Volume Department of Biology, Johns Hopkins University. Oxford Academic. Google Scholar. Cite Citation. Permissions Icon Permissions. Abstract Fluorometric spectroscopy is a powerful tool for investigating the interaction between a carbohydrate ligand and binding proteins. Issue Section:. You do not currently have access to this article. Download all figures. Sign in. You could not be signed in. Sign In Forgot password?
Don't have an account? Japanese Biochemical Society members Sign in via society site. Sign in via your Institution Sign in. The former being totally ineffective and the two latter being toxic. Recently, Zhu-Salzman and colleagues reported the carbohydrate binding and resistance to proteolysis control insecticidal activity of Griffonia simplicifolia lectin II in order to investigate its toxic activity.
In the case of ConA which does not appear to be toxic to mammals, at least at low levels of dietary inclusion, its gene could be used in an transgenic plant project against C. However, the first lectin reported to possess insecticidal activity was PHA. It was attributed the inability of the cowpea bruchid beetle, C. Nevertheless, many years latter, the toxic effects were more attributed to the isecticidal protein arcelin and to a -amylase inhibitor, two lectin-like proteins occurring in Phaseolus vulgaris seeds exhibiting sequence homology to PHA Mirkov et al.
The PHA protein family seems to be a classical example of a integrated defense system which each protein has a precise role to protect seeds, although undefined yet. Structural studies of arcelin, PHA and a -amylase inhibitor have proved that these proteins share very similar three-dimensional folding but differing in quaternary structure and in their active binding site whose are ready distinct Bompard-Gilles et al. Once, the activity and function do seem to be defined by the combine site-region. Apart of present status of the investigation about the lectins as tools in crop biotechnology, a condition sine qua non for their use is the test to engineered plant for resistance in field.
In this way, some non legume plants have already been used Rao et al.
Carbohydrate–protein interactions and their biosensing applications | SpringerLink
In a view of the understanding of the role of legume lectins under the symbiosis establishment or any other activity, the differences in their active combining site and specificity for carbohydrate should be considered. As shown in Table III the set of amino acid which compose the monosaccharide binding-site of legume lectins present some interesting features. Although the well conserved triad Asp-Asn-Gly support the saccharide in the site, the other residues have been not strongly conserved during evolution. The replacement of amino acid residues is unlikely to have generated different specificities among the lectins as the contribution of these semi-conserved and non conserved residues is made by hydrogen bonds established with the sugars via the CO and NH groups or architecture well conserved Loris et al.
Nevertheless, minor differences may change the affinity of lectins by structurally related ligands. Although the lectins are gifted of at least a monosacharide-binding site, it is reasonable to suppose that their biological ligand are larger than a single monosaccharide. Indeed, lectins not only bind to oligosacchaides, but this interaction is tighter than that to their monosacchaide inhibitor Konami et al. Although the ability to interact with oligosacchaide had been proved early, the first complex of a lectin with a complex glycan was established later by crystallographic studies Bourne et al.
These crystallography works clearly identified the involvement of additional amino acid residues in the vicinity of the monosaccharide-binding site, with the glycans complexes. The hydrogen bounds occurring between the glycans and other amino acid residues also mediated by water are responsible for the correct anchorage of the larger receptor and by the magnitude of the affinity constant determined to be so far strong than to that for monosaccharides. Although the completeness of the complexes between legume lectins and complex glycans is of an extraordinary elegance, of most intrinsic and biological relevance seems to be the ability of lectins possessing different monosaccharide specificity to binding the same receptor, through attachment in different epitope present in the same glycan structure for review see Debray et al.
This very interesting biological event puts under suspect the actual role of the monosacchaide-binding site. According to these results, we could speculate that despite the monosaccharide specificity, legume lectins and probably non legume lectins could display similar roles as they can interact with complex glycans broadly distributed in naure.
In this context, the monosacchaide-binding site would serve essentially to attach the ligand, being the specificity of the interaction defined by different epitope in the structure. Although the available results allow speculations on basis of the molecular structure of legume lectins and their specificity, identification of endogenous receptors remains obscure and up to date, our attempt to identify endogenous receptor on free-lectin fractions from seed lectins of some members of Diocleinae lectins has failed.
Legume plants, are the most rich source of lectins and the continuous investigation of new lectins in members of this group may give new insight on the lectin function in nature.
Although investigations under the physiological role of lectins in plant have received few attention, results from biochemical and structural features and mainly the understanding of the molecular basis of the specificity of new lectins may help the discussion. In fact the legume Dolichos biflorus lectin has recently been successfully crystallized and its complex with adenine solved Hamelryck et al.
It should be expected that a new field to discuss the polyfunctional features of these proteins will be initiated fast, adding new data to the present discussion. Ayouba, A. Rouseau, P. A new dimension of binding specificity. FEBS Letters , 2 : Molecular characterization and crystallization of Diocleinae lectins. Acta Bot.
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