1. Expression of a Cecropin B lytic peptide analog in transgenic tobacco confers enhanced resistance to bacterial wilt caused by Pseudomonas solanacearum
- Author
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Jian Hong Huang, Luis Destéfano-Beltrán, Jesse M. Jaynes, Timothy P. Denny, JaeHo Kim, Selim Çetiner, Pablito Nagpala, and Çukurova Üniversitesi
- Subjects
PEPTIDE DESIGN ,biology ,Agrobacterium ,Nicotiana tabacum ,Bacterial wilt ,fungi ,Virulence ,Plant Science ,General Medicine ,Agrobacterium tumefaciens ,biology.organism_classification ,GENETIC ENGINEERING ,Microbiology ,Transformation (genetics) ,Cecropin ,DISEASE RESISTANT PLANTS ,Hyalophora cecropia ,Genetics ,Agronomy and Crop Science - Abstract
Cecropin B is a naturally-occurring lytic peptide found in Hyalophora cecropia, the Giant Silk Moth. It is thought to comprise part of an inducible humoral defense system that combats infection in the insect. Two 38 amino acid peptides, SB-37 and Shiva-1, were produced as substitution analogs of Cecropin B. SB-37 is 95% homologous to Cecropin B while Shiva-1 retains only 46% homology to the natural molecule. However, hydrophobic properties and charge density of the native structure were conserved at 100% in the synthetic peptides. The genes for both peptides were chemically synthesized and cloned into the binary vector pBI121 under the control of a constitutive or wound-inducible plant promoter. Transgenic tobacco plants (RO) were subsequently obtained via Agrobacterium transformation. Bioassays to test disease resistance of R1 progeny indicate that, compared to transgenic control and SB-37 plants, Shiva-1 seedlings exhibited delayed wilt symptoms and reduced disease severity and mortality after infection with a highly virulent strain of Pseudomonas solanacearum. © 1993. Agricultural Experiment Station, New Mexico State University The authors wish to acknowledge the expert technical assistance in peptide synthesis and purification provided by Martha Juban. This research was supported, in part, by funds from the Louisiana State University Agricultural Experiment Station.
- Published
- 1993
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