The gut–brain axis has attracted increasing attention in recent years, fueled by accumulating symptomatic, physiological, and pathological findings. In this study, the aggregation and toxicity of amyloid beta (Aβ), the pathogenic peptide associated with Alzheimer's disease (AD), seeded by FapC amyloid fragments (FapCS) of Pseudomonas aeruginosa that colonizes the gut microbiome through infections are examined. FapCS display favorable binding with Aβ and a catalytic capacity in seeding the peptide amyloidosis. Upon seeding, twisted Aβ fibrils assume a much‐shortened periodicity approximating that of FapC fibrils, accompanied by a 37% sharp rise in the fibrillar diameter, compared with the control. The robust seeding capacity for Aβ by FapCS and the biofilm fragments derived from P. aeruginosa entail abnormal behavior pathology and immunohistology, as well as impaired cognitive function of zebrafish. Together, the data offer the first concrete evidence of structural integration and inheritance in peptide cross‐seeding, a crucial knowledge gap in understanding the pathological correlations between different amyloid diseases. The catalytic role of infectious bacteria in promoting Aβ amyloidosis may be exploited as a potential therapeutic target, while the altered mesoscopic signatures of Aβ fibrils may serve as a prototype for molecular assembly and a biomarker for screening bacterial infections in AD.

中文翻译：

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通过细菌淀粉样蛋白FapC加速淀粉样蛋白β发病机理。

近年来，由于累积了症状，生理和病理学发现，肠脑轴越来越受到关注。在这项研究中，聚集和β淀粉样蛋白（A的毒性β），与阿尔茨海默氏病（AD），由FAPC接种相关的致病性肽的淀粉样蛋白片段（FapCS）铜绿假单胞菌，定殖肠道微生物通过感染检查。FapCS显示有利与A结合β和在接种肽淀粉样变性病的催化能力。一旦接种，扭曲甲β原纤维呈现出多缩短的周期近似于FAPC原纤维伴随着纤维状直径的37％的急剧上升，与对照组相比的。A的强大播种能力FapCS产生的β和源自铜绿假单胞菌的生物膜片段会导致异常的行为病理和免疫组织学，以及斑马鱼的认知功能受损。在一起，这些数据提供了肽交叉播种中结构整合和遗传的第一个具体证据，这是理解不同淀粉样蛋白疾病之间病理相关性的关键知识缺口。传染性细菌在促进催化作用β淀粉样变性可被开发为潜在的治疗靶，而A的改变介观签名β原纤维可以用作原型分子组件和用于在AD筛选细菌感染的生物标记。