Multidimensional signatures in antimicrobial peptides.
Conventional analyses distinguish between antimicrobial peptides by differences in amino acid sequence. Yet structural paradigms common to broader classes of these molecules have not been established. The current analyses examined the potential conservation of structural themes in antimicrobial peptides from evolutionarily diverse organisms. Using proteomics, an antimicrobial peptide signature was discovered to integrate stereospecific sequence patterns and a hallmark three-dimensional motif. This striking multidimensional signature is conserved among disulfide-containing antimicrobial peptides spanning biological kingdoms, and it transcends motifs previously limited to defined peptide subclasses. Experimental data validating this model enabled the identification of previously unrecognized antimicrobial activity in peptides of known identity. The multidimensional signature model provides a unifying structural theme in broad classes of antimicrobial peptides, will facilitate discovery of antimicrobial peptides as yet unknown, and offers insights into the evolution of molecular determinants in these and related host defense effector molecules.
Yount
Nannette Y
NY
Division of Infectious Diseases, Harbor-UCLA Medical Center, 1124 West Carson Street, Torrance, CA 90502, USA.
Yeaman
Michael R
MR
D000595:Amino Acid Sequence; D000900:Anti-Bacterial Agents / Q000737:chemistry* / Q000276:immunology; D008969:Molecular Sequence Data; D010455:Peptides; D020543:Proteome; D017386:Sequence Homology, Amino Acid
D000900:Anti-Bacterial Agents; D010455:Peptides; D020543:Proteome