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Specific recognition of a dsDNA sequence motif by an immunoglobulin V_H homodimer

International Centre for Genetic Engineering and Biotechnology, 34012-Trieste, Italy

(RECEIVED June 9, 2004; FINAL REVISION August 6, 2004; ACCEPTED August 14, 2004)

Anti-DNA antibodies have the potential to be applied in vast fields of fundamental as well as medical research. They are found in autoimmune diseases, such as systemic lupus erythemotosus. In most cases, anti-dsDNA antibodies do not present sequence specificity and are of low affinity. The dominant role of V_H domains in DNA recognition induced us to search for binders based on V_H dimers (VHD), previously reported to bind different protein antigens. We screened a phage displayed homo-VHD library against a 19-bp dsDNA sequence. A sequence-specific binder was selected, which recognizes the terminal located CTGC motif with a K_d of 250 nM. Association of the two identical V_H domains of the molecule was shown to be essential for binding.

Keywords: anti-DNA; VHD; phage display; antibodies

Article published online ahead of print. Article and publication date are at http://www.proteinscience.org/cgi/doi/10.1110/ps.04921704.

Reprint requests to: Oscar R. Burrone, International Centre for Genetic Engineering and Biotechnology, Area Science Park, Padriciano 99, 34012-Trieste, Italy; e-mail: burrone{at}icgeb.org; fax: +39-040-226555.

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