Sensitivity of bacterial and fungal plant pathogens to the lytic peptides, MSI-99, magainin II, and cecropin B.
In vitro and leaf disk assays of bacterial and fungal plant pathogens were conducted using three cationic lytic peptides, MSI-99, magainin II (MII), and cecropin B (CB). Growth of bacterial organisms was retarded or completely inhibited by low concentrations of these lytic peptides. The peptides also significantly reduced germination of fungal spores and growth of mycelia; however, higher concentrations of peptides were needed to inhibit fungal growth compared with those needed to inhibit bacteria. The relative efficacy of the peptides depended on the microorganism tested, but CB was the most inhibitory to the majority of the bacteria and fungi assayed. MSI-99, a synthetic derivative of MII with increased positive charge, showed equal or two- to fivefold higher antibacterial activity compared to MII in the in vitro assays. MSI-99 was also superior to MII against the oomycete, Phytophthora infestans but was slightly inferior to MII in assays with the true fungi, Penicillium digitatum and Alternaria solani. In the leaf disk assays, pretreating spores of Alternaria solani and Phytophthora infestans with the peptides at concentrations as low as 10 microg per ml led to significant reductions in the size of early blight lesions and prevented development of any late blight lesions on tomato leaf disks. Our results from in vitro and leaf disk assays suggest that MSI-99 can be used as a transgene to generate tomato lines with enhanced resistance to bacterial and fungal diseases of this crop.
Alan
Ali R
AR
Department of Plant Breeding, Cornell University, Ithaca, NY 14853, USA.
Earle
Elizabeth D
ED
D000900:Anti-Bacterial Agents; D000890:Anti-Infective Agents / Q000494:pharmacology*; D023181:Antimicrobial Cationic Peptides / Q000494:pharmacology*; D001419:Bacteria / Q000187:drug effects* / Q000254:growth & development / Q000472:pathogenicity; D005658:Fungi / Q000187:drug effects* / Q000254:growth & development / Q000472:pathogenicity; D019476:Insect Proteins / Q000494:pharmacology*; D054806:Magainins; D010455:Peptides; D010940:Plant Proteins / Q000494:pharmacology*; D011994:Recombinant Proteins; D029867:Xenopus Proteins
D000900:Anti-Bacterial Agents; D000890:Anti-Infective Agents; D023181:Antimicrobial Cationic Peptides; D019476:Insect Proteins; C446524:MSI-99 peptide; D054806:Magainins; D010455:Peptides; D010940:Plant Proteins; D011994:Recombinant Proteins; D029867:Xenopus Proteins; C053301:magainin 2 peptide, Xenopus; C031162:cecropin B protein, Insecta