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Departments of
* Medical Microbiology, Dermatology and Infection and
Biophysical Chemistry, Lund University, Lund, Sweden;
Department of Molecular and Cellular Pathology, University of Dundee Medical School, Ninewells Hospital, Dundee, United Kingdom; and
Department of Oral Biology, Royal Dental College, University of Aarhus, Aarhus, Denmark
Bacterial proteins that bind to the Fc part of IgG have found
widespread use in immunology. A similar protein suitable for the
isolation and detection of human IgA has not been described. Here, we
show that a 50-residue synthetic peptide, designated streptococcal
IgA-binding peptide (Sap) and derived from a streptococcal M protein,
can be used for single-step affinity purification of human IgA. High
affinity binding of IgA required the presence in Sap of a C-terminal
cysteine residue, not present in the intact M protein. Passage of human
serum through a Sap column caused depletion of >99% of the IgA, and
elution of the column allowed quantitative recovery of highly purified
IgA, for which the proportions of the IgA1 and IgA2 subclasses were the
same as in whole serum. Moreover, immobilized Sap could be used for
single-step purification of secretory IgA of both subclasses from human
saliva, with a recovery of 
45%. The Sap peptide could also be used
to specifically detect IgA bound to Ag. Together, these data indicate
that Sap is a versatile Fc-binding reagent that may open new
possibilities for the characterization of human
IgA.
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