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Plant Physiology 57:766-774 (1976)
© 1976 American Society of Plant Biologists

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Articles

Host-Pathogen Interactions

XI. Composition and Structure of Wall-released Elicitor Fractions 1

Arthur R. Ayers2, Barbara Valent, Jürgen Ebel3 and Peter Albersheim4

a Department of Molecular, Cellular and Developmental Biology and Department of Chemistry, University of Colorado, Boulder, Colorado 80302

The structures of the four wall-released elicitor fractions isolated from the Phytophthora megasperma var. sojae mycelial walls have been examined. The results demonstrate that fraction I is primarily composed of a branched {beta}-1,3-glucan, similar in structure to the extracellular elicitors described previously (Ayers, A., J. Ebel, F. Finelli, N. Burger, and P. Albersheim. 1976. Plant Physiol. 57: 751-759). Fractions II and IV are primarily composed of a highly branched mannan-containing glycoprotein, with fraction IV richer in protein than fraction II. Fraction III contains, attached to protein, a mixture of the two polysaccharide types found in fraction I and in fractions II and IV. The structural data presented here, in concert with the biological data presented in the previous two papers (Ayers et al. 1976. Plant Physiol. 57: 751-759; 760-765), demonstrate that the only compound produced by P. megasperma var. sojae which contains elicitor activity is the glucan. Evidence is presented that the terminal glycosyl residues of the glucan are required for elicitor activity. In addition, it is demonstrated that 90% of the glucan can be removed enzymically without any loss of biological activity. The active residue of the enzymic digestion is a highly branched 3- and 3,6-linked glucan containing about 4% mannosyl residues. The results presented suggest that the mannosyl residues of the glucan, which represent only about 1% of the undegraded glucan, are likely to participate in the active site of this molecule. The role of elicitors and phytoalexins in host-pathogen interactions is discussed. Evidence for the existence of and possible identity of another factor, which determines race specificity of host-pathogen interactions, is summarized.


2 Present address: Swedish Forest Products Research Laboratory, Box 5604, S-114 86, Stockholm, Sweden.

3 Present address: Biologie II der Universität, D-78 Freiburg, West Germany.

4 To whom reprint requests should be addressed at the Department of Chemistry.

1 Research was supported by the Energy Research and Development Administration E(11-1)-1426, the Herman Frasch Foundation, New York City, a University of Colorado Faculty Fellowship to P. A., and a Deutsche Forschungsgemeinschaft Fellowship to J. E.




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