Helge B. Bode

This study reconstitutes the APD biosynthesis pathway in E. coli to identify the PKS machinery responsible for warhead formation.

The paper develops an in vivo assay called ASCR to determine adenylation domain specificities in NRPS, testing 54 A domains from various organisms and confirming novel cyclic pentapeptides.

This study uses NRPS engineering to generate novel peptides with a pyrrolizixenamide moiety but finds that TE domain specificity limits further diversification.

The paper introduces non-canonical amino acids into non-ribosomal peptides by engineering NRPS systems and performing post-enzymatic chemical synthesis in bacterial culture extracts.

The paper identifies bacterial acyl amides, called stripteamides, as signals controlling nematode development in the Steinernema-Xenorhabdus symbiosis.

The paper develops Indi2GO, an optical reporter system for benchmarking protein-protein interactions using split-indigoidine synthetase, demonstrating its utility in validating PPI tools and NRPS engineering.

The paper studies the evolution of nonribosomal peptides in entomopathogenic bacteria, finding evidence of both neutral drift and natural selection driving structural convergence and toxicity diversification.

This paper describes a Golden Gate assembly method for high-throughput engineering of non-ribosomal peptide synthetases (NRPS) to generate novel peptides and modify natural products.

This paper introduces split inteins to enable modular NRPS engineering, generating 324 hybrid NRPS and over 200 novel peptides through combinatorial transformation.

The paper identifies pseudotetraivprolide from Pseudomonas entomophila, elucidates its biosynthesis, and reveals the function of conserved hypothetical proteins in its production.

The paper identifies xildivaline, a novel peptide deformylase inhibitor produced by Gammaproteobacteria, and elucidates its biosynthesis and structural features.

The paper identifies sphingolipids from a bacterial PKS as mediators of microbiota protection against pathogens in C. elegans.

This study shows that transertion and cell geometry influence the spatial organization of the E. coli nucleoid during growth and antibiotic treatment.

The paper identifies the VelB intrinsically disordered domain's role in promoting selective heterodimer formation and regulating protein stability in fungal development.

This study shows that activating the Yersinia type III secretion system causes large-scale DNA rearrangements in both the virulence plasmid and chromosomal DNA.

This paper uses mutasynthesis to generate stambomycin derivatives by engineering a bacterial strain and leveraging a promiscuous acyl transferase domain, resulting in new analogues with similar or reduced bioactivity.

This study identifies and characterizes XrdM, an amide methyltransferase involved in dithiolopyrrolone antibiotic biosynthesis, and shows it is distinct from DtpM in structure and function.

This study develops new genetic tools for Photorhabdus and Xenorhabdus, including SEVA-based expression vectors and CRISPR/Cpf1 genome editing systems, enabling efficient natural product profiling.

Autoencoder design plus a roughly 24-hour cell-free screen tested 500 candidates over five rounds, finding 30 functional AMPs; six were broad-spectrum with no resistance emerging in E. coli.

This paper introduces guidelines for optimizing type S non-ribosomal peptide synthetases to improve production yields of artificial non-ribosomal peptides.

The paper describes an evolution-inspired method to engineer NRPS by identifying a recombination breakpoint and using it to assemble NRPS fragments for producing a proteasome inhibitor.

The paper introduces synthetic zippers to split and recombine NRPS fragments, enabling the production of novel non-ribosomal peptides at high titres.

This paper identifies a novel melanin biosynthetic pathway in Ustilago maydis involving multiple polyketide synthases and other enzymes, distinct from known fungal melanin pathways.

This paper describes a method to modify and design non-ribosomal peptide synthetases (NRPSs) using a new fusion point in condensation domains to produce peptides, including non-natural amino acids, at high yields.

This study identifies a serotonin receptor in beet armyworms and shows bacterial metabolites inhibit it, leading to immunosuppression.