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. 1971 Aug;68(8):1815–1819. doi: 10.1073/pnas.68.8.1815

Proteins from Plant Cell Walls Inhibit Polygalacturonases Secreted by Plant Pathogens

Peter Albersheim 1, Anne J Anderson 1
PMCID: PMC389299  PMID: 5288769

Abstract

Proteins extracted from the cell walls of Red Kidney bean hypocotyls, tomato stems, and suspension-cultured sycamore cells can completely inhibit the activity of the polygalacturonases (polygalacturonide hydrolases, EC 3.2.1.15) secreted by the fungal plant pathogens Colletotrichum lindemuthianum, Fusarium oxysporum, and Sclerotium rolfsii. The inhibitor of the C. lindemuthianum polygalacturonase, purified 560-fold from bean hypocotyl extracts, is 40 times as effective an inhibitor of the C. lindemuthianum polygalacturonase as of the F. oxysporum polygalacturonase, and does not demonstrably inhibit the S. rolfsii polygalacturonase. A crude hypocotyl extract that completely inhibits the three polygalacturonases does not inhibit C. lindemuthianum-secreted cellulase, xylanase, α-galactosidase, α-arabinofuranosidase, or α-galacturonosidase. The purified bean hypocotyl protein combines with the C. lindemuthianum polygalacturonase to form a complex with a dissociation constant of 2 × 10-9 M or less. The physical properties of these inhibitors are similar to those of phytohemagglutinins and of the plant glycoproteins capable of agglutinating transformed animal cells.

Keywords: host-pathogen interactions, fungi, Colletotrichum lindemuthianum, Fusarium oxysporum, Sclerotium rolfsii, agglutinins

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Selected References

These references are in PubMed. This may not be the complete list of references from this article.

  1. AUB J. C., TIESLAU C., LANKESTER A. REACTIONS OF NORMAL AND TUMOR CELL SURFACES TO ENZYMES. I. WHEAT-GERM LIPASE AND ASSOCIATED MUCOPOLYSACCHARIDES. Proc Natl Acad Sci U S A. 1963 Oct;50:613–619. doi: 10.1073/pnas.50.4.613. [DOI] [PMC free article] [PubMed] [Google Scholar]
  2. Agrawal B. B., Goldstein I. J. Protein-carbohydrate interaction. VI. Isolation of concanavalin A by specific adsorption on cross-linked dextran gels. Biochim Biophys Acta. 1967 Oct 23;147(2):262–271. [PubMed] [Google Scholar]
  3. BOYD W. C. The lectins: their present status. Vox Sang. 1963 Jan-Feb;8:1–32. doi: 10.1111/j.1423-0410.1963.tb04146.x. [DOI] [PubMed] [Google Scholar]
  4. Burger M. M., Goldberg A. R. Identification of a tumor-specific determinant on neoplastic cell surfaces. Proc Natl Acad Sci U S A. 1967 Feb;57(2):359–366. doi: 10.1073/pnas.57.2.359. [DOI] [PMC free article] [PubMed] [Google Scholar]
  5. Dahlgren K., Porath J., Lindahl-Kiessling K. On the purification of phytohemagglutinins from Phaseolus vulgaris seeds. Arch Biochem Biophys. 1970 Apr;137(2):306–314. doi: 10.1016/0003-9861(70)90444-3. [DOI] [PubMed] [Google Scholar]
  6. English P. D., Jurale J. B., Albersheim P. Host-Pathogen Interactions: II. Parameters Affecting Polysaccharide-degrading Enzyme Secretion by Colletotrichum lindemuthianum Grown in Culture. Plant Physiol. 1971 Jan;47(1):1–6. doi: 10.1104/pp.47.1.1. [DOI] [PMC free article] [PubMed] [Google Scholar]
  7. Entlicher G., Kostír J. V., Kocourek J. Studies on phytohemagglutinins. 3. Isolation and characterization of hemagglutinins from the pea (Pisum sativum L.). Biochim Biophys Acta. 1970 Nov 17;221(2):272–281. doi: 10.1016/0005-2795(70)90267-9. [DOI] [PubMed] [Google Scholar]
  8. Frattali V., Steiner R. F. Soybean inhibitors. I. Separation and some properties of three inhibitors from commercial crude soybean trypsin inhibitor. Biochemistry. 1968 Feb;7(2):521–530. doi: 10.1021/bi00842a006. [DOI] [PubMed] [Google Scholar]
  9. Howard I. K., Sage H. J. Isolation and characterization of a phytohemagglutinin from the lentil. Biochemistry. 1969 Jun;8(6):2436–2441. doi: 10.1021/bi00834a028. [DOI] [PubMed] [Google Scholar]
  10. Howard I. K., Sage H. J., Stein M. D., Young N. M., Leon M. A., Dyckes D. F. Studies on a phytohemagglutinin from the lentil. II. Multiple forms of Lens culinaris hemagglutinin. J Biol Chem. 1971 Mar 25;246(6):1590–1595. [PubMed] [Google Scholar]
  11. JAFFE W. G., HANNIG K. FRACTIONATION OF PROTEINS FROM KIDNEY BEANS (PHASEOLUS VULGARIS). Arch Biochem Biophys. 1965 Jan;109:80–91. doi: 10.1016/0003-9861(65)90290-0. [DOI] [PubMed] [Google Scholar]
  12. Kornfeld R., Kornfeld S. The structure of a phytohemagglutinin receptor site from human erythrocytes. J Biol Chem. 1970 May 25;245(10):2536–2545. [PubMed] [Google Scholar]
  13. LOWRY O. H., ROSEBROUGH N. J., FARR A. L., RANDALL R. J. Protein measurement with the Folin phenol reagent. J Biol Chem. 1951 Nov;193(1):265–275. [PubMed] [Google Scholar]
  14. Olson M. O., Liener I. E. Some physical and chemical properties of concanavalin A, the phytohemagglutinin of the jack bean. Biochemistry. 1967 Jan;6(1):105–111. doi: 10.1021/bi00853a018. [DOI] [PubMed] [Google Scholar]
  15. Pressey R. Invertase inhibitors from red beet, sugar beet, and sweet potato roots. Plant Physiol. 1968 Sep;43(9):1430–1434. doi: 10.1104/pp.43.9.1430. [DOI] [PMC free article] [PubMed] [Google Scholar]
  16. RIGAS D. A., OSGOOD E. E. Purification and properties of the phytohemagglutinin of Phaseolus vulgaris. J Biol Chem. 1955 Feb;212(2):607–615. [PubMed] [Google Scholar]
  17. SMOGYI M. Notes on sugar determination. J Biol Chem. 1952 Mar;195(1):19–23. [PubMed] [Google Scholar]
  18. TUNIS M. AGGLUTININS OF THE RED KIDNEY BEAN (PHASEOLUS VULGARIS): A NEW CYTOAGGLUTININ DISTINCT FROM HEMAGGLUTININ. J Immunol. 1964 Jun;92:864–869. [PubMed] [Google Scholar]
  19. Takahashi T., Ramachandramurthy P., Liener I. E. Some physical and chemical properties of a phytohemagglutinin isolated from Phaseolus vulgaris. Biochim Biophys Acta. 1967 Jan 18;133(1):123–133. doi: 10.1016/0005-2795(67)90044-x. [DOI] [PubMed] [Google Scholar]
  20. Tichá M., Entlicher G., Kostír J. V., Kocourek J. Studies on phytohemagglutinins. IV. Isolation and characterization of a hemagglutinin from the lentil, Lens, esculenta, Moench. Biochim Biophys Acta. 1970 Nov 17;221(2):282–289. doi: 10.1016/0005-2795(70)90268-0. [DOI] [PubMed] [Google Scholar]

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