Literature DB >> 3954742

Cell-cell recognition of host surfaces by pathogens. The adsorption of maize (Zea mays) root mucilage by surfaces of pathogenic fungi.

J Gould, D H Northcote.   

Abstract

The adsorption of radioactive mucilage by pathogenic fungi was shown to be dependent upon time, the composition of mucilage, the type of fungal surface (conidia, hyphae, hyphal apices), fungal species, pH and bivalent cations. All fungal adhesins were inactivated by either proteinase or polysaccharase treatments. Adsorption was not inhibited by the numberous mono-, di- and oligo-saccharides that were tested individually, but it was inhibited absolutely by several polysaccharides. This suggested that adsorption of mucilage by pathogens involved conformational and ionic interactions between plant and fungal polymers but not fungal lectins bound to sugar residues of mucilage. Several fractionation schemes showed that pathogens bound only the most acidic of the variety of polymers that comprise mucilage. There was not any absolute distinction between ability to bind radioactive mucilage and type of pathogen or non-pathogen. However, there were notable differences in characteristics of adsorption between two types of pathogen. Differences were revealed by comparison of the adsorption capacities of conidia and germinant conidia and chromatography of radioactive mucilage on germinant conidia. An ectotrophic root-infecting fungus (a highly specialized pathogen) bound a greater proportion of mucilage than did a vascular-wilt fungus (of catholic host and tissue range) with more than one class of site for adsorption. In contrast with the vascular-wilt fungus, sites for adsorption on the specialized pathogen were present solely on surfaces formed by germination.

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Year:  1986        PMID: 3954742      PMCID: PMC1153040          DOI: 10.1042/bj2330395

Source DB:  PubMed          Journal:  Biochem J        ISSN: 0264-6021            Impact factor:   3.857


  23 in total

1.  Preparation of rat epididymal alpha-L-fucosidase free from other glycosidases: its action on root-cap slime from Zea mays L.

Authors:  K Wright; D H Northcote; R M Davey
Journal:  Carbohydr Res       Date:  1976-03       Impact factor: 2.104

2.  The chemical composition and structure of the yeast cell wall.

Authors:  D H NORTHCOTE; R W HORNE
Journal:  Biochem J       Date:  1952-05       Impact factor: 3.857

3.  Covalent linkage of functional groups, ligands, and proteins to polyacrylamide beads.

Authors:  J K Inman
Journal:  Methods Enzymol       Date:  1974       Impact factor: 1.600

4.  New method for quantitative determination of uronic acids.

Authors:  N Blumenkrantz; G Asboe-Hansen
Journal:  Anal Biochem       Date:  1973-08       Impact factor: 3.365

5.  Preparation of adsorbents for biospecific affinity chromatography. Attachment of group-containing ligands to insoluble polymers by means of bifuctional oxiranes.

Authors:  L Sundberg; J Porath
Journal:  J Chromatogr       Date:  1974-03-13

6.  Leucocyte values of alpha-L-iduronidase activity in mucopolysaccharidosis I.

Authors:  T E Kelly; H A Taylor
Journal:  J Med Genet       Date:  1976-04       Impact factor: 6.318

7.  Structure of the cell wall proteogalactomannan from Neurospora crassa. I. Purification of the proteoheteroglycan and characterization of alkali-labile oligosaccharides.

Authors:  T Nakajima; M Yoshida; N Hiura; K Matsuda
Journal:  J Biochem       Date:  1984-10       Impact factor: 3.387

8.  Development and trifoliin A-binding ability of the capsule of Rhizobium trifolii.

Authors:  J E Sherwood; J M Vasse; F B Dazzo; G L Truchet
Journal:  J Bacteriol       Date:  1984-07       Impact factor: 3.490

9.  APPLE FRUIT PECTIC SUBSTANCES.

Authors:  A J BARRETT; D H NORTHCOTE
Journal:  Biochem J       Date:  1965-03       Impact factor: 3.857

10.  The relationship of root-cap slimes to pectins.

Authors:  K Wright; D H Northcote
Journal:  Biochem J       Date:  1974-06       Impact factor: 3.857

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