Specific high affinity binding of human interleukin 1 beta by Caf1A usher protein of Yersinia pestis.

Understanding the interaction of Yersinia pestis with the key components of the immune system is important for elucidation of the pathogenesis of bubonic plague, one of the most severe and acute bacterial diseases. Here we report the specific, high affinity binding (Kd = 1.40 x 10(-10) M +/- 0.14 x 10(-10)) of radiolabelled human interleukin 1 beta (hIL-1 beta) to E. coli cells carrying the capsular f1 operon of Y. pestis. Caf1A outer membrane usher protein was isolated to greater than 98% purity. Competition studies with purified Caf1A, together with immunoblotting studies, identified Caf1A as the hIL-1 beta receptor. Competition between Caf1 subunit and hIL-1 beta for the same or an overlapping binding site on Caf1A was demonstrated. Relevance of these results to the pathogenesis of Y. pestis and other Gram negative bacterial pathogens with homologous outer membrane usher proteins is discussed.