Development and Evaluation of CmeC Subunit Vaccine against Campylobacter jejuni
Ximin Zeng, Fuzhou Xu and Jun Lin*
Department of Animal Science, The University of Tennessee, Knoxville, TN 37996, USA
- *Corresponding Author:
- Dr. Jun Lin
Department of Animal Science
The University of Tennessee 2640 Morgan Circle Drive, Knoxville
TN 37996-4574, USA
E-mail: [email protected]
Received Date: November 30, 2010; Accepted Date: December 30, 2010; Published Date: December 31, 2010
Citation: Zeng X, Xu F, Lin J (2010) Development and Evaluation of CmeC Subunit Vaccine against Campylobacter jejuni. J Vaccines Vaccin 1:112. doi: 10.4172/2157-7560.1000112
Copyright: © 2010 Zeng X, et al. This is an open-access article distributed under the terms of the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original author and source are credited.
Campylobacter jejuni is the leading bacterial cause of human enteritis in many industrialized countries. There is no commercial vaccine against C. jejuni available to date. CmeC is an essential outer membrane component of CmeABC multidrug efflux pump that plays a critical role in antibiotic resistance and in vivo colonization of C. jejuni. CmeC is prevalent in C. jejuni strains and is dramatically induced and immunogenic in vivo. In this study, we analyzed CmeC sequence homology, examined in vitro immune protection of CmeC peptide antibodies, and produced full-length recombinant CmeC (rCmeC) for evaluating immunogenicity and protective efficacy of the CmeC subunit vaccine against C. jejuni using chicken model system. Amino acid sequences of CmeC from 24 diverse C. jejuni strains were determined and subjected to alignment, which revealed that CmeC is highly conserved in C. jejuni with a identity ranging from 97.3% to 100%. CmeC peptide antibodies inhibited the function of CmeABC efflux pump and enhanced susceptibility of C. jejuni to bile salts, the natural antimicrobial present in the intestine. Two full-length rCmeC proteins with N- or C-terminal His tag were produced in E. coli; the N-terminal His-tagged rCmeC with high purity and yield was obtained by single step affinity purification. The purified rCmeC was used in two vaccination trials using a chicken model of C. jejuni infection. Stimulation of CmeC-specific serum IgG responses via oral vaccination required immunization with higher doses of rCmeC (200µg) together with 70µg of mucosal adjuvant mLT (modified E. coli heat-labile enterotoxin). Subcutaneous vaccination of chickens with rCmeC remarkably stimulated both serum IgG and IgA responses. However, CmeC-specific intestinal secretory IgA response was not significantly stimulated regardless of vaccination regimen and the rCmeC vaccination did not confer protection against C. jejuni infection. Together, these findings provide further compelling evidence that CmeC is a promising subunit vaccine candidate against C. jejuni infection. However, the CmeC vaccination regimen should be optimized to enhance CmeC-specific mucosal immune response in the intestine for protection against C. jejuni.