ArticleJournal of biomolecular NMR2019
Identification of conformation-selective nanobodies against the membrane protein insertase BamA by an integrated structural biology approach.
Article in Journal of biomolecular NMR, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 23 papers.
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Who cites it
23 citing papers in PubMed.
- Targeting of the Gram-Negative Outer Membrane for Antibiotic Discovery and Potentiation.ACS infectious diseases · 2026Review
- Structural insights into outer membrane protein biogenesis in pathogenic Neisseria.Structure (London, England : 1993) · 2025Article
- Resurfacing promotes antibacterial activity of a lipid A-binding nanobody.Proceedings of the National Academy of Sciences of the United States of America · 2025Article
- Architecture and conformational dynamics of the BAM-SurA holo insertase complex.Science advances · 2025Article
- The discovery and structural basis of two distinct state-dependent inhibitors of BamA.Nature communications · 2024Article
- A whole-cell platform for discovering synthetic cell adhesion molecules in bacteria.Nature communications · 2024Article
- Methods for Engineering Binders to Multi-Pass Membrane Proteins.Bioengineering (Basel, Switzerland) · 2023Review
- Drug Binding to BamA Targets Its Lateral Gate.The journal of physical chemistry. B · 2023Article
- Targeting BAM for Novel Therapeutics against Pathogenic Gram-Negative Bacteria.Antibiotics (Basel, Switzerland) · 2023Review
- Making a chink in their armor: Current and next-generation antimicrobial strategies against the bacterial cell envelope.Advances in microbial physiology · 2023Article
- Computational identification of a systemic antibiotic for gram-negative bacteria.Nature microbiology · 2022Article
- Mechanism of Action of Ribosomally Synthesized and Post-Translationally Modified Peptides.Chemical reviews · 2022Review
- Multivariate mining of an alpaca immune repertoire identifies potent cross-neutralizing SARS-CoV-2 nanobodies.Science advances · 2022Article
- The role of membrane destabilisation and protein dynamics in BAM catalysed OMP folding.Nature communications · 2021Article
- Article
- Allosteric inhibition of LRRK2, where are we now.Biochemical Society transactions · 2020Review
- Structural insight into the formation of lipoprotein-β-barrel complexes.Nature chemical biology · 2020Article
- Targeted Depletion of Bacteria from Mixed Populations by Programmable Adhesion with Antagonistic Competitor Cells.Cell host & microbe · 2020Article
- Role of the lipid bilayer in outer membrane protein folding in Gram-negative bacteria.The Journal of biological chemistry · 2020Review
- Generation of synthetic nanobodies against delicate proteins.Nature protocols · 2020Article
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Authors and funding
8 authors.
Funding
Abstract
The insertase BamA is an essential protein of the bacterial outer membrane. Its 16-stranded transmembrane β-barrel contains a lateral gate as a key functional element. This gate is formed by the C-terminal half of the last β-strand. The BamA barrel was previously found to sample different conformations in aqueous solution, as well as different gate-open, gate-closed, and collapsed conformations in X-ray crystallography and cryo-electron microscopy structures. Here, we report the successful identification of conformation-selective nanobodies that stabilize BamA in specific conformations. While the initial candidate generation and selection protocol was based on established alpaca immunization and phage display selection procedures, the final selection of nanobodies was enhanced by a solution NMR-based screening step to shortlist the targets for crystallization. In this way, three crystal structures of BamA-nanobody complexes were efficiently obtained, showing two types of nanobodies that indeed stabilized BamA in two different conformations, i.e., with open and closed lateral gate, respectively. Then, by correlating the structural data with high resolution NMR spectra, we could for the first time assign the BamA conformational solution ensemble to defined structural states. The new nanobodies will be valuable tools towards understanding the client insertion mechanism of BamA and towards developing improved antibiotics.
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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.