JCS026682 Supplementary Material

Files in this Data Supplement:

• Supplemental Figure S1 (Adobe PDF) -

  Fig. S1. The predicted amino acid sequence of CfaD. An underline indicates the tryptic sequence obtained from the 27 kDa protein from partially purified CF. An arrow indicates the predicted signal peptide cleavage site. The Peptidase C1A subfamily domain is shaded grey, with the thiol protease cys (AA327-338) and thiol protease his (AA 473-483) active sites indicated by boxes. The sequence is available in GenBank as XP640530. For more information on the protein sequencing and analysis method, please contact the author.

• Supplemental Figure S2 (Adobe PDF) -

  Fig. S2. Multiple amino acid sequence alignment of DdCfaD. A multiple alignment was performed with Cathepsin L amino acid sequences from Ae (Aedes aegypti; ABE72972), Sp (Sarcophaga peregrine; O97453), Dd (Dictyostelium discoideum; XP640530), Hs (Homo sapiens; O60911) and At (Arabidopsis thaliana; Q8LAC2) with the ClustalW program. Amino acids highlighted in yellow represent the identical and similar residues between the sequences. In addition, * represent residues that are identical and ‘.’ or ‘:’ represent residues that are similar between the sequences. Note that the numbering is for a consensus, not for CfaD. The glutamine (Q) and cysteine (C) active site residues are indicated by red boxes.

• Supplemental Figure S3 (Adobe PDF) -

  Fig. S3. All wild type cells contain CfaD. (A) Fields of wild-type (WT) and cfaD⁻ cells were fixed and stained with affinity-purified anti-CfaD antibodies for imunofluorescence. The left panels are phase-contrast images and the right panels are the fluorescence images. Bar is 30 µm. (B) The anti-CfaD staining of three individual wild-type cells was imaged using deconvolution. Bar is 10 µm. For more information on the immunofluorescence method, please contact the author.