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: Shashikant Ray, Hemendra Pal Singh Dhaked, Dulal Panda
• Journal: Biochemistry (Biochemistry) Vol. 53 Issue 41 Pg. 6426-9 (Oct 21 2014) ISSN: 1520-4995 [Electronic] United States
• PMID: 25294259 (Publication Type: Journal Article, Research Support, Non-U.S. Gov't)

Chemical References

• Anti-Bacterial Agents
• Antimicrobial Cationic Peptides
• Bacterial Proteins
• CRAMP (16-33)
• Cathelicidins
• Cytoskeletal Proteins
• Enzyme Inhibitors
• FtsZ protein, Bacteria
• Mutant Proteins
• Peptide Fragments
• Guanosine Triphosphate
• GTP Phosphohydrolases

Topics

• Animals
• Anti-Bacterial Agents (chemistry, metabolism, pharmacology)
• Antimicrobial Cationic Peptides (chemistry, metabolism, pharmacology)
• Bacillus subtilis (drug effects, growth & development, metabolism)
• Bacterial Proteins (antagonists & inhibitors, chemistry, genetics, metabolism)
• Binding Sites
• Cathelicidins (chemistry, metabolism, pharmacology)
• Cytokinesis (drug effects)
• Cytoskeletal Proteins (antagonists & inhibitors, chemistry, genetics, metabolism)
• Enzyme Inhibitors (chemistry, metabolism, pharmacology)
• Escherichia coli (drug effects, growth & development, metabolism)
• GTP Phosphohydrolases (antagonists & inhibitors, chemistry, metabolism)
• Guanosine Triphosphate (metabolism)
• Hemolysis (drug effects)
• Humans
• Hydrolysis (drug effects)
• Membrane Potentials (drug effects)
• Mice
• Microscopy, Electron, Transmission
• Models, Molecular
• Molecular Docking Simulation
• Mutant Proteins (antagonists & inhibitors, chemistry, metabolism)
• Peptide Fragments (chemistry, metabolism, pharmacology)
• Protein Conformation