ArticleCommunications biology2021
ssDNA recombineering boosts in vivo evolution of nanobodies displayed on bacterial surfaces.
Article in Communications biology, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 4 papers.
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Who cites it
4 citing papers in PubMed, 9 citations in OpenAlex.
- Nanobody-based analysis of RhoGTPase stress response inBiotechnology reports (Amsterdam, Netherlands) · 2026Article
- Bacterial surface display of human lectins in Escherichia coli.Microbial biotechnology · 2024Article
- Hypermutation of specific genomic loci of Pseudomonas putida for continuous evolution of target genes.Microbial biotechnology · 2022Article
- Engineering Tropism ofACS synthetic biology · 2021Article
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Authors and funding
8 authors at 3 institutions in 3 countries.
Funding
Abstract
ssDNA recombineering has been exploited to hyperdiversify genomically-encoded nanobodies displayed on the surface of Escherichia coli for originating new binding properties. As a proof-of-principle a nanobody recognizing the antigen TirM from enterohaemorrhagic E. coli (EHEC) was evolved towards the otherwise not recognized TirM antigen from enteropathogenic E. coli (EPEC). To this end, E. coli cells displaying this nanobody fused to the intimin outer membrane-bound domain were subjected to multiple rounds of mutagenic oligonucleotide recombineering targeting the complementarity determining regions (CDRs) of the cognate VHH gene sequence. Binders to the EPEC-TirM were selected upon immunomagnetic capture of bacteria bearing active variants and nanobodies identified with a new ability to strongly bind the new antigen. The results highlight the power of combining evolutionary properties of bacteria in vivo with oligonucleotide synthesis in vitro for the sake of focusing diversification to specific segments of a gene (or protein thereof) of interest.
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