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, 72 (8), 1449-59

Proposal for a Unified Nomenclature for Target-Site Mutations Associated With Resistance to Fungicides

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Proposal for a Unified Nomenclature for Target-Site Mutations Associated With Resistance to Fungicides

Wesley Mair et al. Pest Manag Sci.

Abstract

Evolved resistance to fungicides is a major problem limiting our ability to control agricultural, medical and veterinary pathogens and is frequently associated with substitutions in the amino acid sequence of the target protein. The convention for describing amino acid substitutions is to cite the wild-type amino acid, the codon number and the new amino acid, using the one-letter amino acid code. It has frequently been observed that orthologous amino acid mutations have been selected in different species by fungicides from the same mode of action class, but the amino acids have different numbers. These differences in numbering arise from the different lengths of the proteins in each species. The purpose of the present paper is to propose a system for unifying the labelling of amino acids in fungicide target proteins. To do this we have produced alignments between fungicide target proteins of relevant species fitted to a well-studied 'archetype' species. Orthologous amino acids in all species are then assigned numerical 'labels' based on the position of the amino acid in the archetype protein. © 2016 The Authors. Pest Management Science published by John Wiley & Sons Ltd on behalf of Society of Chemical Industry.

Keywords: Cyp51; SDHI; fungicide; mutation; target site.

Figures

Figure 1
Figure 1
Amino acid sequence alignment of the Cytb family. Sequences are named by species EPPO code and NCBI gene accession number. Residues highlighted in yellow in the archetype sequence from Zymoseptoria tritici denote amino acid substitutions associated with fungicide resistance at an orthologous position in any of the sequences. Numerical mutation labels shown above the alignment are based on the position number of the amino acid in the archetype protein.
Figure 2
Figure 2
Amino acid sequence alignment of the Cyp51A family. Sequences are named by species EPPO code and NCBI gene accession number. Residues highlighted in yellow in the archetype sequence from Aspergillus fumigatus (Cyp51A) denote amino acid substitutions associated with fungicide resistance at an orthologous position in any of the sequences. Numerical mutation labels shown above the alignment are based on the position number of the amino acid in the archetype protein.
Figure 3
Figure 3
Amino acid sequence alignment of the Cyp51B family. Sequences are named by species EPPO code and NCBI gene accession number. Residues highlighted in yellow in the archetype sequence from Zymoseptoria tritici denote amino acid substitutions associated with fungicide resistance at an orthologous position in any of the sequences. Numerical mutation labels shown above the alignment are based on the position number of the amino acid in the archetype protein.
Figure 4
Figure 4
Amino acid sequence alignment of the b‐tubulin family. Sequences are named by species EPPO code and NCBI gene accession number. Residues highlighted in yellow in the archetype sequence from Aspergillus nidulans (benA) denote amino acid substitutions associated with fungicide resistance at an orthologous position in any of the sequences. Numerical mutation labels shown above the alignment are based on the position number of the amino acid in the archetype protein.
Figure 5
Figure 5
Amino acid sequence alignment of the SdhB family. Sequences are named by species EPPO code and NCBI gene accession number. Residues highlighted in yellow in the archetype sequence from Pyrenophora teres f. sp. teres denote amino acid substitutions associated with fungicide resistance at an orthologous position in any of the sequences. Numerical mutation labels shown above the alignment are based on the position number of the amino acid in the archetype protein.
Figure 6
Figure 6
Amino acid sequence alignment of the SdhC family. Sequences are named by species EPPO code and NCBI gene accession number. Residues highlighted in yellow in the archetype sequence from Pyrenophora teres f. sp. teres denote amino acid substitutions associated with fungicide resistance at an orthologous position in any of the sequences. Numerical mutation labels shown above the alignment are based on the position number of the amino acid in the archetype protein.
Figure 7
Figure 7
Amino acid sequence alignment of the SdhD family. Sequences are named by species EPPO code and NCBI gene accession number. Residues highlighted in yellow in the archetype sequence from Pyrenophora teres f. sp. teres denote amino acid substitutions associated with fungicide resistance at an orthologous position in any of the sequences. Numerical mutation labels shown above the alignment are based on the position number of the amino acid in the archetype protein.
Figure 8
Figure 8
Amino acid sequence alignment of the CesA3 family. Sequences are named by species EPPO code and NCBI gene accession number. Residues highlighted in yellow in the archetype sequence from Phytophthora infestans denote amino acid substitutions associated with fungicide resistance at an orthologous position in any of the sequences. Numerical mutation labels shown above the alignment are based on the position number of the amino acid in the archetype protein.
Figure 9
Figure 9
Amino acid sequence alignment of the OS‐1 family. Sequences are named by species EPPO code and NCBI gene accession number. Residues highlighted in yellow in the archetype sequence from Botrytis cinerea denote amino acid substitutions associated with fungicide resistance at an orthologous position in any of the sequences. Numerical mutation labels shown above the alignment are based on the position number of the amino acid in the archetype protein.

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