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A novel structural effector from rust fungi is capable of fibril formation
Author(s) -
Kemen Eric,
Kemen Ariane,
Ehlers Andreas,
Voegele Ralf,
Mendgen Kurt
Publication year - 2013
Publication title -
the plant journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 3.058
H-Index - 269
eISSN - 1365-313X
pISSN - 0960-7412
DOI - 10.1111/tpj.12237
Subject(s) - haustorium , biology , effector , cytoplasm , rust (programming language) , microbiology and biotechnology , virulence , protein filament , obligate , host (biology) , botany , biochemistry , gene , genetics , computer science , programming language
Summary It has been reported that filament‐forming surface proteins such as hydrophobins are important virulence determinants in fungi and are secreted during pathogenesis. Such proteins have not yet been identified in obligate biotrophic pathogens such as rust fungi. Rust transferred protein 1 ( RTP 1p), a rust protein that is transferred into the host cytoplasm, accumulates around the haustorial complex. To investigate RTP 1p structure and function, we used immunocytological, biochemical and computational approaches. We found that RTP 1p accumulates in protuberances of the extra‐haustorial matrix, a compartment that surrounds the haustorium and is separated from the plant cytoplasm by a modified host plasma membrane. Our analyses show that RTP 1p is capable of forming filamentous structures in vitro and in vivo . We present evidence that filament formation is due to β–aggregation similar to what has been observed for amyloid‐like proteins. Our findings reveal that RTP 1p is a member of a new class of structural effectors. We hypothesize that RTP 1p is transferred into the host to stabilize the host cell and protect the haustorium from degradation in later stages of the interaction. Thus, we provide evidence for transfer of an amyloid‐like protein into the host cell, which has potential for the development of new resistance mechanisms against rust fungi.