Abstract
During their interaction with host cells, the pathogenic Yersinia spp. export a set of proteins known as the Yersinia outer membrane proteins, or Yops. This chapter reviews the work that led to the discovery of the Yops and discusses recent progress made in understanding the expression and function of these proteins. Bacterial infection of the lungs results in pneumonic plague, a form of the disease that is transmissible by aerosolization and that is often fatal. Yersinia enterocolitica is responsible for a variety of human illnesses ranging in severity from mild gastroenteritis to acute terminal ileitis. Various rodents, farm animals, and birds are the normal reservoirs for Y. pseudotuberculosis. The product of yscC shares significant homology with PulD, a protein required for the export of pullulanase by Klebsiella pneumoniae. A number of additional polypeptides (later to be identified as the Yops) were detected in sucrose gradient-purified outer membranes from pYV-containing Y. enterocolitica and Yersinia pseudotuberculosis grown under LCR conditions. The ability of Yersinia strains to induce rounding and detachment of cultured mammalian cells has been referred to as "cytotoxicity". A partial cytotoxic activity is reconstituted if these protein preparations are introduced into HeLa cells by the use of glass carrier beads. This indicates that YopE must enter the cytoplasm of the host cell to be active. Signal transduction is critically involved in a number of cellular host responses to microbial infection.