ArticleScientific reports2021
Sequence edition of single domains modulates the final immune and antimicrobial potential of a new generation of multidomain recombinant proteins.
Article in Scientific reports, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 3 papers.
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Who cites it
3 citing papers in PubMed, 4 citations in OpenAlex.
- Exploring the therapeutic potential of recombinant bovine β-defensins for antimicrobial and anti-inflammatory functions in sepsis management.Veterinary research · 2025Article
- Time to consider ruling out inclusion bodies denaturing protocols for spontaneous solubilization of biologically active proteins.Scientific reports · 2024Article
- The future of recombinant host defense peptides.Microbial cell factories · 2022Review
Corrections and comments
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Authors and funding
8 authors at 2 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Combining several innate immune peptides into a single recombinant antimicrobial and immunomodulatory polypeptide has been recently demonstrated. However, the versatility of the multidomain design, the role that each domain plays and how the sequence edition of the different domains affects their final protein activity is unknown. Parental multidomain antimicrobial and immunomodulatory protein JAMF1 and several protein variants (JAMF1.2, JAMF2 and AM2) have been designed and recombinantly produced to explore how the tuning of domain sequences affects their immunomodulatory potential in epithelial cells and their antimicrobial capacity against Gram-positive and Gram-negative bacteria. The replacement of the sequence of defensin HD5 and phospholipase sPLA
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