The AID enzyme induces class switch recombination in fibroblasts

Il-mi Okazaki, Kazuo Kinoshita, Masamichi Muramatsu, Kiyotsugu Yoshikawa and Tasuku Honjo ()
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Il-mi Okazaki: Graduate School of Medicine, Kyoto University
Kazuo Kinoshita: Graduate School of Medicine, Kyoto University
Masamichi Muramatsu: Graduate School of Medicine, Kyoto University
Kiyotsugu Yoshikawa: Graduate School of Medicine, Kyoto University
Tasuku Honjo: Graduate School of Medicine, Kyoto University

Nature, 2002, vol. 416, issue 6878, 340-345

Abstract: Abstract The switch of the immunoglobulin isotype from IgM to IgG, IgE or IgA is mediated by class switch recombination (CSR). CSR changes the immunoglobulin heavy chain constant region (CH) gene from Cμ to one of the other CH genes1,2. Somatic hypermutation introduces massive numbers of point mutations in the immunoglobulin variable (V) region gene, giving rise to immunoglobulin with higher affinity3. Activation-induced cytidine deaminase (AID), a putative RNA-editing cytidine deaminase, is expressed strictly in activated B cells and is indispensable in both CSR and somatic hypermutation4,5. But the exact function of AID is unknown. Here we show that ectopic expression of AID induces CSR in an artificial switch construct in fibroblasts at a level comparable to that in stimulated B cells. Sequences around recombination junctions in the artificial substrate have features similar to endogenous CSR junctions. Furthermore, AID-induced CSR in fibroblasts is dependent on transcription of the target S region, as shown in endogenous CSR in B cells. The results show that AID is the only B-cell-specific factor required for initiation of the CSR reaction in the activated locus.

Date: 2002
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DOI: 10.1038/nature727

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