Purification, Elicitor Activity, and Cell Wall Localization of a Glycoprotein from Phytophthora parasitica var. nicotianae, a Fungal Pathogen of Tobacco.

Abstract:

:ABSTRACT A glycoprotein of 34 kDa (GP 34) was solubilized at acidic pH from the mycelium of Phytophthora parasitica var. nicotianae and was purified by ion exchange and gel permeation chromatography. Whole tobacco plants treated with GP 34 through their roots showed an enhanced lipoxygenase activity as well as hydroxyproline-rich glycoprotein accumulation, indicating that this molecule had elicitor properties. An antiserum raised against the pure glycoprotein allowed localization of GP 34 by immunogold-labeling on the cell surface of the mycelium when the fungus was grown in vitro. In the wall-less zoospores, GP 34 was limited to the flagellum surface. It was then abundantly synthesized at the onset of encystment. During infection of tobacco plants, labeling was very faint at early stages of colonization, particularly in the susceptible host cultivar. It appeared earlier in the resistant host cultivar and was restricted to the living fungus, declining with mycelium cell death.

journal_name

Phytopathology

journal_title

Phytopathology

authors

Séjalon-Delmas N,Mateos FV,Bottin A,Rickauer M,Dargent R,Esquerré-Tugayé MT

doi

10.1094/PHYTO.1997.87.9.899

subject

Has Abstract

pub_date

1997-09-01 00:00:00

pages

899-909

issue

9

eissn

0031-949X

issn

1943-7684

journal_volume

87

pub_type

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