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Mulard, L.

Publications and source records attributed to Mulard, L..

2 recordsLinked to original sources

Polymerase Evolution Enables Access to Glycosylated Xeno-Nucleic Acids with Expanded Chemical Functionality

Chemical modifications expand the functional repertoire of nucleic acids, but the extent to which complex glycans can be integrated into genetic polymers remains largely unexplored. Glycosylated nucleic acids, including glycoRNAs and bacteriophage genomes, are emerging as key mediators of host-pathogen interactions, yet their synthetic accessibility is severely limited by the inability of polymerases to process substrates bearing simultaneous base and backbone modifications. Here we report the directed evolution of a family B DNA polymerase that enables the synthesis of glycosylated xeno-nucleic acids (XNAs). Using fluorescence-activated droplet sorting, we identified an engineered polymerase, termed G2, that efficiently incorporates nucleotides bearing mono- to trisaccharide base-appendages together with C2 substitutions, yielding XNAs containing up to 30% glycosylated bases. Deep sequencing of >93,000 chimeras reveals that this activity arises from epistatic networks concentrated within catalytic domains. These results establish a route to glycan-encoded nucleic acids and advance polymerase engineering for chemically expanded therapeutics.

synthetic biology↗

ADP-heptose is a pathogen-associated molecular pattern of Shigella flexneri infection

During an infection, the detection of pathogens is mediated through interactions between pathogen-associated molecular patterns (PAMPs) and pathogen recognition receptors. {beta}-Heptose 1,7-bisphosphate ({beta}HBP), a metabolite of the lipopolysaccharide (LPS) biosynthesis pathway, was recently identified as a PAMP of gram-negative bacteria. It was reported that {beta}HBP sensing leads within minutes to oligomerization of the protein TIFA, a mechanism controlling NF-{kappa}B activation and pro-inflammatory gene expression. Here, we compared the ability of chemically synthesized {beta}HBP and Shigella flexneri lysate to induce TIFA oligomerization in epithelial cells. In contrast to lysate, we found that {beta}HBP fails to trigger rapid oligomerization of TIFA. {beta}HBP only induces delayed signaling, suggesting that it has to be processed intracellularly to induce inflammation. By dissecting the LPS biosynthesis pathway with deletion mutants and functional complementation experiments, we show that ADP-D-glycero-{beta}-D-manno-heptose and ADP-L-glycero-{beta}-D-manno-heptose are the bacterial metabolites responsible for rapid TIFA oligomerization, and that they strongly induce interleukin-8 expression during S. flexneri infection. Altogether, our results rule out a major role of {beta}HBP in S. flexneri infection and identify ADP-heptose as a new PAMP.

immunology↗