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Figure S1. Multiple sequence alignment of 21 H. armigera trypsin (HaTry; mature protein sequences). Trypsin-like sequences (BmTry-Q1HPT9 &BtTry-P00760) from model Bombyx mori and Bos taurus were also included in the alignment; this served the basis for similarity and divergence. Shaded regions represent conserved sequences, while the active site residues – namely, His (57), Asp (102) and Ser (195) – are highlighted by red rectangles and the predicted signal peptides are highlighted by blue rectangles.

Figure S2. Multiple sequence alignment of nine H. armigera chymotrypsins (HaChy; mature protein sequences). Chymotrypsin-like sequences (BmChy-Q1HPW8 &BtChy-Q7M3E1) from model Bombyx mori and Bos taurus were also included in the alignment; this served the basis for similarity and divergence. Shaded regions represent conserved sequences, while the active site residues – namely, His (57), Asp (102) and Ser (195) – are highlighted by red rectangles and the predicted signal peptides are highlighted by blue rectangles.

Figure S3. Phylogeny and sequence distances matrix of the eight H. armigera trypsins (HaTrys) as well as four HaChys generated out of the multiple sequence alignment (3A) and (3B). The matrix depicts the percent similarity among the sequences.

Figure S4. Semi-quantitative RT-PCR analysis of H. armigera trypsin (HaTry) 1 to 8 of fourth-instar larvae fed on okra (OK), rose (RO), pigeon pea (PP) and maize (MZ). The expression levels were normalized with respect to β-actin.

Figure S5. Activity profile of Helicoverpa gut proteases (HGPs) of fourth-instar larvae fed on okra (OK), rose (RO), pigeon pea (PP) and maize (MZ). Isoforms of H. armigera gut proteases were separated by SDS-PAGE (12%) and visualized using gel X-ray contact print technique (GXCT); untreated X-ray film was used as a substrate.

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