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Instruments / Technical Area	Publication Details	Published	Actions
	Ancestral neuronal receptors are bacterial accessory toxins Finaritra Raoelijaona , Joanna Szczepaniak , Adrien Schahl , James E. Bray , Jin Chuan Zhou , Lindsay Baker , Kamel El Omari , Edward Lowe , Yu Shang Low , Chandra M. Rodriguez , Michael J. Landsberg , J. Shaun Lott , Colin Kleanthous , Matthieu Chavent , Martin C. J. Maiden , Elena Seiradake Nature Communications 29 DOI: 10.1038/s41467-026-69246-x Open Access Show Abstract ▼ Abstract: Horizontal gene transfer events were crucial in the emergence of multicellular life. A striking example is the acquisition of Teneurins, putative surface-exposed toxins in bacteria that function as cell adhesion receptors in metazoan neuronal development. Here, we demonstrate the evolutionary relationships between metazoan and bacterial Teneurins. We use cryogenic electron microscopy and bioinformatic analysis to show that bacterial Teneurins harbour a toxic protein in a proteinaceous shell. They are rare but widely distributed across bacterial taxa and are predominantly seen in species with complex social behaviours, suggesting roles in cell-to-cell interaction. This work confirms that metazoan Teneurins are repurposed bacterial toxins that have evolved to be essential mediators of intercellular communication in all advanced nervous systems. Their acquisition was a key event in the evolution of metazoans.	Feb 2026
Scios-Scios at Diamond	SARM1 is a metabolic sensor activated by an increased NMN/NAD+ ratio to trigger axon degeneration Matthew D. Figley , Weixi Gu , Jeffrey D. Nanson , Yun Shi , Yo Sasaki , Katie Cunnea , Alpeshkumar K. Malde , Xinying Jia , Zhenyao Luo , Forhad K. Saikot , Tamim Mosaiab , Veronika Masic , Stephanie Holt , Lauren Hartley-Tassell , Helen Y. Mcguinness , Mohammad K. Manik , Todd Bosanac , Michael J. Landsberg , Philip S. Kerry , Mehdi Mobli , Robert O. Hughes , Jeffrey Milbrandt , Bostjan Kobe , Aaron Diantonio , Thomas Ve Neuron 109, 1118 - 1136.e11 DOI: 10.1016/j.neuron.2021.02.009 Diamond Proposal Number(s): [24981] Show Abstract ▼ Abstract: Axon degeneration is a central pathological feature of many neurodegenerative diseases. Sterile alpha and Toll/interleukin-1 receptor motif-containing 1 (SARM1) is a nicotinamide adenine dinucleotide (NAD+)-cleaving enzyme whose activation triggers axon destruction. Loss of the biosynthetic enzyme NMNAT2, which converts nicotinamide mononucleotide (NMN) to NAD+, activates SARM1 via an unknown mechanism. Using structural, biochemical, biophysical, and cellular assays, we demonstrate that SARM1 is activated by an increase in the ratio of NMN to NAD+ and show that both metabolites compete for binding to the auto-inhibitory N-terminal armadillo repeat (ARM) domain of SARM1. We report structures of the SARM1 ARM domain bound to NMN and of the homo-octameric SARM1 complex in the absence of ligands. We show that NMN influences the structure of SARM1 and demonstrate via mutagenesis that NMN binding is required for injury-induced SARM1 activation and axon destruction. Hence, SARM1 is a metabolic sensor responding to an increased NMN/NAD+ ratio by cleaving residual NAD+, thereby inducing feedforward metabolic catastrophe and axonal demise.	Apr 2021

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