Surface display of the HPV L1 capsid protein by the autotransporter Shigella IcsA

Dan Xu, Xiaofeng Yang, Depu Wang, Jun Yu, Wang Yili

Research output: Contribution to journalArticle

2 Citations (Scopus)

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.
LanguageEnglish
Pages77-82
Number of pages6
JournalJournal of Microbiology
Volume52
Issue number1
DOIs
Publication statusPublished - 1 Jan 2014

Fingerprint

Shigella
Capsid Proteins
Shigella sonnei
Escherichia coli
Proteins
Bacteria
Viral Proteins
Gram-Negative Bacteria
Genes
Actins
Anti-Idiotypic Antibodies
Vaccines
Human papillomavirus HPV L1 protein
Type V Secretion Systems

Keywords

  • autotransporter
  • gene fusion
  • surface expression
  • shigella sonnei

Cite this

Xu, Dan ; Yang, Xiaofeng ; Wang, Depu ; Yu, Jun ; Yili, Wang. / Surface display of the HPV L1 capsid protein by the autotransporter Shigella IcsA. In: Journal of Microbiology. 2014 ; Vol. 52, No. 1. pp. 77-82.
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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.",
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Surface display of the HPV L1 capsid protein by the autotransporter Shigella IcsA. / Xu, Dan; Yang, Xiaofeng; Wang, Depu; Yu, Jun; Yili, Wang.

In: Journal of Microbiology, Vol. 52, No. 1, 01.01.2014, p. 77-82.

Research output: Contribution to journalArticle

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AB - 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.

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