Cross-Species Amyloid-like Features Shared by Mammalian and Clostridioides difficile Proteins

produces extracellular structures capable of interacting with amyloid-binding dyes, Congo Red-supplemented agar assays were performed. After 48 h of growth, both clinical isolates and a laboratory reference strain exhibited Congo Red-binding colony phenotypes. Because Congo Red binding can arise from several extracellular components and cannot be attributed to a specific protein or sequence motif, these observations should be interpreted cautiously. Taken together, this study presents a motif-based computational framework for identifying candidate amyloidogenic motifs across species and highlights sequence features in bacterial proteomes that may warrant further biochemical and structural investigation. The results should be regarded as hypothesis-generating and provide a basis for future experimental validation of potential amyloid-forming proteins in bacteria.

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Publication Details

Journal
Microorganisms
Published
2026-04-02
DOI
https://doi.org/10.3390/microorganisms14040821
Primary Topic
Alzheimer's disease research and treatments
Type
article
Field-Weighted Citation Impact
0.00

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article

Cross-Species Amyloid-like Features Shared by Mammalian and Clostridioides difficile Proteins

Weichen Gong
Microorganisms
Alzheimer's disease research and treatments
article

Cross-Species Amyloid-like Features Shared by Mammalian and Clostridioides difficile Proteins

Weichen Gong
article en

Abstract

produces extracellular structures capable of interacting with amyloid-binding dyes, Congo Red-supplemented agar assays were performed. After 48 h of growth, both clinical isolates and a laboratory reference strain exhibited Congo Red-binding colony phenotypes. Because Congo Red binding can arise from several extracellular components and cannot be attributed to a specific protein or sequence motif, these observations should be interpreted cautiously. Taken together, this study presents a motif-based computational framework for identifying candidate amyloidogenic motifs across species and highlights sequence features in bacterial proteomes that may warrant further biochemical and structural investigation. The results should be regarded as hypothesis-generating and provide a basis for future experimental validation of potential amyloid-forming proteins in bacteria.

MicroorganismsVol. 14(4)
Tohoku University (JP)
Japan Society for the Promotion of Science
Life in Land
Openalex Percentile: Top 30%
Alzheimer's disease research and treatments
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