Plant Physiol. Drug Metab Dispos
HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS
 QUICK SEARCH:   [advanced]


     


Plant Physiology 59:1104-1110 (1977)
© 1977 American Society of Plant Biologists

This Article
Right arrow Full Text (PDF)
Right arrow Alert me when this article is cited
Right arrow Alert me if a correction is posted
Services
Right arrow Email this article to a friend
Right arrow Similar articles in this journal
Right arrow Similar articles in PubMed
Right arrow Alert me to new issues of the journal
Right arrow Download to citation manager
Right arrow reprints & permissions
Citing Articles
Right arrow Citing Articles via HighWire
Right arrow Citing Articles via CrossRef
Right arrow Citing Articles via Google Scholar
Google Scholar
Right arrow Articles by Ziegler, E.
Right arrow Articles by Albersheim, P.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Ziegler, E.
Right arrow Articles by Albersheim, P.
Agricola
Right arrow Articles by Ziegler, E.
Right arrow Articles by Albersheim, P.
Articles

Host-Pathogen Interactions

XIII. Extracellular Invertases Secreted by Three Races of a Plant Pathogen Are Glycoproteins Which Possess Different Carbohydrate Structures 1

Ernst Ziegler2 and Peter Albersheim3

a Department of Chemistry, University of Colorado, Boulder, Colorado 80309

The invertase present in the culture fluid of races 1, 2, and 3 of Phytophthora megasperma Drechs. var. sojae A. A. Hildebrand (Pms) were purified until they gave but a single band, whether stained for protein or carbohydrate, after isoelectric focusing in flat bed gels. The sugar compositions of multiple preparations of the purified invertases from each race of this fungal pathogen were determined by quantitative gas chromatography of their alditol acetates. The invertases are composed of about 25% carbohydrate. Mannose and glucosamine make up more than 97% of the carbohydrate portions of the invertases of all three Pms races analyzed, but the ratio of mannose to glucosamine is clearly not the same in each race. The glycosyl linkage compositions of the glucosamine-containing mannans of multiple preparations of the Pms invertases were determined by GC-MS analysis of the partially methylated alditol acetate derivatives. The results of these analyses demonstrate clear quantitative differences between the glycosyl components of the different Pms races. The existence of race-specific carbohydrate structures in the differentially virulent Pms races suggests that these carbohydrates may be involved in determining the specificity of hostpathogen interactions.


2 Present address: RWTH-Aachen, Inst. f. Physik. Biol., D-51 Aachen, Kopenikusstr. 16, West Germany.

3 To whom correspondence should be addressed.

1 Supported by a fellowship from the Deutsche Forschungsgemeinschaft to E. Ziegler and by a grant from the Energy Research and Development Administration EY-76-S-02-1426. *A001.




This article has been cited by other articles:


Home page
ScienceHome page
C. J. COOKSEY, P. J. GARRATT, J. S. DAHIYA, and R. N. STRANGE
Sucrose: A Constitutive Elicitor of Phytoalexin Synthesis
Science, June 24, 1983; 220(4604): 1398 - 1400.
[Abstract] [PDF]




HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS
ASPB Publications PLANT PHYSIOLOGY THE PLANT CELL
Copyright © 1977 by the American Society of Plant Biologists