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J Biol Chem, Vol. 274, Issue 21, 14521-14524, May 21, 1999
,,
From the Surface proteins that bind to the Fc part of
human IgA are expressed by many strains of Streptococcus
pyogenes, a major human pathogen. Studies of these proteins have
been complicated by their size and by their ability to bind human
plasma proteins other than IgA. Here, we describe a synthetic
50-residue peptide, derived from streptococcal protein Sir22, that
binds human IgA but not any of the other plasma proteins known to bind
to Sir22. The peptide binds serum IgA and secretory IgA and binds IgA
of both subclasses. Evidence is presented that the peptide folds
correctly both in solution and when it is immobilized and that it
readily renatures after denaturation. Together, these data indicate
that the peptide corresponds to a protein domain that binds IgA with
high specificity. This is the first report of an IgA-binding domain
that retains its properties in isolated form.
Department of Laboratory Medicine, Lund
University, Sölvegatan 23, S-223 62 Lund, Sweden and the
§ Department of Microbiology, University of Alabama at
Birmingham, Birmingham, Alabama, 35294
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