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TitleCryo-EM Observation of AA Amyloid Fibrils in Mouse Model of Systemic AApoAII Amyloidosis.
Journal, issue, pagesJ Mol Biol, Vol. 437, Issue 24, Page 169438, Year 2025
Publish dateSep 11, 2025
AuthorsGiada Andreotti / Keichii Higuchi / Matthias Schmidt / Marcus Fändrich /
PubMed AbstractThe co-deposition of amyloid fibrils from different precursor proteins is a topic of increasing relevance for protein misfolding diseases. Using cryo-electron microscopy (cryo-EM), we here determined ...The co-deposition of amyloid fibrils from different precursor proteins is a topic of increasing relevance for protein misfolding diseases. Using cryo-electron microscopy (cryo-EM), we here determined the structures of two serum amyloid A (SAA) protein-derived amyloid fibril morphologies that were extracted from a mouse strain that is primarily known to be associated with apolipoprotein A-II-derived amyloid fibrils. The two fibril morphologies show the same protomer conformation as in previously reported ex vivo amyloid fibrils from SAA protein but a different relative arrangement of fibril protein stacks. These data establish that serum amyloid A-derived amyloid fibrils share the same fibril protein fold in different mouse strains and disease contexts.
External linksJ Mol Biol / PubMed:40945578
MethodsEM (helical sym.)
Resolution3.5 Å
Structure data

53573

9r4z

EMDB-53573, PDB-9r4z:
Murine AA amyloid fibril morphology III (AA III)
Method: EM (helical sym.) / Resolution: 3.5 Å

Source
  • mus musculus (house mouse)
KeywordsPROTEIN FIBRIL / Amyloid fibril / AA amyloidosis / systemic amyloidosis / AApoAII amyloidosis / misfolfing disease / protein aggregation

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