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New Phytologist

Mcnally, K.E.; Menardo, F.; Lüthi, L.; Praz, C.R.; Müller, M.C.; Kunz, L.; Chandrasekhar, K.; Dinoor, A.; Cowger, C.; Meyers, E.; Xue, M.; Zeng, F.; Gong, S.; Yu, D.; Bourras, S.; Keller, B.

Recognition of the AVRPM3A2/F2 avirulence protein from powdery mildew by the wheat PM3A/F immune receptor induces a hypersensitive response after co-expression in Nicotiana benthamiana. The molecular determinants of this interaction and how they shape natural AvrPm3a2/f2 allelic diversity are unknown. We sequenced the AvrPm3a2/f2 gene in a worldwide collection of 272 mildew isolates. Using the natural polymorphisms of AvrPm3a2/f2 as well as sequence information from related gene family members, we tested 85 single-residue-altered AVRPM3A2/F2 variants with PM3A, PM3F and PM3FL 456P/Y458H (modified for improved signaling) in Nicotiana benthamiana for effects on recognition. An intact AvrPm3a2/f2 gene was found in all analyzed isolates and the protein variant recognized by PM3A/F occurred globally at high frequencies. Single-residue alterations in AVRPM3A2/F2 mostly disrupted, but occasionally enhanced, the recognition response by PM3A, PM3F and PM3FL 456P/Y458H. Residues enhancing hypersensitive responses constituted a protein domain separate from both naturally occurring polymorphisms and positively selected residues of the gene family. These results demonstrate the utility of using gene family sequence diversity to screen residues for their role in recognition. This approach identified a putative interaction surface in AVRPM3A2/F2 not polymorphic in natural alleles. We conclude that molecular mechanisms besides recognition drive AvrPm3a2/f2 diversification. © 2018 New Phytologist Trust.

Department of Plant and Microbial Biology University of Zürich Zollikerstrasse 107 8008 Zürich Switzerland; Institute of Plant Science ARO-Volcani Center 50250 Bet Dagan Israel; Department of Plant Pathology and Microbiology The Robert H. Smith Faculty of Agriculture, Food and Environment The Hebrew University of Jerusalem Rehovot 76100 Israel; United States Department of Agriculture-Agricultural Research Service (USDA-ARS) North Carolina State University Raleigh 27695NC USA; Department of Plant Pathology North Carolina State University Raleigh 27695NC USA; Institute of Plant Protection and Soil Science Hubei Academy of Agricultural Sciences 430064 Wuhan China; Ministry of Agriculture Key Laboratory of Integrated Pest Management in Crops in Central China 430064 Wuhan China; College of Life Science Wuhan University 430072 Wuhan China

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Distinct domains of the AVRPM3A2/F2 avirulence protein from wheat powdery mildew are involved in immune receptor recognition and putative effector function
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Mcnally, K.E.; Menardo, F.; Lüthi, L.; Praz, C.R.; Müller, M.C.; Kunz, L.; Chandrasekhar, K.; Dinoor, A.; Cowger, C.; Meyers, E.; Xue, M.; Zeng, F.; Gong, S.; Yu, D.; Bourras, S.; Keller, B.

Distinct domains of the AVRPM3A2/F2 avirulence protein from wheat powdery mildew are involved in immune receptor recognition and putative effector function

Recognition of the AVRPM3A2/F2 avirulence protein from powdery mildew by the wheat PM3A/F immune receptor induces a hypersensitive response after co-expression in Nicotiana benthamiana. The molecular determinants of this interaction and how they shape natural AvrPm3a2/f2 allelic diversity are unknown. We sequenced the AvrPm3a2/f2 gene in a worldwide collection of 272 mildew isolates. Using the natural polymorphisms of AvrPm3a2/f2 as well as sequence information from related gene family members, we tested 85 single-residue-altered AVRPM3A2/F2 variants with PM3A, PM3F and PM3FL 456P/Y458H (modified for improved signaling) in Nicotiana benthamiana for effects on recognition. An intact AvrPm3a2/f2 gene was found in all analyzed isolates and the protein variant recognized by PM3A/F occurred globally at high frequencies. Single-residue alterations in AVRPM3A2/F2 mostly disrupted, but occasionally enhanced, the recognition response by PM3A, PM3F and PM3FL 456P/Y458H. Residues enhancing hypersensitive responses constituted a protein domain separate from both naturally occurring polymorphisms and positively selected residues of the gene family. These results demonstrate the utility of using gene family sequence diversity to screen residues for their role in recognition. This approach identified a putative interaction surface in AVRPM3A2/F2 not polymorphic in natural alleles. We conclude that molecular mechanisms besides recognition drive AvrPm3a2/f2 diversification. © 2018 New Phytologist Trust.

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