Title Surface Display of the HPV L1 Capsid Protein by the Autotransporter Shigella IcsA
Author Dan Xu1,2, Xiaofeng Yang3, Depu Wang1, Jun Yu2, and Yili Wang1*
Address 1Institute of Cancer Research, School of Life Sciences and Technology, Xi’an Jiaotong University, Xi’an, P. R. China, 2Strathclyde Institute of Pharmacy and Biomedical Sciences, University of Strathclyde, Glasgow, UK, 3The First Affiliated Hospital of Xi’an Jiaotong University, Xi’an, P. R. China
Bibliography Journal of Microbiology, 52(1),77–82, 2014,
DOI 10.1007/s12275-014-3235-9
Key Words autotransporter, gene fusion, surface expression, Shigella sonnei
Abstract Autotransporters have become attractive tools for surface expression of foreign proteins in Gram-negative bacteria. In this study, the Shigella autotransporter IcsA, has been exploited to express the human papillomavirus (HPV) type 16 L1 capsid protein in Shigella sonnei and Escherichia coli. The L1 gene was fused in-frame to replace the coding sequence of the IcsA passenger domain that is responsible for actin-based motility. The resultant hybrid protein could be detected by an anti-L1 antibody on the surface of S. sonnei and E. coli. In E. coli, the protein was expressed on the entire surface of the bacterium. In contrast, the protein was detected mainly at one pole of the Shigella bacterium. However, the protein became evenly distributed on the surface of the Shigella bacterium when the icsP gene was removed. Our study demonstrated the possibility of exploiting autotransporters for surface expression of large, heterologous viral proteins, which may be a useful strategy for vaccine development.