Evidence map›Paper›PMID 37469298›Full record

ArticleAngewandte Chemie (International ed. in English)2023

Secretion-Catalyzed Assembly of Protein Biomaterials on a Bacterial Membrane Surface.

Qi Xie, Sea On Lee, Nitya Vissamsetti, Sikao Guo, Margaret E Johnson, Stephen D Fried

Open access · greenAbstract read
PubMed Full text at PMC Publisher
In one paragraph

Article in Angewandte Chemie (International ed. in English), 2023. 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
1.0field-weighted citation impact, top 28% of its field
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, 10 citations in OpenAlex.

  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

6 authors at 1 institution in 1 country.

Qi XieDepartment of Chemistry, Johns Hopkins University, 21218, Baltimore, MD, USA.ORCID 0000-0002-3591-8749
Sea On LeeDepartment of Chemistry, Johns Hopkins University, 21218, Baltimore, MD, USA.
Nitya VissamsettiDepartment of Chemistry, Johns Hopkins University, 21218, Baltimore, MD, USA.
Sikao GuoT. C. Jenkins Department of Biophysics, Johns Hopkins University, 21218, Baltimore, MD, USA.
Margaret E JohnsonT. C. Jenkins Department of Biophysics, Johns Hopkins University, 21218, Baltimore, MD, USA.ORCID 0000-0001-9881-291X
Stephen D FriedDepartment of Chemistry, Johns Hopkins University, 21218, Baltimore, MD, USA.ORCID 0000-0003-2494-2193
Johns Hopkins University · US

Funding

Watching Proteins Fold (or Misfold) in vivo with Mass SpectrometryDP2GM140926 · NIGMS · JOHNS HOPKINS UNIVERSITY · PI FRIED, STEPHEN DAVID · 2020 to 2020
$2.3M
Mechanisms of Protein Self-Assembly Coupled to Membrane Mechanics in the Cell.R35GM133644 · NIGMS · JOHNS HOPKINS UNIVERSITY · PI JOHNSON, MARGARET ELLEN · 2019 to 2023
$2.0M
NIGMS NIH HHS DP2 GM140926NIGMS NIH HHS DP2-GM140926NIGMS NIH HHS R35 GM133644NIGMS NIH HHS R35-GM133644
6 · The paper itself

Abstract

Protein-based biomaterials have played a key role in tissue engineering, and additional exciting applications as self-healing materials and sustainable polymers are emerging. Over the past few decades, recombinant expression and production of various fibrous proteins from microbes have been demonstrated; however, the resulting proteins typically must then be purified and processed by humans to form usable fibers and materials. Here, we show that the Gram-positive bacterium Bacillus subtilis can be programmed to secrete silk through its translocon via an orthogonal signal peptide/peptidase pair. Surprisingly, we discover that this translocation mechanism drives the silk proteins to assemble into fibers spontaneously on the cell surface, in a process we call secretion-catalyzed assembly (SCA). Secreted silk fibers form self-healing hydrogels with minimal processing. Alternatively, the fibers retained on the membrane provide a facile route to create engineered living materials from Bacillus cells. This work provides a blueprint to achieve autonomous assembly of protein biomaterials in useful morphologies directly from microbial factories.

Indexed as

Biocompatible MaterialsSilkCatalysisHumansPolymersTissue EngineeringBiocompatible MaterialsPolymersSilkEngineered Living MaterialsMicrobial BioengineeringProtein BiomaterialsSecretionSilk Fibers

Identifiers

PMID37469298
PMCPMC11619767
OpenAlexW4384820527

What OpenQuestion holds

Textmetadata
LicenceTDM
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 OpenQuestion graph.