Related Experiment Video
Updated: May 17, 2026

Identification of Functional Protein Regions Through Chimeric Protein Construction
Published on: January 8, 2019
Characterization of a chimeric antimicrobial peptide uncovers evolutionary significance of exon-shuffling
Kuanyu Zhu1, Bin Gao, Shunyi Zhu
1Group of Animal Innate Immunity, State Key Laboratory of Integrated Management of Pest Insects & Rodents, Institute of Zoology, Chinese Academy of Sciences, 1 Beichen West Road, Chaoyang District, 100101 Beijing, China.
Abstract:
The abaecin family comprises a class of proline-rich antimicrobial peptides (AMPs) with restricted distribution in hymenopteran insects. Intriguingly, in the parasitic wasp Nasonia vitripennis its members (termed nabaecin-1 to -3) have gained a carboxyl terminal glycine-rich antimicrobial unit through exon-shuffling. Here, we describe cDNA cloning of nabaecin-3 and the donor gene (navitripenicin) of the shuffling, and structural and functional features of nabaecin-3 and its two domains (respectively called amino-terminal abaecin unit (NtAU) and carboxyl-terminal navitripenicin unit (CtNU)). Nabaecin-3 and navitripenicin were found to be transcriptionally up-regulated in response to bacterial challenge. By using recombinant expression and chemical synthesis techniques, we produced nabaecin-3, NtAU and CtNU. Circular dichroism (CD) analyses show that these peptides remarkably differ in their structures. Functionally, nabaecin-3 displayed a wide spectrum of antimicrobial activity against an array of bacteria, yeasts and fungi at micromolar concentrations, while CtNU only had a weak antibacterial activity and NtAU completely lacked activity. Our results indicate that in Nasonia the antimicrobial function of abaecin depends on the combination of NtAU with CtNU and thus suggest a new role of exon-shuffling in buffering loss-of-function mutation of a gene.
More Related Videos
Related Concept Videos
Exon Recombination
Exon shuffling follows “splice frame rules.” Each exon has three reading...
Transduction
Leaky Scanning
Protein Complexes with Interchangeable Parts
The SCF ubiquitin ligase is a protein complex of five individual proteins. This complex attaches ubiquitin to other target proteins to mark them for degradation. In order to...
Conservative Site-specific Recombination and Phase Variation
The recognition sites for Cre recombinase called LoxP...
Evolution of New Traits in Microbes

