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Octopus-inspired triple-engineered bacteria for precision cancer immunotherapy

ABSTRACT: Bacterial cancer therapies face precision and safety challenges, which limit their clinical application. This study presents a triple-engineered Salmonella typhimurium strain (OITE-bacteria), designed for targeted cancer therapy, inspired by octopus biology and leveraging synthetic biology and biomimetic principles. The strain incorporates SpyTag proteins on the outer membrane, allowing covalent attachment of SpyCatcher-fused quadruple RGD peptides to enhance tumor adhesion via integrin αvβ3 interactions. This promotes bacterial enrichment in various solid tumors and lung metastases. Subsequently, Quorum sensing induces expression of strain HtrA protein within tumors, enhancing extracellular polysaccharide-mediated immunogenicity for activating immune cells. Additionally, the bacteria locally release anti-PD1 nanobodies to anti-immunosuppressive. In murine models, OITE-bacteria achieved a ninefold increase in tumor colonization within 12 hours and sustained melanoma growth suppression for over 40 days, with a 100% response rate. This modular approach, integrating safety and efficacy, provides a new strategy in microbial therapeutics for solid tumors.

ORGANISM(S): Mus musculus

PROVIDER: GSE250146 | GEO | 2026/01/01

REPOSITORIES: GEO

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Project description:This study provides comprehensive proteomic profiles from the venom producing posterior salivary glands of Octopus (superorder Octopodiformes) species. A combined transcriptomic and proteomic approach was used to identify 1,703 proteins from the posterior salivary gland of the southern blue ring octopus, Hapalochlaena maculosa and 1,300 proteins from the posterior salivary gland of the southern sand octopus, Octopus kaurna. The two proteomes were broadly similar, clustering of proteins into orthogroups revealed 1,563 of 2,466 clusters were shared between species. Serine proteases were particularly diverse and abundant in both species. Other abundant proteins included a large number of secreted proteins many of which had no known conserved domains, or homology to proteins with known function. Based on homology to known venom proteins, 23 putative toxins were identified in H. maculosa and 24 in O. kaurna. These toxins span nine protein families: CAP (cysteine rich secretory proteins, antigen 5, parthenogenesis related), chitinase, carboxylesterase, DNase, hyaluronidase, metalloprotease, phospholipase, serine protease and tachykinin. Serine proteases were responsible for 70.9% and 86.3% of putative toxin expression in H. maculosa and O. kaurna respectively as determined using intensity based absolute quantification measurements. Phylogenetic analysis of the putative toxin serine proteases revealed a similar suite of diverse proteins present in both species. Venom composition H. maculosa and O. kaurna differ in several key aspects. While O. kaurna expressed the proteinaceous neurotoxin, tachykinin, this was absent from H. maculosa, perhaps reflecting the acquisition of a potent non-proteinaceous neurotoxin, tetrodotoxin (TTX) produced by bacteria in the salivary glands of that species. Dispersal factors particularly hyaluronidase, were disproportionately high in H. maculosa. Chitinase was abundant in both species and is believed to facilitate envenomation in chitinous/crustacean prey. Cephalopods represent a largely unexplored source of novel proteins distinct from all other venomous taxa and are of interest for further inquiry as novel proteinaceous toxins derived from venoms may contribute to pharmaceutical design.

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Octopus-inspired triple-engineered bacteria for precision cancer immunotherapy

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