ArticleNature communications2024
Structural insights into the transporting and catalyzing mechanism of DltB in LTA D-alanylation.
Article in Nature communications, 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.
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Who cites it
10 citing papers in PubMed, 14 citations in OpenAlex.
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- Kynurenine mediates the chemotherapy-induced intestinal toxicity through modulation of gut microbiota.Nature communications · 2026Article
- Resisting the gallium "Trojan horse": Experimental evolutionary insights into microbial resistance.Gene & protein in disease · 2026Article
- Structural Insights into theBiomolecules · 2025Article
- Dual glycosylation of wall teichoic acid modulates the O-antigen pattern and virulence in serovar 4bmLife · 2025Article
- Acyltransferases that Modify Cell Surface Polymers Across the Membrane.Biochemistry · 2025Review
- Gut commensal Bifidobacterium-derived extracellular vesicles modulate the therapeutic effects of anti-PD-1 in lung cancer.Nature communications · 2025Article
- Gallium Resistance inApplied microbiology (Basel, Switzerland) · 2025Article
- Single-Particle Cryo-EM to Investigate Nonenveloped Virus-Like Particles.Methods in molecular biology (Clifton, N.J.) · 2025Article
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Authors and funding
2 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
DltB, a model member of the Membrane-Bound O-AcylTransferase (MBOAT) superfamily, plays a crucial role in D-alanylation of the lipoteichoic acid (LTA), a significant component of the cell wall of gram-positive bacteria. This process stabilizes the cell wall structure, influences bacterial virulence, and modulates the host immune response. Despite its significance, the role of DltB is not well understood. Through biochemical analysis and cryo-EM imaging, we discover that Streptococcus thermophilus DltB forms a homo-tetramer on the cell membrane. We further visualize DltB in an apo form, in complex with DltC, and in complex with its inhibitor amsacrine (m-AMSA). Each tetramer features a central hole. The C-tunnel of each protomer faces the intratetramer interface and provides access to the periphery membrane. Each protomer binds a DltC without changing the tetrameric organization. A phosphatidylglycerol (PG) molecule in the substrate-binding site may serve as an LTA carrier. The inhibitor m-AMSA bound to the L-tunnel of each protomer blocks the active site. The tetrameric organization of DltB provides a scaffold for catalyzing D-alanyl transfer and regulating the channel opening and closing. Our findings unveil DltB's dual function in the D-alanylation pathway, and provide insight for targeting DltB as a anti-virulence antibiotic.
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