A DltE–DltD–DltX interaction network regulates lipoteichoic acid D-alanylation and Lactiplantibacillus plantarum-mediated growth promotion in Drosophila
Abstract
D-alanylation of teichoic acids is a conserved modification of Gram-positive bacterial cell envelopes that modulates resistance to environmental stresses and host interactions. While the cytosolic steps of this pathway are well characterized, the extracellular reactions responsible for transferring D-alanine onto teichoic acids remain poorly understood. Here we investigate the organization of the Dlt machinery in the symbiotic bacterium Lactiplantibacillus plantarum. We determined the 2.3 Å crystal structure of the extracellular catalytic domain of DltD, which adopts an SGNH-hydrolase fold with a conserved Ser-His-Asp catalytic triad. Docking analyses with lipoteichoic acids (LTA) fragments suggest that the glycerol-phosphate backbone of LTA is accommodated along a surface groove leading to the catalytic serine, with conserved residues contributing to substrate positioning. Biochemical measurements further reveal direct interactions between DltD, the acyl-carrier protein DltX, and the LTA esterase DltE. The conserved C-terminal motif of DltX binds DltD and is required for efficient D-alanylation and for L. plantarum-mediated promotion of Drosophila juvenile growth. Together, our findings support a revised model in which DltD, DltE, and DltX form a coordinated extracellular interaction network that dynamically regulates LTA D-alanylation. This work provides new mechanistic insights into the organization of the Dlt machinery and reveals how species-specific adaptations of this conserved pathway contribute to bacterial interactions with the host.
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BibTeX
@article{matos2026dltedltddltx,
title = {{A DltE–DltD–DltX interaction network regulates lipoteichoic acid D-alanylation and Lactiplantibacillus plantarum-mediated growth promotion in Drosophila}},
author = {Renata C Matos and Nikos Nikolopoulos and Quentin Perrier and Xavier Robert and Virginie Gueguen-Chaignon and Hiroto Hirayama and Jean-Pierre Simorre and François Leulier and Christophe Grangeasse and Yann Guerardel and Stéphanie Ravaud},
journal = {Journal of Biological Chemistry},
year = {2026},
month = sep,
doi = {10.1016/j.jbc.2026.113522},
url = {https://hal.science/hal-05749201v1},
note = {CC BY 4.0},
}
RIS
TY - JOUR
TI - A DltE–DltD–DltX interaction network regulates lipoteichoic acid D-alanylation and Lactiplantibacillus plantarum-mediated growth promotion in Drosophila
AU - Renata C Matos
AU - Nikos Nikolopoulos
AU - Quentin Perrier
AU - Xavier Robert
AU - Virginie Gueguen-Chaignon
AU - Hiroto Hirayama
AU - Jean-Pierre Simorre
AU - François Leulier
AU - Christophe Grangeasse
AU - Yann Guerardel
AU - Stéphanie Ravaud
PY - 2026
DA - 2026/09/14
JO - Journal of Biological Chemistry
DO - 10.1016/j.jbc.2026.113522
UR - https://hal.science/hal-05749201v1
AB - D-alanylation of teichoic acids is a conserved modification of Gram-positive bacterial cell envelopes that modulates resistance to environmental stresses and host interactions. While the cytosolic steps of this pathway are well characterized, the extracellular reactions responsible for transferring D-alanine onto teichoic acids remain poorly understood. Here we investigate the organization of the Dlt machinery in the symbiotic bacterium Lactiplantibacillus plantarum. We determined the 2.3 Å crystal structure of the extracellular catalytic domain of DltD, which adopts an SGNH-hydrolase fold with a conserved Ser-His-Asp catalytic triad. Docking analyses with lipoteichoic acids (LTA) fragments suggest that the glycerol-phosphate backbone of LTA is accommodated along a surface groove leading to the catalytic serine, with conserved residues contributing to substrate positioning. Biochemical measurements further reveal direct interactions between DltD, the acyl-carrier protein DltX, and the LTA esterase DltE. The conserved C-terminal motif of DltX binds DltD and is required for efficient D-alanylation and for L. plantarum-mediated promotion of Drosophila juvenile growth. Together, our findings support a revised model in which DltD, DltE, and DltX form a coordinated extracellular interaction network that dynamically regulates LTA D-alanylation. This work provides new mechanistic insights into the organization of the Dlt machinery and reveals how species-specific adaptations of this conserved pathway contribute to bacterial interactions with the host.
SN - 0021-9258
SN - 1083-351X
ER -