohydrate binding activity. Molecular modelling of the three Cladrastis proteins has shown that their three-dimensional structure is strongly related to the three-dimensional models of other legume lectins and, in addition, revealed that the presumed carbohydrate binding site of CLLRP is disrupted by an insertion of three extra amino acids. Since it is demonstrated for the first time that a lectin and a noncarbohydrate binding lectin-related protein are the two most prominent proteins in the bark of a tree, the biological meaning of their simultaneous occurrence is discussed.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00020986
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  • 9
    Electronic Resource
    Electronic Resource
    Molecular cloning of the lectin and a lectin-related protein from common Solomon's seal (Polygonatum multiflorum) (1996)
    Springer
    Plant molecular biology 31 (1996), S. 657-672 
    Details
    ISSN: 1573-5028
    Keywords: cDNA cloning ; lectin ; lectin-related protein ; Polygonatum multiflorum ; Solomon's seal
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract The most prominent protein ofPolygonatum multiflorum (common Solomon's seal) rhizomes has been identified as a mannose-binding lectin. Analysis of the purified lectin demonstrated that it is a tetramer of four identical subunits of 14 kDa. Molecular cloning further revealed that the lectin from this typical Liliaceae species belongs to the superfamily of monocot mannose-binding proteins. Screening of cDNA libraries constructed with RNA isolated from buds, leaves and flowers ofP. multiflorum also yielded cDNA clones encoding a protein, which contains two tandemly arranged domains with an obvious sequence homology to the mannose-binding lectins. Molecular modelling of thePolygonatum lectin and lectin-related protein indicated that the three-dimensional structure of both proteins strongly resembles that of the snowdrop lectin. In addition, this approach suggested that the presumed carbohydrate-binding sites of the lectin can accommodate a mannose residue whereas most of the carbohydratebinding sites of the lectin-related protein cannot.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00042237
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  • 10
    Electronic Resource
    Electronic Resource
    Molecular cloning of the bark and seed lectins from the Japanese pagoda tree (Sophora japonica) (1997)
    Springer
    Plant molecular biology 33 (1997), S. 523-536 
    Details
    ISSN: 1573-5028
    Keywords: bark proteins ; cDNA cloning ; lectin ; Sophora japonica
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract cDNA clones encoding the bark and seed lectins from Sophora japonica were isolated and their sequences analyzed. Screening of a cDNA library constructed from polyA RNA isolated from the bark resulted in the isolation of three different lectin cDNA clones. The first clone encodes the GalNAc-specific bark lectin which was originally described by Hankins et al. whereas the other clones encode the two isoforms of the mannose/glucose-specific lectin reported by Ueno et al.. Molecular cloning of the seed lectin genes revealed that Sophora seeds contain only a GalNAc-specific lectin which is highly homologous to though not identical with the GalNAc-specific lectin from the bark. All lectin polypeptides are translated from mRNAs of ca. 1.3 kb encoding a precursor carrying a signal peptide. In the case of the mannose/glucose-specific bark lectins this precursor is post-translationally processed in two smaller peptides. Alignment of the deduced amino acid sequences of the different clones revealed striking sequence similarities between the mannose/glucose-binding and the GalNAc-specific lectins. Furthermore, there was a high degree of sequence homology with other legume lectins which allowed molecular modelling of the Sophora lectins using the coordinates of the Pisum sativum, Lathyrus ochrus and Erythrina corallodendron lectins.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1023/A:1005781103418
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