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TitleThe Cryo-EM STRUCTURE of Renal Amyloid Fibril Suggests Structurally Homogeneous Multiorgan Aggregation in AL Amyloidosis.
Journal, issue, pagesJ Mol Biol, Vol. 435, Issue 18, Page 168215, Year 2023
Publish dateJul 27, 2023
AuthorsSarita Puri / Tim Schulte / Antonio Chaves-Sanjuan / Giulia Mazzini / Serena Caminito / Carlo Pappone / Luigi Anastasia / Paolo Milani / Giampaolo Merlini / Martino Bolognesi / Mario Nuvolone / Giovanni Palladini / Stefano Ricagno /
PubMed AbstractImmunoglobulin light chain amyloidosis (AL) is caused by the aberrant production of amyloidogenic light chains (LC) that accumulate as amyloid deposits in vital organs. Distinct LC sequences in each ...Immunoglobulin light chain amyloidosis (AL) is caused by the aberrant production of amyloidogenic light chains (LC) that accumulate as amyloid deposits in vital organs. Distinct LC sequences in each patient yield distinct amyloid structures. However different tissue microenvironments may also cause identical protein precursors to adopt distinct amyloid structures. To address the impact of the tissue environment on the structural polymorphism of amyloids, we extracted fibrils from the kidney of an AL patient (AL55) whose cardiac amyloid structure was previously determined by our group. Here we show that the 4.0 Å resolution cryo-EM structure of the renal fibril is virtually identical to that reported for the cardiac fibril. These results provide the first structural evidence that LC amyloids independently deposited in different organs of the same AL patient share a common fold.
External linksJ Mol Biol / PubMed:37516426
MethodsEM (helical sym.)
Resolution4.0 Å
Structure data

16780

8cpe

EMDB-16780, PDB-8cpe:
CryoEM structure of AL55 amyloid fibrils extracted from the kidney of an AL amyloidosis patient.
Method: EM (helical sym.) / Resolution: 4.0 Å

Source
  • homo sapiens (human)
KeywordsPROTEIN FIBRIL / Light chains / Amyloid fibrils / AL amyloidosis.

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