Recombinant human lysozyme expressed in transgenic mouse milk retained full bactericidal activity against E. coli and other pathogens, validating transgenic animal milk as a production platform for antimicrobial proteins.
Key findingRecombinant human lysozyme produced in transgenic mouse milk maintained bactericidal activity equivalent to native human lysozyme, validating mammary
What the researchers found
Recombinant human lysozyme produced in transgenic mouse milk maintained bactericidal activity equivalent to native human lysozyme, validating mammary gland expression as a scalable production platform for bioactive antimicrobial milk proteins.
Why it matters
Relevant for antimicrobial-peptides, peptide-design.
How the study worked
animal-study study on antimicrobial-peptides, peptide-design.
What this study cannot tell us
See abstract.
How to read the evidence
preliminary evidence.
When this study was published
Published in 2006.
The bigger picture
Advances peptide research.
Questions still open
- Further research needed.
- Clinical translation to evaluate.
Common questions
What was studied?
What was found?
Read the original research
Expression and bioactivity of recombinant human lysozyme in the milk of transgenic mice.
Journal of dairy science, 89(8), 2911-8
Citation
Yu, Z; Meng, Q; Yu, H; Fan, B; Yu, S; Fei, J; Wang, L; Dai, Y; Li, N. (2006). Expression and bioactivity of recombinant human lysozyme in the milk of transgenic mice.. Journal of dairy science, 89(8), 2911-8.