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Structural stability for surface display of antigen 43 and application to bacterial outer membrane vesicles production
Gna Ahn 1,2,# (Research worker), Hyo-Won Yoon 1,# (Research worker), Jae-Won Choi 3,# (Professor), Woo-Ri Shin 1,4 (Research worker), Jiho Min 5 (Professor), Yang-Hoon Kim 1 (Professor), Ji-Young Ahn 1,* (Professor)
1Department of Microbiology and 2Center for Ecology and Environmental Toxicology, Chungbuk National University,
3Department of Biopharmaceutical Sciences, Cheongju University,
4Department of Bioengineering, University of Pennsylvania,
5Graduate School of Semiconductor and Chemical Engineering, Jeonbuk National University
Abstract
Antigen 43 (Ag43) proteins found on the outer membrane of Escherichia coli, are モ-sheets that fold into a unique cylindrical structure known as a モ-barrel. There are several known structural similarities between bacterial Ag43 autotransporters and physical components; however, the factors that stabilize the barrel and the mechanism for Ag43 passenger domain-mediated translocation across the pore of the モ-barrel remain unclear. In this study, we analyzed Ag43モ-enhanced green fluorescent protein chimeric variants to provide new insights into the autotransporter Ag43 モ-barrel assembly, focusing on the impact of the メ-helical linker domain. Among the chimeric variants, Ag43モ700 showed the highest surface display, which was confirmed through extracellular protease digestion, flow cytometry, and an evaluation of outer membrane vesicles (OMVs). The Ag43モ700 module offered reliable information on stable barrel folding and chimera expression at the exterior of the OMVs.
Abstract, Accepted Manuscript [Submitted on April 15, 2024, Accepted on May 10, 2024]
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