Role of carbohydrate as an antigenic determinant of a glycoprotein from rye-grass (Lolium perenne) pollen.
Journal: 1982/March - Biochemical Journal
ISSN: 0264-6021
PUBMED: 6173038
Abstract:
The carbohydrate component of Glycoprotein 2 (12% carbohydrate) from rye-grass (Lolium perenne) pollen has saccharide sequences that contribute to its antigenicity. Radioimmunoassay inhibition tests show that the antiserum to this glycoprotein cross-reacts with a number of other plant glycoproteins. In contrast, antiserum to another glycoprotein from rye-grass pollen, Glycoprotein 1 (5% carbohydrate), does not cross-react with any of the test glycoconjugates. Treatment of glycoproteins with sodium metaperiodate (0.02 M, 4 degree C, 6 h, in the dark) causes the loss of their ability to cross-react antigenically with Glycoprotein 2, and a loss of capacity to bind 125I-labelled concanavalin A. The cross-reactivity of this plant glycoprotein with other glycoconjugates imposes limitations on the interpretation of ultrastructural studies aimed at localizing a particular glycoprotein to a cellular site by using fluorescent or ferritin-labelled antisera. A radioimmunoassay inhibition technique for quantitative determination of the amounts of antigens in plants is also described.
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Biochem J 197(3): 707-714

Role of carbohydrate as an antigenic determinant of a glycoprotein from rye-grass (Lolium perenne) pollen.

Abstract

The carbohydrate component of Glycoprotein 2 (12% carbohydrate) from rye-grass (Lolium perenne) pollen has saccharide sequences that contribute to its antigenicity. Radioimmunoassay inhibition tests show that the antiserum to this glycoprotein cross-reacts with a number of other plant glycoproteins. In contrast, antiserum to another glycoprotein from rye-grass pollen, Glycoprotein 1 (5% carbohydrate), does not cross-react with any of the test glycoconjugates. Treatment of glycoproteins with sodium metaperiodate (0.02 M, 4 degree C, 6 h, in the dark) causes the loss of their ability to cross-react antigenically with Glycoprotein 2, and a loss of capacity to bind 125I-labelled concanavalin A. The cross-reactivity of this plant glycoprotein with other glycoconjugates imposes limitations on the interpretation of ultrastructural studies aimed at localizing a particular glycoprotein to a cellular site by using fluorescent or ferritin-labelled antisera. A radioimmunoassay inhibition technique for quantitative determination of the amounts of antigens in plants is also described.

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Selected References

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  • Basha SM, Beevers L. Glycoprotein Metabolism in the Cotyledons of Pisum sativum during Development and Germination. Plant Physiol. 1976 Jan;57(1):93–97.[PMC free article] [PubMed] [Google Scholar]
  • Christner JE, Caterson B, Baker JR. Immunological determinants of proteoglycans. Antibodies against the unsaturated oligosaccharide products of chondroitinase ABC-digested cartilage proteoglycans. J Biol Chem. 1980 Aug 10;255(15):7102–7105. [PubMed] [Google Scholar]
  • Clarke J, Shannon LM. The isolation and characterization of the glycopeptides from horseradish peroxidase isoenzyme C. Biochim Biophys Acta. 1976 Apr 14;427(2):428–442. [PubMed] [Google Scholar]
  • Geoghegan KF, Dallas JL, Feeney RE. Periodate inactivation of ovotransferrin and human serum transferrin. J Biol Chem. 1980 Dec 10;255(23):11429–11434. [PubMed] [Google Scholar]
  • Gleeson PA, Clarke AE. Structural studies on the major component of Gladiolus style mucilage, an arabinogalactan-protein. Biochem J. 1979 Sep 1;181(3):607–621.[PMC free article] [PubMed] [Google Scholar]
  • Gleeson PA, Clarke AE. Antigenic determinants of a plant proteoglycan, the Gladiolus style arabinogalactan-protein. Biochem J. 1980 Nov 1;191(2):437–447.[PMC free article] [PubMed] [Google Scholar]
  • GOA J. A micro biuret method for protein determination; determination of total protein in cerebrospinal fluid. Scand J Clin Lab Invest. 1953;5(3):218–222. [PubMed] [Google Scholar]
  • Howlett BJ, Clarke AE. Isolation and partial characterization of two antigenic glycoproteins from rye-grass (Lolium perenne) pollen. Biochem J. 1981 Sep 1;197(3):695–706.[PMC free article] [PubMed] [Google Scholar]
  • Ishihara H, Takahashi N, Oguri S, Tejima S. Complete structure of the carbohydrate moiety of stem bromelain. An application of the almond glycopeptidase for structural studies of glycopeptides. J Biol Chem. 1979 Nov 10;254(21):10715–10719. [PubMed] [Google Scholar]
  • Kabat EA. The nature of an antigenic determinant. J Immunol. 1966 Jul;97(1):1–11. [PubMed] [Google Scholar]
  • Kieda CM, Bowles DJ, Ravid A, Sharon N. Lectins in lymphocyte membranes. FEBS Lett. 1978 Oct 15;94(2):391–396. [PubMed] [Google Scholar]
  • Lloyd KO, Kabat EA, Layug EJ, Gruezo F. Immunochemical studies on blood groups. XXXIV. Structures of some oligosaccharides produced by alkaline degradation of blood group A, B, and H substances. Biochemistry. 1966 May;5(5):1489–1501. [PubMed] [Google Scholar]
  • Pueppke SG, Bauer WD. Role of Lectins in Plant-Microorganism Interactions: II. Distribution of Soybean Lectin in Tissues of Glycine max (L.) Merr. Plant Physiol. 1978 May;61(5):779–784.[PMC free article] [PubMed] [Google Scholar]
  • Romani M, Vidali G, Tahourdin CS, Bustin M. Solid phase radioimmunoassay for chromosomal components. J Biol Chem. 1980 Jan 25;255(2):468–474. [PubMed] [Google Scholar]
  • Simeral LS, Kapmeyer W, MacConnell WP, Kaplan NO. On the role of the covalent carbohydrate in the action of ricin. J Biol Chem. 1980 Dec 10;255(23):11098–11101. [PubMed] [Google Scholar]
  • Talbot CF, Etzler ME. Development and Distribution of Dolichos biflorus Lectin as Measured by Radioimmunoassay. Plant Physiol. 1978 May;61(5):847–850.[PMC free article] [PubMed] [Google Scholar]
Abstract
The carbohydrate component of Glycoprotein 2 (12% carbohydrate) from rye-grass (Lolium perenne) pollen has saccharide sequences that contribute to its antigenicity. Radioimmunoassay inhibition tests show that the antiserum to this glycoprotein cross-reacts with a number of other plant glycoproteins. In contrast, antiserum to another glycoprotein from rye-grass pollen, Glycoprotein 1 (5% carbohydrate), does not cross-react with any of the test glycoconjugates. Treatment of glycoproteins with sodium metaperiodate (0.02 M, 4 degree C, 6 h, in the dark) causes the loss of their ability to cross-react antigenically with Glycoprotein 2, and a loss of capacity to bind 125I-labelled concanavalin A. The cross-reactivity of this plant glycoprotein with other glycoconjugates imposes limitations on the interpretation of ultrastructural studies aimed at localizing a particular glycoprotein to a cellular site by using fluorescent or ferritin-labelled antisera. A radioimmunoassay inhibition technique for quantitative determination of the amounts of antigens in plants is also described.
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