Cloning and expression of outer membrane proteins of Yersinia pestis

  Objective   To clone and express the outer membrane proteins of Yersinia pestis.

  Methods   The genes encoded the outer membrane proteins of Yersinis pestis were amplified by PCR and PCR products were digested by restriction enzymes.Then the restricted fragments were ligated to the prokaryotic expression vector p ET32a and transformed into E.coli.After inducing with 0.1mM IPT G, SDS-PA GE and protein chip were used to detect proteins that were expressed.

  Results   All of the selected genes were expressed in E.coli.with a level of 20-45% of the total bacterial proteins.The purity of expressed products were up to 85%.

  Conclusion   This work settled a foundation for studying the structure and function of the outer membrane proteins Yersinia pestis.