Recent studies have shown that polyspecific antibodies play an important role in the frontline defense against the dissemination of pathogens in the pre-immune host. Interestingly, antigen-binding polyspecificity can not only be inherent, but also acquired post-translationally. The ability of individual monoclonal IgE and IgG antibodies to acquire polyspecificity following contact with protein-modifying agents has been studied in detail. However, to the best of our knowledge this property of human IgA has previously been described only cursorily. In the present study pooled human serum IgA and two monoclonal IgA antibodies were exposed to buffers with acidic pH, to free heme or to pro-oxidative ferrous ions, and the antigen-binding behavior of the native and modified IgA to viral and bacterial antigens were compared using Western blotting and ELISA. We observed a dose-dependent increase in reactivity to several bacterial extracts and to pure viral antigens. This newly described property of IgA may have therapeutic potential as has already been shown for pooled IgG with induced polyspecificity.