Open AccessHost-Pathogen Interactions
Author(s) -
Eugene A. Nothnagel,
Michael McNeil,
Peter Albersheim,
Anne Dell
Publication year - 1983
Publication title -
plant physiology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 3.554
H-Index - 312
eISSN - 1532-2548
pISSN - 0032-0889
DOI - 10.1104/pp.71.4.916
Subject(s) - elicitor , pectin , phytoalexin , pectinase , cell wall , glycine , chemistry , biochemistry , pectate lyase , molecular mass , pectinesterase , hydrolysate , hydrolysis , chromatography , enzyme , amino acid , resveratrol
Elicitors of phytoalexin accumulation in soybean (Glycine max L. Merr., cv Wayne) cotyledons were released from soybean cell walls and from citrus pectin by partial acid hydrolysis. These two hydrolysates yielded nearly identical distributions of elicitor activity when fractionated on anion-exchange columns. Chromatography of the pectin elicitor on gel filtration and high-pressure anion-exchange columns did not further purify the elicitor. Elicitor activity of the preparation was lost by treatment with either endo-alpha-1,4-polygalacturonase or pectate lyase. Glycosyl residue compositions of the purified elicitors from cell walls and pectin were both found to be approximately 98% galacturonosyl residues. Linkage analysis of the pectin elicitor showed that most, if not all, of the galacturonosyl residues were alpha-1,4-linked. The high-mass molecular ions detected by fast atom bombardment-mass spectrometry of the most active elicitor fractions from cell walls and pectin both corresponded precisely to a molecule composed of 12 galacturonosyl residues. These results suggest that dodeca-alpha-1,4-d-galacturonide is the active elicitor, but the possibility remains that the active component could be a slightly modified oligogalacturonide present, but not detected, in the purified fractions.