AI Article Synopsis
- The study aimed to enhance the expression of a virulent outer membrane protein, OmpL17, from Leptospira interrogans serovar Lai and test its immunogenicity in rabbits.
- The OmpL17 protein was cloned into a bacterial expression vector, leading to its successful expression and purification.
- High levels of specific antibodies against OmpL17 were generated in rabbits, laying the groundwork for further research into the protein's role in disease and immune response.
Article Abstract
This study was conducted to potentiate the expression of outer membrane protein OmpL17 of the strong virulent L. interrogans serovar Lai and investigate its immunogenicity in rabbits. The OmpL17 was cloned into prokaryotic expression vector pGEX-1lambdaT. The recombination expression plasmid pGEX-OmpL17 was transformed into E. Coli JM109. The GST fused protein GST-OmpL17 was expressed after induction by IPTG, then GST-tag was by thrombin and purified using Bulk GST purification Modules. SDS-PAGE and Western blotting analysis indicated that the molecular weight of GST-OmpL17 and OmpL17 was about 54 KDa and 28 KDa respectively. The outer membrane protein OmpL17 was subcutaneously injected into rabbits and high titre anti-OmpL17 antibody was obtained (1:4896) which could conjugate specifical with OmpL17. In conclusion, OmpL17 and specifical anti-OmpL17 antibody were obtained, which provided an experimental basis for researching pathogenic effect and immunity functions of OmpL17.
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[Expression and immunity reaction of a novel gene OmpL17 of the strong virulent L. interrogans serovar Lai in China].
Sheng Wu Yi Xue Gong Cheng Xue Za Zhi
April 2005
Research Unit of Infection and Immunity, West China Center of Medical Sciences, Sichuan University, Chengdu 610041, China.
Article Synopsis
- The study aimed to enhance the expression of a virulent outer membrane protein, OmpL17, from Leptospira interrogans serovar Lai and test its immunogenicity in rabbits.
- The OmpL17 protein was cloned into a bacterial expression vector, leading to its successful expression and purification.
- High levels of specific antibodies against OmpL17 were generated in rabbits, laying the groundwork for further research into the protein's role in disease and immune response.
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