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  • 1
    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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  • 2
    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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  • 3
    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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  • 4
    Electronic Resource
    Electronic Resource
    Isolation, characterization and molecular cloning of the mannose-binding lectins from leaves and roots of garlic (Allium sativum L.) (1997)
    Springer
    Plant molecular biology 33 (1997), S. 223-234 
    Details
    ISSN: 1573-5028
    Keywords: Allium ; Garlic ; lectin ; tissue specific expression
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract Two novel lectins were isolated from roots and leaves of garlic. Characterization of the purified proteins indicated that the leaf lectin ASAL is a dimer of two identical subunits of 12 kDa, which closely resembles the leaf lectins from onion, leek and shallot with respect to its molecular structure and agglutination activity. In contrast, the root lectin ASARI, which is a dimer of subunits of 15 kDa, strongly differs from the leaf lectin with respect to its agglutination activity. cDNA cloning of the leaf and root lectins revealed that the deduced amino acid sequences of ASAL and ASARI are virtually identical. Since both lectins have identical N-terminal sequences the larger Mr of the ASARI subunits implies that the root lectin has an extra sequence at its C-terminus. These results not only demonstrate that virtually identical precursor polypeptides are differently processed at their C-terminus in roots and leaves but also indicate that differential processing yields mature lectins with strongly different biological activities. Further screening of the cDNA library for garlic roots also yielded a cDNA clone encoding a protein composed of two tandemly arrayed lectin domains. Since the presumed two-domain root lectin has not been isolated yet, its possible relationship to the previously described two-domain bulb lectin could not be studied at the protein level.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1023/A:1005717020021
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  • 5
    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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  • 6
    Electronic Resource
    Electronic Resource
    The seed lectins of black locust (robinia pseudoacacia) are encoded by two genes which differ from the bark lectin genes (1995)
    Springer
    Plant molecular biology 29 (1995), S. 1197-1210 
    Details
    ISSN: 1573-5028
    Keywords: Black locust ; cDNA cloning ; lectin ; Robinia pseudoacacia
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract Two lectins were isolated from Robinia pseudoacacia (black locust) seeds using affinity chromatography on fetuin-agarose, and ion exchange chromatography on a Neobar CS column. The first lectin, R. pseudoacacia seed agglutinin I, referred to as RPsAI, is a homotetramer of four 34 kDa subunits whereas the second lectin, referred to as RPsAII, is composed of four 29 kDa polypeptides. cDNA clones encoding the polypeptides of RPsAI and RPsAII were isolated and their sequences were determined. Both polypeptides are translated from mRNAs of ca. 1.2 kb encoding a precursor carrying a signal peptide. Alignment of the deduced amino acid sequences of the different clones indicates that the 34 and 29 kDa seed lectin polypeptides show 95% sequence identity. In spite of this striking homology, the 29 kDa polypeptide has only one putative glycosylation site whereas the 34 kDa subunit has four of these sites. Carbohydrate analysis revealed that the 34 kDa possesses three carbohydrate chains whereas the 29 kDa polypeptide is only partially glycosylated at one site. A comparison of the deduced amino acid sequences of the two seed and three bark lectin polypeptides demonstrated unambiguously that they are encoded by different genes. This implies that five different genes are involved in the control of the expression of the lectins in black locust.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00020462
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  • 7
    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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  • 8
    Electronic Resource
    Electronic Resource
    Curculin, a sweet-tasting and taste-modifying protein, is a non-functional mannose-binding lectin (1997)
    Springer
    Plant molecular biology 33 (1997), S. 691-698 
    Details
    ISSN: 1573-5028
    Keywords: sweet proteins ; lectins ; curculin ; molecular modelling ; docking ; epitopes
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract A three-dimensional model of curculin, a sweet-tasting and taste-modifying protein from the fruits of Curculigo latifolia, was built from the X-ray coordinates of GNA, a mannose-binding lectin from snowdrop (Galanthus nivalis). The three mannose-binding sites present in GNA were found in curculin but are devoid of mannose-binding activity as shown by docking experiments performed with mannose. Some regions well exposed on the surface of the three-dimensional model of curculin could act as epitopes responsible for the sweet-tasting properties of this protein.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1023/A:1005704616565
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  • 9
    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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  • 10
    Electronic Resource
    Electronic Resource
    Homology modelling of the core domain of the endogenous lectin comitin: structural basis for its mannose-binding specificity (1999)
    Springer
    Plant molecular biology 39 (1999), S. 969-978 
    Details
    ISSN: 1573-5028
    Keywords: comitin ; mannose-binding specificity ; molecular modelling ; Dictyostelium discoideum
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract The N-terminal core domain of comitin from the slime mold Dictyostelium discoideum has been modelled from the X-ray coordinates of the monocot mannose-binding lectin from snowdrop (Galanthus nivalis). Docking experiments performed on the three-dimensional model showed that two of the three mannose-binding sites of the comitin monomer are functional. They are located at both ends of the comitin dimer whereas the actin-interacting region occurs in the central hinge region where both monomers are non covalently associated. This distribution is fully consistent with the bifunctional character of comitin which is believed to link the Golgi vesicles exhibiting mannosylated membrane glycans to the actin cytoskeleton in the cell.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1023/A:1006133527621
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