MOTS-c is a mitochondrial-encoded host defense peptide (HDP).
(A) Bacteria and bacteria-derived mitochondria possess gene-encoded immune peptides, known as host defense peptides (HDPs) in higher eukaryotes. (B) MOTS-c has a hydrophobic core (8YIFY11), determined using the hydrophobicity scales of Kyte and Doolittle (K&D)32 and Sweet and Eisenberg (S&E)33. Blue: cationic residues. (C) MOTS-c has a cationic tail (13RKLR16) that confers positive charge (Z) across a pH range. (D) MOTS-c treatment (0-100 µM) immediately aggregates E. coli in a dose dependent manner. (E) MOTS-c-dependent E. coli aggregation is lost in increasing salt concentrations (NaCl; 0-1%) and (F, G) requires its hydrophobic core and cationic tail, consistent with other HDPs. EGFP-expressing E. coli (BL21) shown. Wildtype MOTS- c (WT) and mutants devoid of its hydrophobic (YIFY: 8YIFY11>8AAAA11) or cationic domain (RKLR: 13RKLR16>13AAAA16). Bar, 75 µm. (H) Scanning electron micrographs of E. coli treated with MOTS-c (100 µM) for 0 (immediate fixation), 30, and 60 minutes (n=3). Representative images shown. Bar, 100 nm. (I-J) Growth curve of E. coli (BL21), measured by optical density at 600 nm (OD600), following (n=6) (I) MOTS-c treatment in the presence of 1% NaCl, and (J) treatment with wildtype (WT) MOTS-c and mutants devoid of its hydrophobic (8YIFY11>8AAAA11; YIFY), or cationic domain (13RKLR16>13AAAA16; RKLR). Data expressed as mean +/- SEM. Two-way ANOVA repeated measures. *** P<0.001.