[Objective] This study was to identify the expression of exogenous antimicrobial peptide in transgenic Houttuynia cordata Thunb. plants,and analyze their resistance to stem rot disease. [Methods] SDS-PAGE and Western ...[Objective] This study was to identify the expression of exogenous antimicrobial peptide in transgenic Houttuynia cordata Thunb. plants,and analyze their resistance to stem rot disease. [Methods] SDS-PAGE and Western blot analysis were employed to detect expression of exogenous antimicrobial peptide in transgenic H. cordata plants. Both wild type and transgenic H. cordata plants were inoculated with different concentrations of Rhizoctonia solani spores for detecting their resistance. [Results] The exogenous antimicrobial peptide was detected at translation level. The optimal parameters for detecting the resistance of transgenic H. cordata plants to R. solani was inoculation of spores at a concentration of 3×105 ind./ml and cultured for three days. The results showed that resistance of transgenic H. cordata plants to R. solani was enhanced in comparison with CKs. [Conclusion] Expression of exogenous antimicrobial peptide can enhance the resistance of transgenic H. cordata plants to stem rot disease.展开更多
HPRP-A1, a 15-mer α-helical cationic peptide, was derived from N-terminus of ribosomal protein L1 (RpL1) of Helicobacter pylori. In this study, HPRP-A1 was used as a framework to obtain a series of peptide analogs wi...HPRP-A1, a 15-mer α-helical cationic peptide, was derived from N-terminus of ribosomal protein L1 (RpL1) of Helicobacter pylori. In this study, HPRP-A1 was used as a framework to obtain a series of peptide analogs with different hydrophobicity by single amino acid substitutions in the center of nonpolar face of the amphipathic helix in order to systematically study the effect of hydrophobicity on biological activities of -helical antimicrobial peptides. Hydrophobicity and net charge of peptides played key roles in the biological activities of these peptide analogs; HPRP-A1 and peptide analogs with relative higher hydrophobicity exerted broad spectrum antimicrobial activity against Gram-negative bacteria, Gram-positive bacteria and pathogenic fungi, but also showed stronger hemolytic activity; the change of hydrophobicity and net charge of peptides had similar effects with close trend and extent on antibacterial activities and antifungal activities. This indicated that there were certain correlations between the antibacterial mode of action and the antifungal mode of action of these peptides in this study. The peptides exhibited antimicrobial specificity for bacteria and fungi, which provided potentials to develop new antimicrobial drugs for clinical practices.展开更多
基金Supported by National Natural Science Foundation of China(30772737)~~
文摘[Objective] This study was to identify the expression of exogenous antimicrobial peptide in transgenic Houttuynia cordata Thunb. plants,and analyze their resistance to stem rot disease. [Methods] SDS-PAGE and Western blot analysis were employed to detect expression of exogenous antimicrobial peptide in transgenic H. cordata plants. Both wild type and transgenic H. cordata plants were inoculated with different concentrations of Rhizoctonia solani spores for detecting their resistance. [Results] The exogenous antimicrobial peptide was detected at translation level. The optimal parameters for detecting the resistance of transgenic H. cordata plants to R. solani was inoculation of spores at a concentration of 3×105 ind./ml and cultured for three days. The results showed that resistance of transgenic H. cordata plants to R. solani was enhanced in comparison with CKs. [Conclusion] Expression of exogenous antimicrobial peptide can enhance the resistance of transgenic H. cordata plants to stem rot disease.
基金Natural Science Foundation of Jilin Province(201015130)the Youth Foundation of Jilin Province (20100126)
文摘HPRP-A1, a 15-mer α-helical cationic peptide, was derived from N-terminus of ribosomal protein L1 (RpL1) of Helicobacter pylori. In this study, HPRP-A1 was used as a framework to obtain a series of peptide analogs with different hydrophobicity by single amino acid substitutions in the center of nonpolar face of the amphipathic helix in order to systematically study the effect of hydrophobicity on biological activities of -helical antimicrobial peptides. Hydrophobicity and net charge of peptides played key roles in the biological activities of these peptide analogs; HPRP-A1 and peptide analogs with relative higher hydrophobicity exerted broad spectrum antimicrobial activity against Gram-negative bacteria, Gram-positive bacteria and pathogenic fungi, but also showed stronger hemolytic activity; the change of hydrophobicity and net charge of peptides had similar effects with close trend and extent on antibacterial activities and antifungal activities. This indicated that there were certain correlations between the antibacterial mode of action and the antifungal mode of action of these peptides in this study. The peptides exhibited antimicrobial specificity for bacteria and fungi, which provided potentials to develop new antimicrobial drugs for clinical practices.
