Susceptibility of Rickettsia monacensis and Rickettsia peacockii to Cecropin A, Ceratotoxin A, and lysozyme.
Ticks host obligate intracellular bacteria that range from benign symbiotes to virulent human pathogens. The effects on those bacteria of antimicrobial peptides (AMPs) involved in arthropod innate immunity to microbial infections are largely unknown. We evaluated effects of AMPs and a c-type lysozyme on host cell-free suspensions of the tick symbiotes Rickettsia monacensis and Rickettsia peacockii with stain-based infectivity and viability assays. Cecropin A at a concentration of 8 muM: had a lethal effect on both rickettsiae while ceratotoxin A was approximately 20-fold less effective. Toxicity of both AMPs was synergized by lysozyme, an enzyme expressed by ticks. Lactoferrin, a transferrin, had no effect on R. monacensis at up to 110 microM. The rickettsiae were less sensitive to the AMPs than is typical of bacteria that grow extracellularly. Our assays may be useful in the study of AMP activity against other obligate intracellular bacteria.
Baldridge
Gerald D
GD
Department of Entomology, University of Minnesota, Paul, 55108, USA. Baldr001@umn.edu
Kurtti
Timothy J
TJ
Munderloh
Ulrike G
UG
D023181:Antimicrobial Cationic Peptides / Q000494:pharmacology* / Q000633:toxicity; D019476:Insect Proteins / Q000494:pharmacology* / Q000633:toxicity; D008826:Microbial Sensitivity Tests; D009113:Muramidase / Q000494:pharmacology* / Q000633:toxicity; D012281:Rickettsia / Q000145:classification / Q000187:drug effects* / Q000378:metabolism
D023181:Antimicrobial Cationic Peptides; D019476:Insect Proteins; C082689:ceratotoxin A protein, Ceratitis capitata; C031161:cecropin A; D009113:Muramidase