title: Human antimicrobial peptides: defensins, cathelicidins and histatins.
abstract: Antimicrobial peptides, which have been isolated from many bacteria, fungi, plants, invertebrates and vertebrates, are an important component of the natural defenses of most living organisms. The isolated peptides are very heterogeneous in length, sequence and structure, but most of them are small, cationic and amphipathic. These peptides exhibit broad-spectrum activity against Gram-positive and Gram-negative bacteria, yeasts, fungi and enveloped viruses. A wide variety of human proteins and peptides also have antimicrobial activity and play important roles in innate immunity. In this review we discuss three important groups of human antimicrobial peptides. The defensins are cationic non-glycosylated peptides containing six cysteine residues that form three intramolecular disulfide bridges, resulting in a triple-stranded beta-sheet structure. In humans, two classes of defensins can be found: alpha-defensins and beta-defensins. The defensin-related HE2 isoforms will also be discussed. The second group is the family of histatins, which are small, cationic, histidine-rich peptides present in human saliva. Histatins adopt a random coil conformation in aqueous solvents and form alpha-helices in non-aqueous solvents. The third group comprises only one antimicrobial peptide, the cathelicidin LL-37. This peptide is derived proteolytically from the C-terminal end of the human CAP18 protein. Just like the histatins, it adopts a largely random coil conformation in a hydrophilic environment, and forms an alpha-helical structure in a hydrophobic environment.
authors.affiliation: Unit of Fundamental and Applied Molecular Biology, Department for Molecular Biomedical Research, Ghent University and VIB, Technologiepark 927, B-9052, Ghent, Belgium.
authors.forename: Kris
authors.initials: K
authors.lastname: De Smet
authors.forename: Roland
authors.initials: R
authors.lastname: Contreras
mesh_terms: D000595:Amino Acid Sequence; D000890:Anti-Infective Agents / Q000737:chemistry* / Q000494:pharmacology*; D023181:Antimicrobial Cationic Peptides / Q000737:chemistry / Q000235:genetics / Q000494:pharmacology; D001419:Bacteria / Q000187:drug effects / Q000254:growth & development; D023082:Defensins / Q000737:chemistry / Q000235:genetics / Q000494:pharmacology; D005658:Fungi / Q000187:drug effects / Q000254:growth & development; D006801:Humans; D008826:Microbial Sensitivity Tests; D008958:Models, Molecular; D008969:Molecular Sequence Data; D017433:Protein Structure, Secondary; D011506:Proteins / Q000737:chemistry / Q000235:genetics / Q000494:pharmacology; D054804:Cathelicidins; D000099053:Histidine-Rich Glycoprotein
chemical_list: D000890:Anti-Infective Agents; D023181:Antimicrobial Cationic Peptides; D023082:Defensins; D011506:Proteins; D000099053:Histidine-Rich Glycoprotein; D054804:Cathelicidins