ArticlePLoS pathogens2014
Delineation of interfaces on human alpha-defensins critical for human adenovirus and human papillomavirus inhibition.
Article in PLoS pathogens, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 35 papers.
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Who cites it
35 citing papers in PubMed.
- Human alpha-defensin 5 stabilizes the enterovirus A71 capsid and blocks infection.bioRxiv : the preprint server for biology · 2026Article
- Systemic removal of host restriction factors enables rapid, scalable virus production for cell culture-based vaccine development.Frontiers in bioengineering and biotechnology · 2026Article
- Human neutrophil α-defensin HNP1 interacts with bacterial cell wall components to promote biofilm formation byBiofilm · 2025Article
- Mechanisms of AAV neutralization by human alpha-defensins.PLoS pathogens · 2025Article
- Human neutrophil α-defensin HNP1 interacts with bacterial OmpA to promote Acinetobacter baumannii biofilm formation.Nature communications · 2025Article
- Human Defensins: Structure, Function, and Potential as Therapeutic Antimicrobial Agents with Highlights Against SARS CoV-2.Probiotics and antimicrobial proteins · 2025Review
- Effect of Nk-lysin peptides on bacterial growth, MIC, antimicrobial resistance, and viral activities.Animal biotechnology · 2024Article
- Lung antimicrobial proteins and peptides: from host defense to therapeutic strategies.Physiological reviews · 2024Review
- Understanding the Dynamics of Human Defensin Antimicrobial Peptides: Pathogen Resistance and Commensal Induction.Applied biochemistry and biotechnology · 2024Review
- Alpha-defensin binding expands human adenovirus tropism.PLoS pathogens · 2024Article
- A Single Surface-Exposed Amino Acid Determines Differential Neutralization of AAV1 and AAV6 by Human Alpha-Defensins.Journal of virology · 2023Article
- Roles of Antimicrobial Peptides in Gynecological Cancers.International journal of molecular sciences · 2022Review
- VP4 Is a Determinant of Alpha-Defensin Modulation of Rotaviral Infection.Journal of virology · 2022Article
- Adenovirus-α-Defensin Complexes Induce NLRP3-Associated Maturation of Human Phagocytes via Toll-Like Receptor 4 Engagement.Journal of virology · 2022Article
- Inflammation, immunity and potential target therapy of SARS-COV-2: A total scale analysis review.Food and chemical toxicology : an international journal published for the British Industrial Biological Research Association · 2021Review
- Defensin-driven viral evolution.PLoS pathogens · 2020Article
- Antimicrobial host defence peptides: functions and clinical potential.Nature reviews. Drug discovery · 2020Review
- Defensins: A Double-Edged Sword in Host Immunity.Frontiers in immunology · 2020Review
- Antiviral Activities of Human Host Defense Peptides.Current medicinal chemistry · 2020Review
- Human Enteric Defensin 5 PromotesInfection and immunity · 2019Article
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Authors and funding
5 authors.
Funding
Abstract
Human α-defensins are potent anti-microbial peptides with the ability to neutralize bacterial and viral targets. Single alanine mutagenesis has been used to identify determinants of anti-bacterial activity and binding to bacterial proteins such as anthrax lethal factor. Similar analyses of α-defensin interactions with non-enveloped viruses are limited. We used a comprehensive set of human α-defensin 5 (HD5) and human neutrophil peptide 1 (HNP1) alanine scan mutants in a combination of binding and neutralization assays with human adenovirus (AdV) and human papillomavirus (HPV). We have identified a core of critical hydrophobic residues that are common determinants for all of the virus-defensin interactions that were analyzed, while specificity in viral recognition is conferred by specific surface-exposed charged residues. The hydrophobic residues serve multiple roles in maintaining the tertiary and quaternary structure of the defensins as well as forming an interface for virus binding. Many of the important solvent-exposed residues of HD5 group together to form a critical surface. However, a single discrete binding face was not identified for HNP1. In lieu of whole AdV, we used a recombinant capsid subunit comprised of penton base and fiber in quantitative binding studies and determined that the anti-viral potency of HD5 was a function of stoichiometry rather than affinity. Our studies support a mechanism in which α-defensins depend on hydrophobic and charge-charge interactions to bind at high copy number to these non-enveloped viruses to neutralize infection and provide insight into properties that guide α-defensin anti-viral activity.
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