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<p>Accumulating evidence suggests a link between gut microbiota, host immunity, and Alzheimer’s disease (AD), while specific MHC-II alleles have been associated with disease susceptibility or protection. Here, we applied a computational framework to investigate whether microbial proteins contain amyloid-like motifs capable of interacting with Aβ42 and whether such peptides are differentially presented by distinct MHC-II alleles. We identified an aggregation-prone core within Aβ42 and screened AD-associated gut microbial proteomes to detect homologous peptide motifs. Predicted antigen presentation was evaluated using IEDB, and potential co-aggregation was assessed in silico. We identified microbial amyloid-mimicking peptides predicted to be presented by AD-associated MHC-II alleles, whereas fewer candidate peptides were identified for the protective alleles. Several peptides shared sequence similarity with Aβ42 aggregation motifs and demonstrated predicted structural compatibility for co-aggregation. These findings suggest a potential link between microbial peptide mimicry, antigen presentation, and amyloid biology. This study is computational and hypothesis-generating, providing a systems-level framework for understanding microbiota–immune interactions in AD.</p><p></p>

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Computational identification of amyloid-mimicking microbial peptides with predicted MHC-II presentation relevance to Alzheimer’s disease

  • 期刊论文

  • 出版模式：

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  • 发表日期：

    2026年7月30日

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  • Weichen Gong

摘要

Accumulating evidence suggests a link between gut microbiota, host immunity, and Alzheimer’s disease (AD), while specific MHC-II alleles have been associated with disease susceptibility or protection. Here, we applied a computational framework to investigate whether microbial proteins contain amyloid-like motifs capable of interacting with Aβ42 and whether such peptides are differentially presented by distinct MHC-II alleles. We identified an aggregation-prone core within Aβ42 and screened AD-associated gut microbial proteomes to detect homologous peptide motifs. Predicted antigen presentation was evaluated using IEDB, and potential co-aggregation was assessed in silico. We identified microbial amyloid-mimicking peptides predicted to be presented by AD-associated MHC-II alleles, whereas fewer candidate peptides were identified for the protective alleles. Several peptides shared sequence similarity with Aβ42 aggregation motifs and demonstrated predicted structural compatibility for co-aggregation. These findings suggest a potential link between microbial peptide mimicry, antigen presentation, and amyloid biology. This study is computational and hypothesis-generating, providing a systems-level framework for understanding microbiota–immune interactions in AD.