ArticleInternational journal of molecular sciences2016
Insights into the Antimicrobial Mechanism of Action of Human RNase6: Structural Determinants for Bacterial Cell Agglutination and Membrane Permeation.
Article in International journal of molecular sciences, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 30 papers.
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Who cites it
30 citing papers in PubMed, 50 citations in OpenAlex.
- Proteomic Characterization of Bottlenose Dolphin (Journal of proteome research · 2026Article
- The lysosomal catabolism of nucleic acids-critical regulators of the innate immune system.Nucleic acids research · 2025Review
- Ribonucleases of Mice and Men: Unveiling the Roles of the RNase A Superfamily in Host Defence.Journal of immunology research · 2025Review
- Plasma Proteomics Reveals Biomarkers and Undulating Changes in Metabolic Aging.Research (Washington, D.C.) · 2025Article
- Transriptome Analysis of Peripheral Blood Monocytes in Chronic Obstructive Pulmonary Disease Patients.Doklady. Biochemistry and biophysics · 2024Article
- Bacterial RNA sensing by TLR8 requires RNase 6 processing and is inhibited by RNA 2'O-methylation.EMBO reports · 2024Article
- Aggrescan4D: A comprehensive tool for pH-dependent analysis and engineering of protein aggregation propensity.Protein science : a publication of the Protein Society · 2024Review
- Genetic Signatures of Positive Selection in Human Populations Adapted to High Altitude in Papua New Guinea.Genome biology and evolution · 2024Article
- A Common Polymorphism inInternational journal of molecular sciences · 2024Article
- Identification of Ribonuclease 6 as an immunoinflammatory key gene associated with the glomerular injury in diabetic nephropathy.Scientific reports · 2022Article
- Single-cell RNA Sequencing Analysis Reveals New Immune Disorder Complexities in Hypersplenism.Frontiers in immunology · 2022Article
- Structure-Based Design of an RNase Chimera for Antimicrobial Therapy.International journal of molecular sciences · 2021Article
- De novo design of a pH-triggered self-assembled β-hairpin nanopeptide with the dual biological functions for antibacterial and entrapment.Journal of nanobiotechnology · 2021Article
- ELAVL1a is an immunocompetent protein that protects zebrafish embryos from bacterial infection.Communications biology · 2021Article
- Strengths and Challenges of Secretory Ribonucleases as AntiTumor Agents.Pharmaceutics · 2021Review
- The Role of Nucleases and Nucleic Acid Editing Enzymes in the Regulation of Self-Nucleic Acid Sensing.Frontiers in immunology · 2021Review
- Surface adhesion of viruses and bacteria: Defend only and/orMRS advances · 2021Article
- Insights into Structural and Dynamical Changes Experienced by Human RNase 6 upon Ligand Binding.Biochemistry · 2020Article
- Functional roles of the human ribonuclease A superfamily in RNA metabolism and membrane receptor biology.Molecular aspects of medicine · 2019Review
- Insight into the Antifungal Mechanism of Action of Human RNase N-terminus Derived Peptides.International journal of molecular sciences · 2019Article
Corrections and comments
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Authors and funding
7 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Human Ribonuclease 6 is a secreted protein belonging to the ribonuclease A (RNaseA) superfamily, a vertebrate specific family suggested to arise with an ancestral host defense role. Tissue distribution analysis revealed its expression in innate cell types, showing abundance in monocytes and neutrophils. Recent evidence of induction of the protein expression by bacterial infection suggested an antipathogen function in vivo. In our laboratory, the antimicrobial properties of the protein have been evaluated against Gram-negative and Gram-positive species and its mechanism of action was characterized using a membrane model. Interestingly, our results indicate that RNase6, as previously reported for RNase3, is able to specifically agglutinate Gram-negative bacteria as a main trait of its antimicrobial activity. Moreover, a side by side comparative analysis with the RN6(1-45) derived peptide highlights that the antimicrobial activity is mostly retained at the protein N-terminus. Further work by site directed mutagenesis and structural analysis has identified two residues involved in the protein antimicrobial action (Trp1 and Ile13) that are essential for the cell agglutination properties. This is the first structure-functional characterization of RNase6 antimicrobial properties, supporting its contribution to the infection focus clearance.
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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.