Abstract
The direct double-antibody enzymelinked immunosorbent assay system was used in the detection and measurement of seed lectins from peanut (Arachis hypogaea L.) and soybean (Glycine max L.) plants (PSL and SBL, respectively) that had been inoculated with their respective rhizobia. Concentrations of PSL dropped to undetectable levels in peanut roots at 9 d and stems and leaves at 27 d after planting; SBL could no longer be detected in soybean roots at 9 d and in stems and leaves at 12 d. A lectin antigenically similar to PSL was first detected in root nodules of peanuts at 21 d reaching a maximum of 8 μg/g at 29 d then decreasing to 2.5 μg/g at 60 d. There was no evidence of a corresponding lectin in soybean nodules.
Sugar haemagglutination inhibition tests with neuraminidase-treated human blood cells established that PSL and the peanut nodule lectin were both galactose/lactose-specific. Further tests with rabbit blood cells demonstrated a second mannosespecific lectin in peanut nodule extracts that was not detected in root extracts of four-week-old inoculated plants or six-week-old uninoculated plants, although six-week-old root extracts from inoculated plants showed weak lectin activity. The root extracts from both nodulated and uninoculated plants contained another peanut lectin that agglutinated rabbit but not human blood cells. Haemagglutination by this lectin was, however, not inhibited by simple sugars but a glycoprotein, asialothyroglobulin, was effective in this respect.
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Abbreviations
- DAS:
-
double antibody sandwich
- ELISA:
-
enzyme-linked immunosorbent assay
- PBS:
-
phosphate-buffered saline
- PSL:
-
peanut seed lectin
- SBL:
-
soybean lectin
References
Bauer, W.D. (1980) Role of soybean lectin in the soybean-Rhizobium japonicum symbiosis. In: Nitrogen Fixation, Vol II. Symbiotic association and cyanobacteria, pp. 205–214. Newton, W.E., Orme-Johnson, W.H., eds. University Park Press, Baltimore
Borrebaeck, C.A.K., Mattiasson, B. (1983) Distribution of a lectin in tissues of Phaseolus vulgaris. Physiol. Plant. 58, 29–32
Borrebaeck, C.A.K., (1984) Detection and characterization of a lectin from non-seed tissue of Phaseolus vulgaris. Planta 161, 223–228
Bowles, D.J., Lis, H., Sharon, N. (1979) Distribution of lectins in membranes of soybean and peanut plants. 1. General distribution in root, shoot and leaf tissue at different stages of growth. Planta 145, 193–198
Clark, M.F., Adams, A.N. (1977) Characteristics of the microplate method of enzyme-linked immunosorbent assay for the detection of plant viruses. J. Gen. Virol. 34, 475–483
Diaz, C.L., Lems-van Kan, P., van der Schaal, I.A.M., Kijnne, J.W. (1984) Determination of pea (Pisum sativum L.) root lectin using an enzyme-linked immunoassay. Planta 161, 302–307
Etzler, M.E. (1986) Distribution and function of plant lectins. In: The lectins. pp. 371–435, Liener, I.E., Sharon, N., Goldstein, I.J., eds. Academic Press, New York
Hewitt, E.J. (1966) Sand and water culture methods used in the study of plant nutrition 2nd edn. Commonwealth Agricultural Bureau, Farnham Royal, England
Kabat, E.A. (1956) Blood group substances: Their chemistry and immunochemistry. Academic Press, New York
Law, I.J., Strijdom, B.W. (1984) Role of lectins in the specific recognition of Rhizobium by Lotononis bainesii. Plant Physiol. 74, 779–785
Law, I.J., Haylett, T., Strijdom, B.W. (1988) Differences in properties of peanut seed lectin and purified mannose and galactose-binding lectins from nodules of peanut. Planta 176, 19–27
Lotan, R., Skutelsky, E., Danon, D., Sharon, N. (1975) The purification, composition and specificity of the anti-T lectin from peanut (Arachis hypogaea). J. Biol. Chem. 250, 8518–8523
Pueppke, S.G. (1979) Distribution of lectins in the Jumbo Virginia and Spanish varieties of the peanut, Arachis hypogaea L. Plant Physiol. 64, 575–580
Pueppke, S.G., Bauer, W.D., Keegstra, K., Ferguson, A.L. (1978) Role of lectins in plant-microorganism interactions. II. Distribution of soybean lectin in tissues of Glycine Max (L.) Merr. Plant Physiol. 61, 779–784
Pueppke, S.G., Freund, T.G., Schultz, B.C., Friedman, H.P. (1980) Interaction of lectins from soybean and peanut with rhizobia that nodulate soybean, peanut or both plants. Can. J. Microbiol. 26, 1489–1497
Rutherford, W.M., Dick, W.E., Cavins, J.F., Dombrink-Kurtzmann, M.A., Slodki, M.E. (1986) Isolation and characterization of a soybean lectin having 4-O-methylglucuronic acid specificity. Biochemistry 25, 952–958
Stacey, G., Paau, A.S., Brill, W.J. (1980) Host recognition in the Rhizobium-soybean symbiosis. Plant Physiol 66, 609–614
Vance, C.P. (1983) Rhizobium infection and nodulation: A beneficial plant disease? Annu. Rev. Microbiol 37, 399–424
Vincent, J.M. (1970) A manual for the practical study of rootnodule bacteria. Blackwell Scientific Publications, Oxford
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Kishinevsky, B.D., Law, I.J. & Strijdom, B.W. Detection of lectins in nodulated peanut and soybean plants. Planta 176, 10–18 (1988). https://doi.org/10.1007/BF00392474
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DOI: https://doi.org/10.1007/BF00392474