Expression of a Cecropin B lytic peptide analog in transgenic tobacco confers enhanced resistance to bacterial wilt caused by Pseudomonas solanacearum

Jaynes, Jesse M.; Nagpala, P. G.; Destéfano-Beltrán, Luis; Huang, J.Y.; Kim, Jae-Ho; Denny, Timothy P.; Çetiner, Selim

doi:10.1016/0168-9452(93)90169-z

Cited by 145 publications

(81 citation statements)

References 23 publications

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“…The EC 50 values, with the exception of those for peptide 2M2, were 5 to 15 times lower than that of purified cecropin B, which had EC 50 values of about 15 M (data not shown) (mean values for 2M5 and 6M1 were not significantly different from each other but were significantly different from mean values for 2L2 and 2M2; mean values for 2M2 and 2L2 were significantly different from each other [P Ͻ 0.05]). These effective concentrations are of the same magnitude as those reported for other synthetic lytic peptides derived from cecropin B against a variety of gram-positive and gramnegative bacteria (4,5,6,11,13,14,15,17,18,20,21).…”

supporting

confidence: 73%

Effects of Synthetic Cecropin Analogs on in Vitro Growth of Acholeplasma laidlawii

Borth

Jones

Ullman

et al. 2001

Antimicrob Agents Chemother

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Four synthetic peptides (Peptidyl MIMs; Demeter Biotechnologies, Inc.) were evaluated for their in vitro activity against Acholeplasma laidlawii. Fifty percent effective concentration values ranged from 1 to 15 M. Three of these compounds are more lethal than cecropin B against A. laidlawii.Lytic polypeptides with antimicrobial activity have been isolated from insect hemolymph, amphibians, and mammals (3). Encoded by single genes, these short peptides have potent antimicrobial activity against a wide spectrum of microorganisms, including bacteria and fungi, yet have very low toxicities to higher organisms. Biologically active synthetic peptides have been produced, and gene constructs coding for lytic polypeptides have been introduced into a number of higher plants for the control of bacterial and fungal phytopathogens (1,2,7,9,10,11,12,14,17,18,19). We have evaluated the activity of four synthetic cecropin analogs for their antimicrobial activities against the mollicute Acholeplasma laidlawii. These analogs were designed for enhanced membrane lysis activity, and each possesses features characteristic of cecropin-like lytic polypeptides (6). Specifically, these peptides each are strongly basic polar molecules which are predicted to form hydrophilic amphipathic ␣-helices in their N-terminal regions and more hydophobic ␣-helices in their C-terminal regions.A. laidlawii strain PG-8 (ATCC 23206) was grown in liquid SP-4 medium (22) at 37°C. To assess the lytic activity of each peptide, early-log-phase cultures were exposed to six concentrations of four synthetic Peptidyl Membrane Interactive Molecules (Peptidyl MIMs; Demeter Biotechnologies Inc., Triangle Park, N.C.). The amino acid sequences of these peptides and cecropin B are as follows: 6M1, FKLRAKIKVRLRAKIKL; 2M5, KRKRAVKRVGRRLKKLARKIARLGVAKLAGLR AVKLF; 2M2, KRKRAVKRVGRRLKKLARKIARLGVAF; 2L2, FAKKFAKKFKKFAKKFAKFAFAF; cecropin B, KW KVFKKIEKMGRNIRNGIVKAGPAIAVLGEAKAL.To each of seven 270-l aliquots of early-log-phase A. laidlawii (10 7 to 10 8 CFU/ml) was added 30 l of dilutions of each Peptidyl MIM. Solutions and cells were incubated at 37°C for 60 min, and three 20-l aliquots of each dilution were plated and allowed to dry, without spreading, onto SP-4 medium solidified with 12% Noble agar. Plates were incubated at 37°C for 2 to 3 days in a humidified chamber, and CFUs were counted after staining in Diene's stain. All treatments with each Peptidyl MIM were replicated three times. Mean viable CFU/ml values were calculated from each replicated dilution plating. Percent survival for each Peptidyl MIM at each peptide concentration was calculated based upon the CFU/ml from each dilution plating divided by the CFU/ml of the water control. EC 50 s (estimated concentrations resulting in 50% survival) were calculated for each compound by regressing the percent survival against the natural logarithm of the compound concentration. The resulting regression equation was used to calculate the concentration of compound that would result in 50% survival. Paired t tests were used...

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supporting

confidence: 73%

Effects of Synthetic Cecropin Analogs on in Vitro Growth of Acholeplasma laidlawii

Borth

Jones

Ullman

et al. 2001

Antimicrob Agents Chemother

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“…In the present study, transgenic tobacco plants expressing the Lfc gene were developed to enhance resistance against a broad spectrum of plant pathogens. As a result, Lfc exhibited bactericidal activity as high as bactericidal peptides, such as sarcotoxin IA derived from fresh y Sarcophaga peregrina (Ohshima et al 1999) and cecropin derived from giant silk moth Hylophora cecropiaie (Hightower et al 1994;Jan et al 2010;Jaynes et al 1993).…”

Section: Discussionmentioning

confidence: 99%

“…Transgenic plants showed considerably greater resistance to pathogens (Hightower et al 1994;Jan et al 2010;Jaynes et al 1993;Ohshima et al 1999;Osusky et al 2000;Osusky et al 2004) and parasitic weeds (Radi et al 2006) than to the wild types. Zhang et al (1998) reported that transgenic tobacco expressing human lactoferrin protein demonstrated signi cant delays in developing bacterial wilt symptoms when inoculated with the bacterial pathogen Ralstonia solanacearum.…”

mentioning

confidence: 99%

“…Many studies have shown the expression of antimicrobial cationic peptides in plants, e.g., cecropin in tobacco (Hightower et al 1994;Jaynes et al 1993) and tomato (Jan et al 2010), sarcotoxin in tobacco (Ohshima et al 1999) and tomato (Radi et al 2006), MsrA3 in potatoes (Osusky et al 2004), and cecropinmelittin chimeric peptide in potato (Osusky et al 2000). Transgenic plants showed considerably greater resistance to pathogens (Hightower et al 1994;Jan et al 2010;Jaynes et al 1993;Ohshima et al 1999;Osusky et al 2000;Osusky et al 2004) and parasitic weeds (Radi et al 2006) than to the wild types.…”

mentioning

confidence: 99%

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Transgenic tobacco plants expressing antimicrobial peptide bovine lactoferricin show enhanced resistance to phytopathogens

Fukuta

Kawamoto²,

Mizukami

et al. 2012

Plant Biotechnology

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Lactoferricin B, the antimicrobially active N-terminal peptide derived from acid pepsin hydrolysis of bovine lactoferrin, has broad spectrum antimicrobial activities. We expressed the lactoferricin gene in tobacco plants to evaluate its antimicrobial activity. e coding region for the chimeric peptide gene of the signal peptide from tobacco pathogenrelated protein (PR-1) and bovine lactoferricin was synthesized using the recombinant polymerase chain reaction (PCR) method. Transgenic tobacco plants expressing the lactoferricin gene were developed using the Agrobacterium-mediated transformation method. e lactoferricin B gene was integrated into the tobacco genome and its transcription was detected by PCR, Southern blot analysis, and reverse transcription PCR (RT-PCR), respectively. e transgenic tobacco plants were challenged with the pathogenic bacteria Pseudomonas syringae pv. tabaci and Botrytis cinerea. At 30 or 28 days postinoculation, the transgenic plants were still green and continued to grow, whereas the control plants were infected with bacterial or fungal pathogens from the roots to the tips, resulting in death of the plants. In conclusion, transgenic tobacco plants that overexpressed the lactoferricin gene, linked to the signal peptide of tobacco PR-1 protein under the control of a high expression constitutive promoter, showed enhanced resistance to bacterial (P. syringae pv. tabaci) and fungal (B. cinerea) diseases.

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“…9); (ii) peptides with one to six intramolecular disulfide bridges including the arthropod defensins (10), antifungal peptides from Drosophila, drosomycin (11) and metchnikowin (12), thanatin from Podisus (13), tachyplesin, big defensin and tachycitin from limulus (14 -16), and other cysteine-rich antimicrobial peptides isolated from a scorpion (17) and from a bivalve mollusk (18,19); (iii) prolinerich peptides, among them the apidaecins and abaecins from Hymenoptera (20,21) and drosocin from Drosophila hemolymph (22); (iv) glycine-rich antimicrobial peptides or polypeptides (9 -30 kDa) such as the attacins (23), diptericin (24) and sarcotoxins (25). The mode of action, the broad activity, the molecular diversity, and the noncytotoxicity of all these circulating antimicrobial peptides make them very attractive as therapeutic agents for pharmaceutical or agricultural applications (26,27).…”

mentioning

confidence: 99%

Penaeidins, a New Family of Antimicrobial Peptides Isolated from the Shrimp Penaeus vannamei (Decapoda)

Destoumieux

Bulet

Loew

et al. 1997

Journal of Biological Chemistry

374

247

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We report here the isolation of three members of a new family of antimicrobial peptides from the hemolymph of shrimps Penaeus vannamei in which immune response has not been experimentally induced. The three molecules display antimicrobial activity against fungi and bacteria with a predominant activity against Gram-positive bacteria. The complete sequences of these peptides were determined by a combination of enzymatic cleavages, Edman degradation, mass spectrometry, and cDNA cloning using a hemocyte cDNA library. The mature molecules (50 and 62 residues) are characterized by an NH 2 -terminal domain rich in proline residues and a COOH-terminal domain containing three intramolecular disulfide bridges. One of these molecules is post-translationally modified by a pyroglutamic acid at the first position. Comparison of the data obtained from the cDNA clones and mass spectrometry showed that two of these peptides are probably COOHterminally amidated by elimination of a glycine residue. These molecules with no evident homology to other hitherto described antimicrobial peptides were named penaeidins.

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Expression of a Cecropin B lytic peptide analog in transgenic tobacco confers enhanced resistance to bacterial wilt caused by Pseudomonas solanacearum

Cited by 145 publications

References 23 publications

Effects of Synthetic Cecropin Analogs on in Vitro Growth of Acholeplasma laidlawii

Effects of Synthetic Cecropin Analogs on in Vitro Growth of Acholeplasma laidlawii

Transgenic tobacco plants expressing antimicrobial peptide bovine lactoferricin show enhanced resistance to phytopathogens

Penaeidins, a New Family of Antimicrobial Peptides Isolated from the Shrimp Penaeus vannamei (Decapoda)

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