Staphylococcus aureus is a robust organism that deploys an array of toxins and virulence factors to assist in its colonisation and survival. Arguably the best known virulence factors are the toxic shock inducing superantigens, which target the immunological synapse between Antigen Presenting Cells and T cells by binding to Major Histocompatibility Complex (MHC) Class II and T cell Receptor; stimulating large numbers of T cells in an antigen independent manner. One prominent feature of the superantigen family is their conserved two domain structure, which is also to be shared by 14 superantigen-like proteins called the SSLs. The ssl genes are clustered on a pathogenicity island and their expression seems to be regulated by factors that sense adverse conditions such as iron imbalance. Recent studies by our group and others using recombinant SSL proteins have revealed a variety of activities for the SSLs towards molecules involved in innate immunity and remarkably each SSL appears to have more than one function. For example SSL7 blocks IgA binding to its Fc receptor through one domain and inhibits complement C5 through the other domain. The broad specificity of the SSL and superantigen super families highlights how a bacterial protein can provide a modular scaffold for the generation of multiple inhibitors of host immunity and inflammation. Current studies seek to determine the importance of the SSLs, both individually and collectively to staphylococcal infection and disease.