ArticleMolecular biology reports2011
Molecular analysis and recombinant expression of bovine neutrophil β-defensin 12 and its antimicrobial activity.
Article in Molecular biology reports, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 5 papers.
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Who cites it
5 citing papers in PubMed, 17 citations in OpenAlex.
- Exploring the therapeutic potential of recombinant bovine β-defensins for antimicrobial and anti-inflammatory functions in sepsis management.Veterinary research · 2025Article
- Evaluating Host Defense Peptides: A Comparative Analysis of Synthetic Peptides and Recombinant Concatemers.Biomolecules · 2025Article
- Influence of maternal nutrition and one-carbon metabolites supplementation on bovine antimicrobial peptides in fetal and maternal tissues.Frontiers in veterinary science · 2024Article
- Expression, Regulation, and Function of β-Defensins in the Bovine Mammary Glands: Current Knowledge and Future Perspectives.Animals : an open access journal from MDPI · 2023Review
- Exploring the pharmacological potential of promiscuous host-defense peptides: from natural screenings to biotechnological applications.Frontiers in microbiology · 2011Article
Corrections and comments
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Authors and funding
7 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
To analyze molecular characteristics and antimicrobial activity of bovine neutrophil β-defensin 12 (BNBD12), Pro-BNBD12 gene was amplified from Chinese Holstein cow using reverse transcription polymerase chain reaction. Based on the sequence of mature BNBD12 and codon preference in E. coli, a modified mature BNBD12 cDNA was synthesized, cloned into pET32a (+) vector and expressed in E. coli BL21 as a 26 kD fusion protein after isopropyl β-D-1-thiogalactopyranoside induction. The expressed mature BNBD12 accounted for 21.4% of total protein. 0.05 mg/ml purified BNBD12 had antimicrobial activity against both E. coli and S. aureus in vitro assayed by agar diffusion method. Electron microscopy found that BNBD12 treatment of E. coli and S. aureus could induce cell content leakage. Taking together, BNBD12 protein was successfully expressed in E. coli and it has antimicrobial activity against both Gram-positive and negative bacteria and potentials in control of mastitis clinically.
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