ArticleMicrobial cell factories2020
A new generation of recombinant polypeptides combines multiple protein domains for effective antimicrobial activity.
Article in Microbial cell factories, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 16 papers.
What it found
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The trial behind it
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Who cites it
16 citing papers in PubMed, 31 citations in OpenAlex.
- Potential of inclusion bodies for disease control in aquaculture and livestock.Veterinary and animal science · 2026Review
- The p40 fusion domain as a scaffold for producing functional inclusion bodies.Applied microbiology and biotechnology · 2026Article
- Recombinant production of antimicrobial proteins in bacterial expression systems: Escherichia coli vs. lactic acid bacteria.Microbial cell factories · 2025Review
- Antimicrobial Peptides: Mechanism, Expressions, and Optimization Strategies.Probiotics and antimicrobial proteins · 2025Review
- Advancements in antiviral approaches against foot-and-mouth disease virus: a comprehensive review.Frontiers in veterinary science · 2025Review
- Cathelicidins: Opportunities and Challenges in Skin Therapeutics and Clinical Translation.Antibiotics (Basel, Switzerland) · 2024Review
- Time to consider ruling out inclusion bodies denaturing protocols for spontaneous solubilization of biologically active proteins.Scientific reports · 2024Article
- Immunomodulation Evidence of Nanostructured Recombinant Proteins in Salmonid Cells.Animals : an open access journal from MDPI · 2024Article
- Lactiplantibacillus plantarum: a new example of inclusion body producing bacteria.Microbial cell factories · 2023Article
- A Novel Generation of Tailored Antimicrobial Drugs Based on Recombinant Multidomain Proteins.Pharmaceutics · 2023Article
- The future of recombinant host defense peptides.Microbial cell factories · 2022Review
- The dual interaction of antimicrobial peptides on bacteria and cancer cells; mechanism of action and therapeutic strategies of nanostructures.Microbial cell factories · 2022Review
- Exploring the impact of the recombinant Escherichia coli strain on defensins antimicrobial activity: BL21 versus Origami strain.Microbial cell factories · 2022Article
- Sequence edition of single domains modulates the final immune and antimicrobial potential of a new generation of multidomain recombinant proteins.Scientific reports · 2021Article
- Coiled-Coil Based Inclusion Bodies and Their Potential Applications.Frontiers in bioengineering and biotechnology · 2021Review
- Exploring the use of leucine zippers for the generation of a new class of inclusion bodies for pharma and biotechnological applications.Microbial cell factories · 2020Article
Corrections and comments
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Authors and funding
5 authors at 1 institution in 1 country.
Funding
Abstract
backgroundAlthough most of antimicrobial peptides (AMPs), being relatively short, are produced by chemical synthesis, several AMPs have been produced using recombinant technology. However, AMPs could be cytotoxic to the producer cell, and if small they can be easily degraded. The objective of this study was to produce a multidomain antimicrobial protein based on recombinant protein nanoclusters to increase the yield, stability and effectivity.
resultsA single antimicrobial polypeptide JAMF1 that combines three functional domains based on human α-defensin-5, human XII-A secreted phospholipase A2 (sPLA
conclusionsOur findings demonstrated that multidomain antimicrobial proteins forming nanoclusters can be efficiently produced in recombinant bacteria, being a novel and valuable strategy to create a versatile, highly stable and easily editable multidomain constructs with a broad-spectrum antimicrobial activity in both soluble and nanostructured format.
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What OpenQuestion holds
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.