| Yersinia enterocolitica is a Gram-negative enteric pathogen responsible for a number of gastrointestinal disorders and is widely distributed in nature. The bacteria has the ability to multiply in foods at low temperatures. The infections caused by Yersinia enterocolitica are quite normal in many countries, belonging to the global disease. We selected a pathogenic Y. enterocolitica strain, bio-serotype 2/O:9, isolated from China, and compared the immunogenicities and the proteomics with those of another pathogenic Y. enterocolitica strain, bio-serotype 1B/O:8, isolated from Japan. The purpose of this study is observing something differences between high pathogenic strain (bio-serotype 1B/O:8) and low pathogenic one (bio-serotype 2/O:9) in immunogen and proteomics, looking for the reasons of the different pathogenic ability in these aspects.The results showed these two strains had different LPS immune response patterns. Comparison of their Yops also showed differences that could, we speculate, account for their differences in pathogenicity. The major antigens of the two strains eliciting the host immune response were the LPS and membrane proteins, as shown by comparing protein samples with reference and purified preparations. The membrane and whole-cell proteins of both strains were similar; immunoblots showed 35 kDa and perhaps the 10 kDa proteins to be immunogens in both.Compared the immunogenicities of the outer membrane proteins and proteomics of the whole-cell proteins cultured at 25℃and 37℃with these two pathogenic Y. enterocolitica strain by two-dimensional gel electrophoresis. The results showed that the outer membrane protein A (OmpA), C (OmpC), F (OmpF) were the major immunogens for both strains, some proteins located on the bacterium's surface and enzymes involved in energy metabolism also identified as their immunogens. We compared the whole-cell proteins of two strains cultured at 25℃and 37℃respectively, found that parts of the outer membrane proteins (OmpX, OmpF and OmpA) were down regulated when cultured at 37℃, however, some protein subunits (UreA, UreC UreE) involved in urease synthesis were up regulated when grown at 37℃. |