Immunogold localization of THRGP-like epitopes in the haustorial interface of obligate,biotrophic fungi on monocots |
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Authors: | Hippe-Sanwald S Marticke K H Kieliszewski M J Somerville S C |
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Institution: | (1) Botanisches Institut, Christian-Albrechts-Universität zu Kiel, Kiel;(2) DOE Plant Research, Laboratory Michigan State University, East Lansing, Michigan;(3) Department of Botany and Plant Pathology, Michigan State University, East Lansing, Michigan;(4) Department of Plant Biology, Carnegie Institution of Washington, 290 Panama Street, 94305-1297 Stanford, CA, USA;(5) Present address: Complex Carbohydrate Research Center, University of Georgia, Athens, Georgia, USA |
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Abstract: | Summary Immunoelectron microscopy was used to determine the subcellular distribution of threonine-hydroxyproline-rich glycoprotein (THRGP) epitopes in host-parasite interactions between obligate, biotrophic fungi and cereals. Infection sites of stem rust (Puccinia graminis f. sp.tritici) and leaf rust (Puccinia recondita) on primary leaves of wheat (Triticum aestivum), as well as of powdery mildew (Erysiphe graminis f. sp.hordei) on coleoptiles of barley (Hordeum vulgare), wete probed with a polyclonal antiserum to maize THRGP. A few immunogold particles were found over the cell walls of wheat mesophyll tissue and barley coleoptile epidermis. Unlike previous examples in dicot plants, no enhanced accumulation of THRGP was observed in cereal cell walls adjacent to sites of pathogen ingress. Instead, the most pronounced accumulation of THRGP-like molecules occurred over the extrahaustorial matrix in both incompatible and compatible plant-pathogen interactions. For powdery mildew of barley, immunogold staining was distinctly increased over the center of the penetration sites; however, no labeling was found over papillae that formed during incompatible and compatible interactions. In addition, no cross-reactivity of the anti-THRGP antiserum with intercellularly growing rust pathogens was observed. The highly localized deposition of THRGP-like molecules in the extrahaustorial matrix suggests that the host plant establishes a modified barrier between itself and the pathogen.Abbreviations C
chloroplast
- EC
plant epidermal cell
- EM
extrahaustorial membrane
- EMA
extrahaustorial matrix
- GO
Golgi body
- GRP
glycine-rich protein
- HP
high pressure
- HRGP
hydroxyprolinerich glycoprotein
- Hyp
hydroxyproline
- LT
low temperature
- PBS
phosphate-buffered saline
- PBST
PBS with Tween-20
- THRGP
threonine-hydroxyproline-rich glycoprotein
- VA
vesicular arbuscular |
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Keywords: | Blumeria graminis Extensin Extracellular protein Haustorium High pressure/low temperature freezing Plant-pathogen interaction |
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