Abstract
Helicobacter pylori is a gram negative pathogen which commonly colonizes in the human gastric mucosa from early childhood and persists throughout life. CagL is a 27-kDa protein that is located at the tip of T4SS pili and highly conserved among pathogenic H. pylori strains. Lactic acid bacteria especially Lactococcus lactis (L. lactis) could serve as an antigen-delivering vehicle for the development of edible vaccine. In this study H. pylori CagL gene was cloned in pAMJ2008 vector and transferred to Lactococcus lactis MG1363 as the host for CagL antigen production. This recombinant bacterium was orally subjected to mice, and the immune response to CagL was evaluated by ELISA. Intracellular expression of CagL protein was confirmed by Western blot analysis. Mucosal immunization of mice with the recombinant L. lactis significantly stimulated CagL-Specific antibodies: IgA, IgG, cytokine IL-17 and IFN-γ. Moreover, the specific anti-CagL IgA response was detected in the feces of immunized mice. These results indicate that CagL of H. pylori was successfully expressed in L. lactis and the recombinant bacteria can be potentially used as an edible vaccine against H. pylori infection.
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