ArticleProceedings of the National Academy of Sciences of the United States of America2016
Gram-negative trimeric porins have specific LPS binding sites that are essential for porin biogenesis.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 70 papers.
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70 citing papers in PubMed, 124 citations in OpenAlex.
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- Depth-Resolved Temperature-Dependent Penetration of Polymyxin B in Phospholipids/Lipopolysaccharide Asymmetric Bilayers.ACS omega · 2025Article
- The synergistic role of gut microbiota and RNA in metabolic diseases: mechanisms and therapeutic insights.Frontiers in microbiology · 2025Review
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- Molecular mechanism of phospholipid transport at the bacterial outer membrane interface.Nature communications · 2023Article
- Escherichia coli displays a conserved membrane proteomic response to a range of alcohols.Biotechnology for biofuels and bioproducts · 2023Article
- High-throughput screening of BAM inhibitors in native membrane environment.Nature communications · 2023Article
- Evaluation of copper-induced biomolecular changes in different porin mutants of Escherichia coli W3110 by infrared spectroscopy.Journal of biological physics · 2023Article
10 more citing papers are in PubMed but not listed here.
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Authors and funding
8 authors at 2 institutions in 2 countries.
Funding
Abstract
The outer membrane (OM) of gram-negative bacteria is an unusual asymmetric bilayer with an external monolayer of lipopolysaccharide (LPS) and an inner layer of phospholipids. The LPS layer is rigid and stabilized by divalent cation cross-links between phosphate groups on the core oligosaccharide regions. This means that the OM is robust and highly impermeable to toxins and antibiotics. During their biogenesis, OM proteins (OMPs), which function as transporters and receptors, must integrate into this ordered monolayer while preserving its impermeability. Here we reveal the specific interactions between the trimeric porins of Enterobacteriaceae and LPS. Isolated porins form complexes with variable numbers of LPS molecules, which are stabilized by calcium ions. In earlier studies, two high-affinity sites were predicted to contain groups of positively charged side chains. Mutation of these residues led to the loss of LPS binding and, in one site, also prevented trimerization of the porin, explaining the previously observed effect of LPS mutants on porin folding. The high-resolution X-ray crystal structure of a trimeric porin-LPS complex not only helps to explain the mutagenesis results but also reveals more complex, subtle porin-LPS interactions and a bridging calcium ion.
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