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Yersinia pestis capsular antigen Caf1 is shown to be a β-structural protein that in polymeric form possesses very high conformational stability. Different approaches show that a dimer is the minimal cooperative block of Caf1 adhesin. Caf1 dimer interacts effectively with IL-1 receptors of human macrophage and epithelial cells. The specificity of such interaction is confirmed by the inhibition of IL-1α binding by Caf1. The Caf1 role in pneumonic plague pathogenesis is discussed.
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Abramov et al. (2002) studied this question.
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