ArticleMolecules (Basel, Switzerland)2019
Fusion of Lysostaphin to an Albumin Binding Domain Prolongs Its Half-Life and Bactericidal Activity in the Systemic Circulation.
Article in Molecules (Basel, Switzerland), 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.
What it found
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
The trial behind it
Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
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Who cites it
8 citing papers in PubMed, 16 citations in OpenAlex.
- EV-LYSG101: Extracellular Vesicles Loaded With Lysin LYSG101 for Potent Anti-Staphylococcal Activity.Journal of extracellular biology · 2026Article
- A chimeric, half-life extended lysin with a unique mode of action.Frontiers in microbiology · 2026Article
- Nanocarrier-based immunotherapy for viral diseases.International journal of pharmaceutics: X · 2025Review
- Modifying Pharmacokinetic Properties of the Gram-Negative Bacteria Targeting Endolysin ML06 Without Affecting Antibacterial Activity.International journal of molecular sciences · 2025Article
- Antibacterial and Anti-Biofilm Properties of Diopside Powder Loaded with Lysostaphin.Pathogens (Basel, Switzerland) · 2023Article
- Efficacy of Phage- and Bacteriocin-Based Therapies in Combatting Nosocomial MRSA Infections.Frontiers in molecular biosciences · 2021Review
- Article
- Structure-activity analysis of truncated albumin-binding domains suggests new lead constructs for potential therapeutic delivery.The Journal of biological chemistry · 2020Article
Corrections and comments
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Authors and funding
14 authors at 4 institutions in 1 country.
Funding
Abstract
Antibacterial lysins are promising proteins that are active against both antibiotic-susceptible and antibiotic-resistant bacterial strains. However, a major limitation of antibacterial lysins is their fast elimination from systemic circulation. PEGylation increases the plasma half-life of lysins but renders them inactive. Here we report the construction of a fusion protein of lysostaphin, a potent anti-staphylococcal lysin, and an albumin-binding domain from streptococcal protein G. The resulting fusion protein was less active than the parent enzyme lysostaphin, but it still retained significant antibacterial activity even when bound to serum albumin. The terminal half-life of the fusion protein in rats was five-fold greater than that of lysostaphin (7.4 vs. 1.5 h), and the area under the curve increased more than 115 times. Most importantly, this increase in systemic circulation time compensated for the decrease in activity. The plasma from rats that received an injection of the fusion protein retained bactericidal activity for up to 7 h, while plasma from rats that received plain lysostaphin lacked any detectable activity after 4 h. To the best of our knowledge, this is the first report of an antibacterial lysin with both improved pharmacokinetic parameters and prolonged bactericidal activity in the systemic circulation.
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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.