Yet another mysterious and deadly condition may turn out to be nothing more than endotoxin\/LPS overload in disguise. For decades, we have been told that the dreaded so-called “Mad Cow” disease (also known as BSE) can only be caused by a misfolded, infections proteins that accumulate in the brain and cause irreversible damage that is invariably lethal. The study below pours cold water on those claims and calls for a complete revamping of the hypothesis behind the BSE condition. The study demonstrated that the administration of endotoxin\/LPS by itself was enough to reproduce all features of the disease (except the infectious aspects), with the same lethality as the one seen in the experimental groups that received injections with the actual infectious, misfolded, BSE-causing prions. When endotoxin\/LPS as administered together with the prion injections, the effects were synergistic. As the authors state, inflammation may be the original driver of BSE pathology, with the prions being a late effect of the already established systemic inflammatory state caused by endotoxin\/LPS. And last but not least, the fact that endotoxin\/LPS injections caused beta-amyloid accumulation and cognitive deficits strongly suggests that another incurable, progressive and lethal brain condition – Alzheimer’s Disease – is also endotoxin\/LPS\/inflammation-driven.<\/p>\n
https:\/\/doi.org\/10.3390\/ijms26136245<\/a><\/p>\n https:\/\/www.ualberta.ca\/en\/folio\/2025\/12\/u-of-a-led-research-suggests-new-culprit-in-mad-cow-disease.html<\/a><\/p>\n https:\/\/www.sciencealert.com\/prion-like-brain-damage-can-occur-without-infectious-prions-study-finds<\/a><\/p>\n “…We may have been overestimating the role of a pathological class of misfolded protein in neurodegenerative disease. Called prions, these molecules are responsible for conditions such as\u00a0bovine spongiform encephalopathy<\/a>\u00a0or ‘mad cow disease’,\u00a0chronic wasting disease<\/a>\u00a0in deer, and\u00a0Creutzfeldt-Jakob disease<\/a> in humans. A new study in mice has found that some of the hallmarks of prion disease in brain tissue<\/strong><\/span> \u2013 such as the appearance of sponge-like holes, scarring, and accumulation of amyloid plaques<\/a>\u00a0\u2013 can develop even in the complete absence of prions in their infectious configuration<\/strong><\/span>….This finding suggests we have overlooked some of the mechanisms that contribute to prion diseases, and in some cases, even mistaken the underlying cause. It also has implications for prion-like conditions such as\u00a0Alzheimer’s<\/a>,\u00a0Parkinson’s<\/a>, and ALS, in which misfolded proteins are central to irreversible brain damage<\/strong><\/span>.”<\/p>\n