ArticlePlant molecular biology2000
Characterization and cDNA cloning of two glycine- and histidine-rich antimicrobial peptides from the roots of shepherd's purse, Capsella bursa-pastoris.
Article in Plant molecular biology, 2000. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 44 papers.
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Who cites it
44 citing papers in PubMed.
- Recent Advances in Antimicrobial Proteins and Peptides: A Promising Clinical Breakthrough and Patent Landscape.Current protein & peptide science · 2026Review
- Shepherin II Gene Synthesis and Peptide Characterization:Protein and peptide letters · 2025Article
- Antimicrobial Plant Peptides: Structure, Classification, Mechanism and Therapeutic Potential.Current topics in medicinal chemistry · 2025Review
- Transcriptome and Gene Expression Analysis RevealedInternational journal of molecular sciences · 2024Article
- Microbial- and Plant-Derived Bioactive Peptides and Their Applications against Foodborne Pathogens: Current Status and Future Prospects.International journal of microbiology · 2024Review
- Glycine-rich peptides from fermented Chenopodium formosanum sprout as an antioxidant to modulate the oxidative stress.Journal of food and drug analysis · 2023Article
- Zn(II) Induces Fibril Formation and Antifungal Activity in Shepherin I, An Antimicrobial Peptide fromInorganic chemistry · 2023Article
- Comprehensive transcriptome analyses of3 Biotech · 2023Article
- Phytochemical Constituents from the Seeds of Capsella bursa-pastoris and Their Antioxidant Activities.Plant foods for human nutrition (Dordrecht, Netherlands) · 2023Article
- The antimicrobial peptide database is 20 years old: Recent developments and future directions.Protein science : a publication of the Protein Society · 2023Article
- Diversity of Cationic Antimicrobial Peptides in Black Cumin (International journal of molecular sciences · 2023Article
- Plant Antimicrobial Peptides: Insights into Structure-Function Relationships for Practical Applications.Current issues in molecular biology · 2023Review
- The Synergy between Zinc and Antimicrobial Peptides: An Insight into Unique Bioinorganic Interactions.Molecules (Basel, Switzerland) · 2023Review
- The Updated Review on Plant Peptides and Their Applications in Human Health.International journal of peptide research and therapeutics · 2022Review
- Antimicrobial Peptides: An Update on Classifications and Databases.International journal of molecular sciences · 2021Review
- A cell wall-localized glycine-rich protein of dodder acts as pathogen-associated molecular pattern.Communicative & integrative biology · 2021Article
- Histidine-Rich Defensins from theJournal of fungi (Basel, Switzerland) · 2020Article
- Article
- Isolation of antimicrobial peptides from different plant sources: Does a general extraction method exist?Plant methods · 2020Review
- A Commensal Dipeptidyl Aminopeptidase with Specificity for N-Terminal Glycine Degrades Human-Produced Antimicrobial Peptides in Vitro.ACS chemical biology · 2018Article
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Authors and funding
6 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Two novel antimicrobial peptides were isolated and characterized from the roots of shepherd's purse, Capsella bursa-pastoris. These antimicrobial peptides, named shepherin I and shepherin II, consist of 28 and 38 amino acids, respectively, and are glycine- and histidine-rich peptides. Shepherin I and shepherin II have 67.9% and 65.8% (mol/mol) glycine, respectively, and 28.6% and 21.1% (mol/mol) histidine, respectively. Both shepherins have a Gly-Gly-His motif. These antimicrobial peptides exhibit antimicrobial activity against Gram-negative bacteria and fungi. Circular dichroism spectra of shepherin I and shepherin II showed that shepherin I and shepherin II in 50% trifluoroethanol have 66.7% and 75% random coils, respectively, without any alpha-helices. cDNA sequence analysis revealed that shepherin I and shepherin II are produced from a single polypeptide, designated shep-GRP, consisting of 120 amino acids; shep-GRP has five distinct domains, an amino-terminal putative signal peptide, a shepherin I, a linker dipeptide, a shepherin II and a carboxy-terminal peptide. Southern blot analysis indicates that the gene encoding shepherins belongs to a low-complexity gene family. Northern blot analysis revealed that transcripts of shep-GRP are present in roots but not in leaves and stems.
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Registered trials
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