AI Article Synopsis
- Antigen 43 (Ag43) proteins form a unique β-barrel structure on the outer membrane of Escherichia coli, but the mechanisms for their stability and function are still not fully understood.
- This study focused on Ag43β-enhanced green fluorescent protein chimeras, particularly the Ag43β700 variant, to investigate the role of the α-helical linker domain in barrel assembly.
- The findings revealed that Ag43β700 had improved surface display and provided insights into stable barrel folding and expression at the outer membrane, validated through various experimental methods.
Article Abstract
Antigen 43 (Ag43) proteins, found on the outer membrane of Escherichia coli, are β-sheets that fold into a unique cylindrical structure known as a β-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 domainmediated translocation across the pore of the β-barrel remain unclear. In this study, we analyzed Ag43β-enhanced green fluorescent protein chimeric variants to provide new insights into the autotransporter Ag43β-barrel assembly, focusing on the impact of the α-helical linker domain. Among the chimeric variants, Ag43β700 showed the highest surface display, which was confirmed through extracellular protease digestion, flow cytometry, and an evaluation of outer membrane vesicles (OMVs). The Ag43β700 module offered reliable information on stable barrel folding and chimera expression at the exterior of the OMVs. [BMB Reports 2024; 57(8): 369-374].
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|---|---|
| http://www.ncbi.nlm.nih.gov/pmc/articles/PMC11362141 | PMC |
| http://dx.doi.org/10.5483/BMBRep.2024-0056 | DOI Listing |
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