title: Venom peptides cathelicidin and lycotoxin cause strong inhibition of Escherichia coli ATP synthase.
abstract: Venom peptides are known to have strong antimicrobial activity and anticancer properties. King cobra cathelicidin or OH-CATH (KF-34), banded krait cathelicidin (BF-30), wolf spider lycotoxin I (IL-25), and wolf spider lycotoxin II (KE-27) venom peptides were found to strongly inhibit Escherichia coli membrane bound F1Fo ATP synthase. The potent inhibition of wild-type E. coli in comparison to the partial inhibition of null E. coli by KF-34, BF-30, Il-25, or KE-27 clearly links the bactericidal properties of these venom peptides to the binding and inhibition of ATP synthase along with the possibility of other inhibitory targets. The four venom peptides KF-34, BF-30, IL-25, and KE-27, caused ≥85% inhibition of wild-type membrane bound E.coli ATP synthase. Venom peptide induced inhibition of ATP synthase and the strong abrogation of wild-type E. coli cell growth in the presence of venom peptides demonstrates that ATP synthase is a potent membrane bound molecular target for venom peptides. Furthermore, the process of inhibition was found to be fully reversible.
authors.affiliation: Department of Biochemistry, Kirksville College of Osteopathic Medicine, A.T. Still University, Kirksville, MO, United States; Department of Biological Sciences, East Tennessee State University, Johnson City, TN 37614, United States.
authors.forename: Sofiya
authors.initials: S
authors.lastname: Azim
authors.affiliation: Department of Biochemistry, Kirksville College of Osteopathic Medicine, A.T. Still University, Kirksville, MO, United States.
authors.forename: Derek
authors.initials: D
authors.lastname: McDowell
authors.affiliation: Department of Biochemistry, Kirksville College of Osteopathic Medicine, A.T. Still University, Kirksville, MO, United States.
authors.forename: Alec
authors.initials: A
authors.lastname: Cartagena
authors.affiliation: Department of Biochemistry, Kirksville College of Osteopathic Medicine, A.T. Still University, Kirksville, MO, United States.
authors.forename: Ricky
authors.initials: R
authors.lastname: Rodriguez
authors.affiliation: Department of Biological Sciences, East Tennessee State University, Johnson City, TN 37614, United States.
authors.forename: Thomas F
authors.initials: TF
authors.lastname: Laughlin
authors.affiliation: Department of Biochemistry, Kirksville College of Osteopathic Medicine, A.T. Still University, Kirksville, MO, United States. Electronic address: zahmad@atsu.edu.
authors.forename: Zulfiqar
authors.initials: Z
authors.lastname: Ahmad
mesh_terms: D025181:ATP Synthetase Complexes / Q000037:antagonists & inhibitors*; D000595:Amino Acid Sequence; D023181:Antimicrobial Cationic Peptides / Q000737:chemistry / Q000494:pharmacology*; D002462:Cell Membrane / Q000187:drug effects / Q000378:metabolism; D049109:Cell Proliferation / Q000187:drug effects; D004791:Enzyme Inhibitors / Q000737:chemistry / Q000494:pharmacology*; D004926:Escherichia coli / Q000166:cytology / Q000201:enzymology*; D013111:Spider Venoms / Q000737:chemistry / Q000494:pharmacology*; D054804:Cathelicidins
chemical_list: D023181:Antimicrobial Cationic Peptides; D004791:Enzyme Inhibitors; D013111:Spider Venoms; C110534:lycotoxin I; C110535:lycotoxin II; D025181:ATP Synthetase Complexes; D054804:Cathelicidins
keywords: Cathelicidin; E. coli F(1)F(o) ATP synthase; F(1)-ATPase; Lycotoxin I; Lycotoxin II; OH-CATH; Venom peptides