Antigen 43-mediated autotransporter display, a versatile bacterial cell surface presentation system

Kjaergaard, K., Hasman, H., Schembri, M. A. and Klemm, P. (2002) Antigen 43-mediated autotransporter display, a versatile bacterial cell surface presentation system. Journal of Bacteriology, 184 15: 4197-4204. doi:10.1128/JB.184.15.4197-4204.2002

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Author Kjaergaard, K.
Hasman, H.
Schembri, M. A.
Klemm, P.
Title Antigen 43-mediated autotransporter display, a versatile bacterial cell surface presentation system
Journal name Journal of Bacteriology   Check publisher's open access policy
ISSN 0021-9193
Publication date 2002-08
Sub-type Article (original research)
DOI 10.1128/JB.184.15.4197-4204.2002
Open Access Status File (Publisher version)
Volume 184
Issue 15
Start page 4197
End page 4204
Total pages 8
Place of publication Washington, DC, United States
Publisher American Society for Microbiology
Language eng
Abstract Antigen 43 (Ag43), a self-recognizing outer membrane protein of Escherichia coli, has been converted into an efficient and versatile tool for surface display of foreign protein segments. Ag43 is an autotransporter protein characterized by the feature that all information required for transport to the outer membrane and secretion through the cell envelope is contained within the protein itself. Ag43 consists of two subunits (alpha and beta), where the beta-subunit forms an integral outer membrane translocator to which the alpha-subunit is noncovalently attached. The simplicity of the Ag43 system makes it ideally suited as a surface display scaffold. Here we demonstrate that the Ag43 alpha-module can accommodate and display correctly folded inserts and has the ability to display entire functional protein domains, exemplified by the FimH lectin domain. The presence of heterologous cysteine bridges does not interfere with surface display, and Ag43 chimeras are correctly processed into alpha- and beta-modules, offering optional and easy release of the chimeric alpha-subunits. Furthermore, Ag43 can be displayed in many gram-negative bacteria. This feature is exploited for display of our chimeras in an attenuated Salmonella strain.
Keyword Microbiology
Uropathogenic Escherichia-coli
Gram-negative Bacteria
Aida-i Autotransporter
Cholera-toxin Epitope
Type-1 Fimbriae
Fimh Adhesin
Colony Morphology
Extracellular Transport
Q-Index Code C1
Q-Index Status Provisional Code
Institutional Status Unknown

Document type: Journal Article
Sub-type: Article (original research)
Collections: Excellence in Research Australia (ERA) - Collection
School of Chemistry and Molecular Biosciences
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Citation counts: TR Web of Science Citation Count  Cited 42 times in Thomson Reuters Web of Science Article | Citations
Scopus Citation Count Cited 43 times in Scopus Article | Citations
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Created: Wed, 19 Sep 2007, 15:29:07 EST