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Siphoviridae phage tails co-enrich with ex vivo amyloids

Jan-Hannes Schäfer1,2, Robert T O'Neill2, Danielle Grotjahn1

  • 1Department of Integrative Structural and Computational Biology, Scripps Research; La Jolla, CA, USA.

Biorxiv : the Preprint Server for Biology
|June 29, 2026
PubMed

Insights

Researchers found phage tails in amyloid extracts from patients with amyloidosis. This discovery suggests a potential link between bacteriophages and amyloid remodeling, opening avenues for new therapeutic strategies.

Area of Science:

  • Microbiology
  • Structural Biology
  • Biochemistry

Background:

  • Bacteriophages are abundant in the human microbiome, but their role in health and disease is unclear.
  • The human phagome, encompassing all viruses infecting bacteria in the human body, is largely uncharacterized.
  • Amyloidosis involves the misfolding and aggregation of proteins into amyloid fibrils, leading to various diseases.

Purpose of the Study:

  • To investigate the presence and potential role of bacteriophages in human amyloidosis.
  • To explore the structural relationship between phage-derived components and amyloid fibrils.

Main Methods:

  • Cryo-electron microscopy (cryo-EM) analysis of ex vivo amyloid extracts.
  • Automated model building and database searches for structural identification.
  • Analysis of amyloid extracts from patients with lysozyme amyloidosis (ALys) and light-chain amyloidosis (AL).

Main Results:

  • Phage tails, specifically phage tail tube protein (TTP) assemblies, were identified in amyloid extracts.
  • The presence of phage tails suggests they may bind to or be co-purified with amyloid fibrils.
  • While contamination cannot be entirely excluded, the findings point to a potential interaction.

Conclusions:

  • Bacteriophage components may be associated with human amyloidosis.
  • Phage-derived assemblies could play a role in amyloid remodeling.
  • These findings may inform the development of novel therapeutic strategies for amyloidosis.
Keywords:
amyloidosiscryoSPARChelical reconstructionphage

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