Fig. 7

Structural similarity of Colletotrichum lentis ClToxB with ToxB of other species. a. ClToxB shows structural similarity to ToxB proteins from closely related species and 3 ToxB variants from Pyrenophora tritici-repentis. Four conserved cysteine residues were identified in the mature protein, and these amino acid residues are likely to form two cystine bridges, which may provide stability to ToxB proteins in the host cell apoplast. Peptide sequences were aligned using ESPrint version 3.0. Putative signal peptides (black line) were predicted using SignalP version 4.1. ClToxB, Colletotrichum lentis (Race 1, CT-21 [less virulent isolate] and Race 0, CT-30 [virulent isolate]); CoToxB, C. orbiculare 104-T (virulent isolate); CgToxB, C. gloeosporiodes Nara gc5 (virulent isolate); ChToxB, Colletotrichum higginsianum IMI349063 (virulent isolate); MoToxB, Magnaporthe oryzae Y34 (virulent isolate); 90-2toxb, Pyrenophora tritici-repentis 90–2 (Race 4, 90–2 [avirulent isolate]); SD20toxb, Pyrenophora tritici-repentis (Race 4, SD20 [avirulent isolate]); and Alg3-24ToxB, Pyrenophora tritici-repentis (Race 5, Alg3-24 [most virulent isolate]). b. ClToxB homologs contain a conserved cysteine residue pattern. Sequence logo was generated from the Clustal W-aligned ToxB mature proteins using Seg2Logo (Thomsen and Nielsen [50]). Big and small amino acid residue stacks indicate conserved and variable sites, respectively. Conserved cysteine residues are likely to form two cystine bridges (disulfide bonds)