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Targeting diversity

Nature Structural & Molecular Biology volume 12, pages 830–831 (2005)Cite this article

A bacteriophage has a mechanism for producing a family of receptor-binding proteins that rivals the immunoglobulins in diversity.

To change specificity, the Bordetella phage has evolved a diversity-generating mechanism that achieves a result similar to diversity in the antigen-binding site of immunoglobulins but uses a genetically distinct strategy2 (Fig. 1a). The receptor-binding protein is encoded by the locus designated the major tropism determinant (Mtd). A copy of just a short sequence of the gene, the variable region, is selectively mutagenized in a cycle of transcription into RNA followed by retrotranscription by a phage-encoded reverse transcriptase. During this process, adenine residues are changed at a high frequency to any of the other nucleotides. The modified variable region is then inserted back into the functional mtd gene. By selectively targeting adenines, this mechanism ensures that amino acids encoded by codons lacking adenine are invariant. At the same time, the high frequency of changes to adenine residues has the potential to generate enormous diversity at amino acid positions in which adenine forms part of the codon. This mechanism of mutagenizing just adenines in a restricted segment of the gene allows essentially pinpoint accuracy, targeting the variability to a specific set of amino acids and leaving the adjacent residues unchanged.

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Figure 1: Variability of the receptor-binding protein of Bordetella phage, expressed from the mtd locus.

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  1. Division of Molecular Biosciences, Imperial College London, London, SW7 2AZ, UK

    Kurt Drickamer & Maureen E Taylor

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  1. Kurt Drickamer
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  2. Maureen E Taylor
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Drickamer, K., Taylor, M. Targeting diversity. Nat Struct Mol Biol 12, 830–831 (2005). https://doi.org/10.1038/nsmb1005-830

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