Amyotrophic lateral sclerosis (ALS) is a complex neurodegenerative disease characterised by motor neuron loss in the brain, brainstem, and spinal cord. ALS is caused by mutations in more than 50 genes, including OPTN, encoding for optineurin, a ubiquitin-binding protein that regulates inflammatory signalling. It has been hypothesized that ALS-linked optineurin mutations cause protein loss-of-function, leading to dysregulated immune response that could trigger ALS. However, the exact mechanism of disease pathogenesis is still unclear given that optineurin participates in various other cellular functions including autophagy, cell death and others. Since most ALS cases display spinal onset, we characterised the potential neuroinflammatory pathology in the lumbar spinal cord of young adult mice carrying ALS-like optineurin truncation (Optn470T). We assessed if this optineurin mutation is by itself sufficient to induce ALS-like neuropathology, or whether the latter could be provoked by lipopolysaccharide (LPS). We demonstrated an absence of exaggerated neuroinflammation, TDP-43 aggregation and neurodegeneration in the lumbar spinal cords of Optn470T mice for both basal and LPS-stimulated conditions. Our results indicate that optineurin truncation in mice does not induce ALS-like neuropathology in these settings, suggesting that a short-term inflammatory stimulus is insufficient to precipitate the disease. It is still an open question if chronic inflammation or mutation in other ALS-affected genes together with optineurin truncation could uncover the role of optineurin in neuropathology