Evidence map›Paper›PMID 38919015›Full record

ArticleBMB reports2024

Structural stability for surface display of antigen 43 and application to bacterial outer membrane vesicles production.

Gna Ahn, Hyo-Won Yoon, Jae-Won Choi, Woo-Ri Shin, Jiho Min, Yang-Hoon Kim, Ji-Young Ahn

Abstract read
PubMed Full text at PMC
In one paragraph

Article in BMB reports, 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 3 papers.

0numbers the graph read from it
0cells of the map it votes in
3citing papers in PubMed
–field-weighted citation impact
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

3 citing papers in PubMed.

  1. Article
  2. Article
  3. Article
4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

7 authors.

Gna AhnDepartment of Microbiology, Chungbuk National University, Cheongju 28644; Center for Ecology and Environmental Toxicology, Chungbuk National University, Cheongju 28644, Korea.
Hyo-Won YoonDepartment of Microbiology, Chungbuk National University, Cheongju 28644, Korea.
Jae-Won ChoiDepartment of Biopharmaceutical Sciences, Cheongju University, Cheongju 28160, Korea.
Woo-Ri ShinDepartment of Microbiology, Chungbuk National University, Cheongju 28644; Department of Bioengineering, University of Pennsylvania, Philadelphia, PA 19104, USA.
Jiho MinGraduate School of Semiconductor and Chemical Engineering, Jeonbuk National University, Jeonju 54896, Korea.
Yang-Hoon KimDepartment of Microbiology, Chungbuk National University, Cheongju 28644, Korea.
Ji-Young AhnDepartment of Microbiology, Chungbuk National University, Cheongju 28644; Center for Ecology and Environmental Toxicology, Chungbuk National University, Cheongju 28644, Korea.

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

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].

Indexed as

Bacterial Outer MembraneEscherichia coliGreen Fluorescent ProteinsAdhesins, Escherichia coliBacterial Outer Membrane ProteinsEscherichia coli ProteinsProtein FoldingAdhesins, Escherichia coliantigen 43, E coliBacterial Outer Membrane Proteinsenhanced green fluorescent proteinEscherichia coli ProteinsGreen Fluorescent Proteins

Identifiers

PMID38919015
PMCPMC11362141

What Socratic holds

Textmetadata
LicenceCC BY-NC
Read underepoch 390

Registered trials

None linked

Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the Socratic graph.