Structures of the flax-rust effector AvrM reveal insights into the molecular basis of plant-cell entry and effector-triggered immunity

Ve, Thomas, Williams, Simon J., Catanzariti, Ann-Maree, Rafiqi, Maryam, Rahman, Motiur, Ellis, Jeffrey G., Hardham, Adrienne R., Jones, David A., Anderson, Peter A., Dodds, Peter N. and Kobe, Bostjan (2013) Structures of the flax-rust effector AvrM reveal insights into the molecular basis of plant-cell entry and effector-triggered immunity. Proceedings of the National Academy of Sciences of the United States of America, 110 43: 17594-17599. doi:10.1073/pnas.1307614110

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Author Ve, Thomas
Williams, Simon J.
Catanzariti, Ann-Maree
Rafiqi, Maryam
Rahman, Motiur
Ellis, Jeffrey G.
Hardham, Adrienne R.
Jones, David A.
Anderson, Peter A.
Dodds, Peter N.
Kobe, Bostjan
Title Structures of the flax-rust effector AvrM reveal insights into the molecular basis of plant-cell entry and effector-triggered immunity
Journal name Proceedings of the National Academy of Sciences of the United States of America   Check publisher's open access policy
ISSN 0027-8424
1091-6490
Publication date 2013-10-01
Year available 2013
Sub-type Article (original research)
DOI 10.1073/pnas.1307614110
Open Access Status File (Author Post-print)
Volume 110
Issue 43
Start page 17594
End page 17599
Total pages 6
Place of publication Washington, United States
Publisher National Academy of Sciences
Language eng
Formatted abstract
Fungal and oomycete pathogens cause some of the most devastating diseases in crop plants, and facilitate infection by delivering a large number of effector molecules into the plant cell. AvrM is a secreted effector protein from flax rust (Melampsora lini) that can internalize into plant cells in the absence of the pathogen, binds to phosphoinositides (PIPs), and is recognized directly by the resistance protein M in flax (Linum usitatissimum), resulting in effector-triggered immunity. We determined the crystal structures of two naturally occurring variants of AvrM, AvrM-A and avrM, and both reveal an L-shaped fold consisting of a tandem duplicated four-helix motif, which displays similarity to the WY domain core in oomycete effectors. In the crystals, both AvrM variants form a dimer with an unusual nonglobular shape. Our functional analysis of AvrM reveals that a hydrophobic surface patch conserved between both variants is required for internalization into plant cells, whereas the C-terminal coiled-coil domain mediates interaction with M. AvrM binding to PIPs is dependent on positive surface charges, and mutations that abrogate PIP binding have no significant effect on internalization, suggesting that AvrM binding to PIPs is not essential for transport of AvrM across the plant membrane. The structure of AvrM and the identification of functionally important surface regions advance our understanding of the molecular mechanisms underlying how effectors enter plant cells and how they are detected by the plant immune system.
Keyword innate immunity
plant cell internalization
plant disease resistance
avirulence protein
Q-Index Code C1
Q-Index Status Confirmed Code
Grant ID DP120100685
Institutional Status UQ

Document type: Journal Article
Sub-type: Article (original research)
Collections: Official 2014 Collection
School of Chemistry and Molecular Biosciences
Institute for Molecular Bioscience - Publications
 
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