Skurnik M, Bölin I, Heikkinen H, Piha S, Wolf-Watz H
J Bacteriol. 1984 Jun;158(3):1033-6. doi: 10.1128/jb.158.3.1033-1036.1984.
The autoagglutination of Yersinia enterocolitica was dependent on the presence of the virulence plasmid and on the active growth of bacteria in tissue culture media at 37 degrees C. Cultures with a high initial concentration of bacteria failed to autoagglutinate , indicating that synthesis of new virulence plasmid-associated surface factors was essential for autoagglutination. The synthesis of a plasmid-encoded polypeptide (molecular weight, 240,000), designated P1, that could be dissociated under strongly reducing conditions into subunits of 52,500 daltons was found to be correlated with autoagglutination. Further, a strain of Yersinia pseudotuberculosis [ YPIII ( PIB102 )], which has Tn5 inserted within the structural gene of P1 that prevents the synthesis of P1, failed to autoagglutinate , in contrast to the wild-type strain, strongly indicating that P1 is involved in this phenomenon. It was also found by immunoblotting that in addition to the common response to temperature, the P1 proteins of Y. enterocolitica and Y. pseudotuberculosis were immunologically related.
小肠结肠炎耶尔森菌的自身凝集取决于毒力质粒的存在以及细菌在37℃组织培养基中的活跃生长。初始细菌浓度高的培养物未能发生自身凝集，这表明新的毒力质粒相关表面因子的合成对于自身凝集至关重要。发现一种质粒编码的多肽（分子量240,000），命名为P1，在强还原条件下可解离成52,500道尔顿的亚基，其合成与自身凝集相关。此外，一株假结核耶尔森菌[YPIII (PIB102)]，其Tn5插入到P1的结构基因内，阻止了P1的合成，与野生型菌株相比，未能发生自身凝集，这强烈表明P1参与了这一现象。通过免疫印迹还发现，除了对温度的共同反应外，小肠结肠炎耶尔森菌和假结核耶尔森菌的P1蛋白在免疫上相关。
