title: Antimicrobial peptide CRAMP (16-33) stalls bacterial cytokinesis by inhibiting FtsZ assembly.
abstract: A cathelin-related antimicrobial peptide (CRAMP) of 37 amino acid residues is thought to regulate innate immunity and provide a host defense mechanism in mammals. Here, a part of the CRAMP peptide, CRAMP (16-33) (GEKLKKIGQKIKNFFQKL), was found to bind to FtsZ and to inhibit the assembly and GTPase activity of FtsZ in vitro. A computational analysis indicated that CRAMP (16-33) binds in the cavity of the T7 loop of FtsZ. Both hydrophobic and ionic interactions were involved in the binding interactions. Further, CRAMP (16-33) inhibited the formation of the FtsZ ring in bacteria, indicating that it inhibited bacterial cell division by inhibiting FtsZ assembly.
authors.affiliation: Department of Biosciences and Bioengineering, IIT Bombay , Powai, Mumbai 400076, India.
authors.forename: Shashikant
authors.initials: S
authors.lastname: Ray
authors.forename: Hemendra Pal Singh
authors.initials: HP
authors.lastname: Dhaked
authors.forename: Dulal
authors.initials: D
authors.lastname: Panda
mesh_terms: D000818:Animals; D000900:Anti-Bacterial Agents / Q000737:chemistry / Q000378:metabolism / Q000494:pharmacology*; D023181:Antimicrobial Cationic Peptides / Q000737:chemistry / Q000378:metabolism / Q000494:pharmacology*; D001412:Bacillus subtilis / Q000187:drug effects / Q000254:growth & development / Q000378:metabolism; D001426:Bacterial Proteins / Q000037:antagonists & inhibitors* / Q000737:chemistry / Q000235:genetics / Q000378:metabolism; D001665:Binding Sites; D054804:Cathelicidins / Q000737:chemistry / Q000378:metabolism / Q000494:pharmacology*; D048749:Cytokinesis / Q000187:drug effects*; D003598:Cytoskeletal Proteins / Q000037:antagonists & inhibitors* / Q000737:chemistry / Q000235:genetics / Q000378:metabolism; D004791:Enzyme Inhibitors / Q000737:chemistry / Q000378:metabolism / Q000494:pharmacology*; D004926:Escherichia coli / Q000187:drug effects / Q000254:growth & development / Q000378:metabolism; D020558:GTP Phosphohydrolases / Q000037:antagonists & inhibitors / Q000737:chemistry / Q000378:metabolism; D006160:Guanosine Triphosphate / Q000378:metabolism; D006461:Hemolysis / Q000187:drug effects; D006801:Humans; D006868:Hydrolysis / Q000187:drug effects; D008564:Membrane Potentials / Q000187:drug effects; D051379:Mice; D046529:Microscopy, Electron, Transmission; D008958:Models, Molecular; D062105:Molecular Docking Simulation; D050505:Mutant Proteins / Q000037:antagonists & inhibitors / Q000737:chemistry / Q000378:metabolism; D010446:Peptide Fragments / Q000737:chemistry / Q000378:metabolism / Q000494:pharmacology*; D011487:Protein Conformation
chemical_list: D000900:Anti-Bacterial Agents; D023181:Antimicrobial Cationic Peptides; D001426:Bacterial Proteins; C000594016:CRAMP (16-33); D054804:Cathelicidins; D003598:Cytoskeletal Proteins; D004791:Enzyme Inhibitors; C071525:FtsZ protein, Bacteria; D050505:Mutant Proteins; D010446:Peptide Fragments; D006160:Guanosine Triphosphate; D020558:GTP Phosphohydrolases