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A library of mAbs to the species- and serogroup-specific epitopes of Yersinia pseudotuberculosis serogroups I–VI was developed. These mAbs recognized linear sequential protein epitopes, as shown by ELISA and immunoblotting. Using the mAbs, Y. pseudotuberculosis was found to produce serogroup-specific proteins, whose synthesis was dependent on cultivation temperature. These proteins appeared to be parts of heat-stable O-antigens prepared by heating Y. pseudotuberculosis serogroups I–VI at 100 °C for 2 h, and are responsible for the protein serotype specificity of these bacteria. The high specificity of serogroup- or species-specific mAbs obtained in ELISA suggests that they may be effective for serotyping of Y. pseudotuberculosis strains or differentiation from other pathogenic yersiniae.
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