ArticlePathogens & immunity2019
α-Defensin HD5 Stabilizes
Article in Pathogens & immunity, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 papers.
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Who cites it
14 citing papers in PubMed, 20 citations in OpenAlex.
- Human alpha-defensin 5 stabilizes the enterovirus A71 capsid and blocks infection.bioRxiv : the preprint server for biology · 2026Article
- Next-generation antiviral peptides: AI-driven design, translational delivery platforms, and future therapeutic directions.Virus research · 2025Review
- Review
- Understanding the Dynamics of Human Defensin Antimicrobial Peptides: Pathogen Resistance and Commensal Induction.Applied biochemistry and biotechnology · 2024Review
- Defensins: defenders of human reproductive health.Human reproduction update · 2023Review
- 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
- HPV16 Entry into Epithelial Cells: Running a Gauntlet.Viruses · 2021Review
- Recent Advances in Our Understanding of the Infectious Entry Pathway of Human Papillomavirus Type 16.Microorganisms · 2021Review
- Defensin-driven viral evolution.PLoS pathogens · 2020Article
- Inferring Virus-Host relationship between HPV and its host Homo sapiens using protein interaction network.Scientific reports · 2020Article
- The Interplay between Antiviral Signalling and Carcinogenesis in Human Papillomavirus Infections.Cancers · 2020Review
- Theta-Defensins Inhibit High-Risk Human Papillomavirus Infection Through Charge-Driven Capsid Clustering.Frontiers in immunology · 2020Article
- Defensins: A Double-Edged Sword in Host Immunity.Frontiers in immunology · 2020Review
Corrections and comments
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Authors and funding
5 authors at 2 institutions in 1 country.
Funding
Abstract
background
methodsWe have used cryo-electron microscopy (cryoEM), mass spectrometry (MS) crosslinking and differential lysine modification studies, and molecular dynamics (MD) simulations to probe the interaction of HPV16 pseudovirions (PsVs) with HD5.
resultsCryoEM single particle reconstruction did not reveal HD5 density on the capsid surface. Rather, increased density was observed under the capsid shell in the presence of HD5. MS studies indicate that HD5 binds near the L1 and L2 capsid proteins and specifically near the C-terminal region of L1. MD simulations indicate that favorable electrostatic interactions can be formed between HD5 and the L1 C-terminal tail.
conclusionsA model is presented for how HD5 affects HPV16 structure and cell entry. In this model, HD5 binds to disordered regions of L1 and L2 protruding from the icosahedrally ordered capsid. HD5 acts to cement interactions between L1 and L2 and leads to a closer association of the L2/genome core with the L1 capsid. This model provides a structural rationale for our prior observation that HD5 interferes with the separation of L1 from the L2/genome complex during cell entry. GRAPHICAL ABSTRACT:
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.