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. 2017 Aug 7;114(34):8980–8985. doi: 10.1073/pnas.1706894114

Fig. 1.

Fig. 1.

Biochemical characterization of Y3. (A) Sequence alignment of Y3 and its homologs from fungal species. Conserved cysteine residues that potentially form disulfide bridges are shaded in dark- and light green and all other conserved residues are indicated with dots (·). Potential N-glycosylation site (Asn110-Ser112) in Y3 is underlined with a dark line, and Asn110 is labeled with an asterisk (*). Residues potentially involved in ligand binding are shaded in yellow. Y3: C. comatus, GenBank: ADK35888.1; Agaricus: Agaricus bisporus var. burnettii JB137-S8, GenBank: XP_007333380.1; Galerina: Galerina marginata CBS 339.88, GenBank: KDR84548.1; Gymnopus: Gymnopus luxurians FD-317 M1, GenBank: KIK60251.1; Hebeloma: Hebeloma cylindrosporum h7, GenBank: KIM42673.1; Leucoagaricus: Leucoagaricus sp. SymC.cos, GenBank: KXN92904.1. (B) Recombinant Y3 was a putative dimer as shown in SEC analysis. Retention volumes of molecular standards of 1.35, 17, 44, and 158 kDa are indicated. (C) SDS/PAGE analysis showed the high purity of recombinant Y3. (D) The m/z value of purified Y3 at 12,204.85 in MALDI-MS analysis matched with calculated molecular weight of mature Y3 monomer (12,229.54 Da). (E) The inhibitory curve of recombinant Y3 on TMGMV infection. Data are presented as mean ± SD (n = 6).