ArticlePLoS pathogens2013
Identification of a novel antimicrobial peptide from human hepatitis B virus core protein arginine-rich domain (ARD).
Article in PLoS pathogens, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 27 papers.
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Who cites it
27 citing papers in PubMed, 49 citations in OpenAlex.
- Molecular insights into domestic cat hepatitis B virus linking genome to function.Veterinary research communications · 2026Article
- Antibacterial Efficacy of Chlamydomonas reinhardtii-Expressed Enterocin RM6 Against Gram-Positive and Gram-Negative Bacteria.Probiotics and antimicrobial proteins · 2026Article
- Progress in the classification, optimization, activity, and application of antimicrobial peptides.Frontiers in microbiology · 2025Review
- In Silico and In vitro Evaluations of the Antibacterial Activities of HIV-1 Nef Peptides againstInternational journal of molecular and cellular medicine · 2024Article
- A Novel Antimicrobial Peptide Derived from Bony Fish IFN1 Exerts Potent Antimicrobial and Anti-Inflammatory Activity in Mammals.Microbiology spectrum · 2022Article
- Identification of a Novel Antimicrobial Peptide From the Ancient Marine Arthropod Chinese Horseshoe Crab,Frontiers in immunology · 2022Article
- PaP1, a Broad-Spectrum Lysin-Derived Cationic Peptide to Treat Polymicrobial Skin Infections.Frontiers in microbiology · 2022Article
- PCL-1, a Trypsin-Resistant Peptide, Exerts Potent Activity Against Drug-Resistant Bacteria.Probiotics and antimicrobial proteins · 2021Article
- Anticancer activity of pyrimidodiazepines based on 2-chloro-4-anilinoquinazoline: synthesis, DNA binding and molecular docking.RSC advances · 2021Article
- In Vitro Evaluation of the Potential Pharmacological Activity and Molecular Targets of New Benzimidazole-Based Schiff Base Metal Complexes.Antibiotics (Basel, Switzerland) · 2021Article
- A nematode-derived, mitochondrial stress signaling-regulated peptide exhibits broad antibacterial activity.Biology open · 2021Article
- Fine-Tuning of Alkaline Residues on the Hydrophilic Face Provides a Non-toxic Cationic α-Helical Antimicrobial Peptide Against Antibiotic-Resistant ESKAPE Pathogens.Frontiers in microbiology · 2021Article
- Antibacterial Activity of a Cationic Antimicrobial Peptide against Multidrug-Resistant Gram-Negative Clinical Isolates and Their Potential Molecular Targets.Molecules (Basel, Switzerland) · 2020Article
- Cathelicidin-DM is an Antimicrobial Peptide fromACS omega · 2020Article
- Gram-Negative Bacterial Lysins.Antibiotics (Basel, Switzerland) · 2020Review
- Antimicrobial Peptide JH-3 Effectively Kills Salmonella enterica Serovar Typhimurium Strain CVCC541 and Reduces Its Pathogenicity in Mice.Probiotics and antimicrobial proteins · 2019Article
- Mechanism of action of antimicrobial peptide P5 truncations against Pseudomonas aeruginosa and Staphylococcus aureus.AMB Express · 2019Article
- Adding a C-terminal Cysteine (CTC) Can Enhance the Bactericidal Activity of Three Different Antimicrobial Peptides.Frontiers in microbiology · 2018Article
- The therapeutic applications of antimicrobial peptides (AMPs): a patent review.Journal of microbiology (Seoul, Korea) · 2017Review
- New Potent Membrane-Targeting Antibacterial Peptides from Viral Capsid Proteins.Frontiers in microbiology · 2017Article
Corrections and comments
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Authors and funding
9 authors at 7 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The rise of multidrug-resistant (MDR) pathogens causes an increasing challenge to public health. Antimicrobial peptides are considered a possible solution to this problem. HBV core protein (HBc) contains an arginine-rich domain (ARD) at its C-terminus, which consists of 16 arginine residues separated into four clusters (ARD I to IV). In this study, we demonstrated that the peptide containing the full-length ARD I-IV (HBc147-183) has a broad-spectrum antimicrobial activity at micro-molar concentrations, including some MDR and colistin (polymyxin E)-resistant Acinetobacter baumannii. Furthermore, confocal fluorescence microscopy and SYTOX Green uptake assay indicated that this peptide killed Gram-negative and Gram-positive bacteria by membrane permeabilization or DNA binding. In addition, peptide ARD II-IV (HBc153-176) and ARD I-III (HBc147-167) were found to be necessary and sufficient for the activity against P. aeruginosa and K. peumoniae. The antimicrobial activity of HBc ARD peptides can be attenuated by the addition of LPS. HBc ARD peptide was shown to be capable of direct binding to the Lipid A of lipopolysaccharide (LPS) in several in vitro binding assays. Peptide ARD I-IV (HBc147-183) had no detectable cytotoxicity in various tissue culture systems and a mouse animal model. In the mouse model by intraperitoneal (i.p.) inoculation with Staphylococcus aureus, timely treatment by i.p. injection with ARD peptide resulted in 100-fold reduction of bacteria load in blood, liver and spleen, as well as 100% protection of inoculated animals from death. If peptide was injected when bacterial load in the blood reached its peak, the protection rate dropped to 40%. Similar results were observed in K. peumoniae using an IVIS imaging system. The finding of anti-microbial HBc ARD is discussed in the context of commensal gut microbiota, development of intrahepatic anti-viral immunity and establishment of chronic infection with HBV. Our current results suggested that HBc ARD could be a new promising antimicrobial peptide.
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