Increased diversity of intestinal antimicrobial peptides by covalent dimer formation.
Antimicrobial peptides are essential effector molecules of the innate immune system. Here we describe the structure, function and diversity of cryptdin-related sequence (CRS) peptides, a large family of antimicrobial molecules. We identified the peptides as covalent dimers in mouse intestinal tissue in amounts comparable to those of Paneth cell-derived enteric alpha-defensins. CRS peptides caused rapid and potent killing of commensal and pathogenic bacteria. The CRS peptides formed homo- and heterodimers in vivo, thereby expanding the repertoire of antimicrobial peptides and increasing the peptide diversity of Paneth cell secretions. CRS peptides might therefore be important in the maintenance of the microbial homeostasis within the intestinal tract.
Hornef
Mathias W
MW
Institute of Medical Microbiology and Hygiene, University of Freiburg, D-79104 Freiburg, Germany.
Pütsep
Katrin
K
Karlsson
Jenny
J
Refai
Essam
E
Andersson
Mats
M
D000595:Amino Acid Sequence; D000818:Animals; D002851:Chromatography, High Pressure Liquid; D019281:Dimerization; D005260:Female; D014644:Genetic Variation; D007413:Intestinal Mucosa / Q000276:immunology*; D051379:Mice; D008969:Molecular Sequence Data; D019879:Paneth Cells / Q000276:immunology; D010455:Peptides / Q000235:genetics / Q000276:immunology; D011498:Protein Precursors / Q000737:chemistry / Q000235:genetics* / Q000276:immunology; D012333:RNA, Messenger / Q000032:analysis; D020133:Reverse Transcriptase Polymerase Chain Reaction; D017386:Sequence Homology, Amino Acid
D010455:Peptides; D011498:Protein Precursors; D012333:RNA, Messenger; C059569:cryptdin