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Protein Engineering vol. 4 no. 8 pp. 963-970, 1991
© 1991 Oxford University Press

RESEARCH-ARTICLE

Synthesis and mutagenesis of an IgG-binding protein based upon protein A of Staphylococcus aureus

Andrew G. Popplewell, Micheal G. Gore1, Michael Scawen2 and Tony Atkinson2

Department of Biochemistry, SERC Centre for Molecular Recognition. School of Biological Sciences Basseft Crescent East, University of Southampton, Southampton, SO9 3TU, UK 2Biotechnology Division, PHLS, Centre for Applied Microbiology and Research Porton, Salisbury SP4 0JG, UK

1To whom correspondence should be addressed

A novel protein able to bind with high affinity to the Fc fragment of IgG from a variety of animals has been produced by a gene synthesis approach. The IgG binding is accomplished by the presence of a single or two consecutive domains based upon domain B from protein A of Staphylo-coccus aureus. The IgG-binding moiety is fused to a peptide containing 21, 53 or 81 amino acids derived from the N-terminus of bovine DNase I. The latter is present to guide the expression of the protein in Escherichia coli into an inclusion body. This facilitates the high expression and recovery of the IgG-binding domains. The binding activity of this fusion protein is very close to that of the native protein A. Site-directed mutagenesis of the fusion protein and subsequent identification of changed binding interactions is reported.

Keywords: Fc/immunoglobulins/inclusion body/protein A/protein engineering

Received July 30, 1991; revised September 30, 1991;
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