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• Supplemental file 1 - Fig. S1a. Sequence alignment of the heat shock proteins used in this study. Comparison of the amino acid sequence of Mycobacterium bovis HSP65 (M. bovis, Swiss-Prot CH602_MYCBO, or M. tuberculosis, Swis-Prot CH602_MYCTU) with the HSP sequences from M. leprae (M. leprae, Swiss-Prot CH602_MYCLE), E. coli (E. coli, Swiss-Prot CH60_ECOLI), human (Homo sapiens, Swiss-Prot CH60_HUMAN), and mouse (Mus musculus, Swiss-Prot CH60_MOUSE). Asterisks mark identical amino acid residues in all five proteins, colons mark residues with high similarity, and periods mark residues with low similiarity. Fig. S1b. Sequence alignment of HSP70. Comparison of the amino acid sequence of M. tuberculosis HSP70 (M. tuberculosis, Swiss-Prot DNAK_MYCTU) with the HSP70 sequence from the mouse (Mus musculus, Swiss-Prot HS70A_MOUSE). Asterisks mark identical amino acid residues in all five proteins, colons mark residues with high similarity, and periods mark residues with low similarity. Sequence alignments were done with CLUSTAL X, version 1.8.1.
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