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. |