ArticlePloS one2013
Single, double and quadruple alanine substitutions at oligomeric interfaces identify hydrophobicity as the key determinant of human neutrophil alpha defensin HNP1 function.
Article in PloS one, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 15 papers.
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Who cites it
15 citing papers in PubMed, 33 citations in OpenAlex.
- Human neutrophil α-defensin HNP1 interacts with bacterial cell wall components to promote biofilm formation byBiofilm · 2025Article
- Human neutrophil α-defensin HNP1 interacts with bacterial OmpA to promote Acinetobacter baumannii biofilm formation.Nature communications · 2025Article
- Exploring the potential of anticancer peptides as therapeutic agents for cancer treatment.Research in pharmaceutical sciences · 2025Review
- Enhancement of the activity of the antimicrobial peptides HNP1 and LL-37 by bovine pancreatic ribonuclease A.F1000Research · 2022Article
- Endogenous Peptide Inhibitors of HIV Entry.Advances in experimental medicine and biology · 2022Article
- Antiviral Activities of Human Host Defense Peptides.Current medicinal chemistry · 2020Review
- High-Throughput Quantification of Bacterial-Cell Interactions Using Virtual Colony Counts.Frontiers in cellular and infection microbiology · 2018Article
- Targeting and inactivation of bacterial toxins by human defensins.Biological chemistry · 2017Review
- Cyclic Peptides as Novel Therapeutic Microbicides: Engineering of Human Defensin Mimetics.Molecules (Basel, Switzerland) · 2017Review
- Thermodynamic instability of viral proteins is a pathogen-associated molecular pattern targeted by human defensins.Scientific reports · 2016Article
- Article
- Quantification of polysaccharides fixed to Gram stained slides using lactophenol cotton blue and digital image processing.F1000Research · 2015Article
- Human defensins facilitate local unfolding of thermodynamically unstable regions of bacterial protein toxins.Immunity · 2014Article
- Safety, efficacy and utility of methods of transferring adhesive and cohesive Escherichia coli cells to microplates to avoid aerosols.F1000Research · 2014Article
- Cationic host defense peptides; novel antimicrobial therapeutics against Category A pathogens and emerging infections.Pathogens and global healthReview
Corrections and comments
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Authors and funding
9 authors at 2 institutions in 2 countries.
Funding
Abstract
HNP1 is a human alpha defensin that forms dimers and multimers governed by hydrophobic residues, including Tyr¹⁶, Ile²⁰, Leu²⁵, and Phe²⁸. Previously, alanine scanning mutagenesis identified each of these residues and other hydrophobic residues as important for function. Here we report further structural and functional studies of residues shown to interact with one another across oligomeric interfaces: I20A-HNP1 and L25A-HNP1, plus the double alanine mutants I20A/L25A-HNP1 and Y16A/F28A-HNP1, and the quadruple alanine mutant Y16A/I20A/L25A/F28A-HNP1. We tested binding to HIV-1 gp120 and HNP1 by surface plasmon resonance, binding to HIV-1 gp41 and HNP1 by fluorescence polarization, inhibition of anthrax lethal factor, and antibacterial activity using the virtual colony count assay. Similar to the previously described single mutant W26A-HNP1, the quadruple mutant displayed the least activity in all functional assays, followed by the double mutant Y16A/F28A-HNP1. The effects of the L25A and I20A single mutations were milder than the double mutant I20A/L25A-HNP1. Crystallographic studies confirmed the correct folding and disulfide pairing, and depicted an array of dimeric and tetrameric structures. These results indicate that side chain hydrophobicity is the critical factor that determines activity at these positions.
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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.