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TitleRelease of frustration drives corneal amyloid disaggregation by brain chaperone.
Journal, issue, pagesCommun Biol, Vol. 6, Issue 1, Page 348, Year 2023
Publish dateMar 30, 2023
AuthorsJia Yi Kimberly Low / Xiangyan Shi / Venkatraman Anandalakshmi / Dawn Neo / Gary Swee Lim Peh / Siew Kwan Koh / Lei Zhou / M K Abdul Rahim / Ketti Boo / JiaXuan Lee / Harini Mohanram / Reema Alag / Yuguang Mu / Jodhbir S Mehta / Konstantin Pervushin /
PubMed AbstractTGFBI-related corneal dystrophy (CD) is characterized by the accumulation of insoluble protein deposits in the corneal tissues, eventually leading to progressive corneal opacity. Here we show that ...TGFBI-related corneal dystrophy (CD) is characterized by the accumulation of insoluble protein deposits in the corneal tissues, eventually leading to progressive corneal opacity. Here we show that ATP-independent amyloid-β chaperone L-PGDS can effectively disaggregate corneal amyloids in surgically excised human cornea of TGFBI-CD patients and release trapped amyloid hallmark proteins. Since the mechanism of amyloid disassembly by ATP-independent chaperones is unknown, we reconstructed atomic models of the amyloids self-assembled from TGFBIp-derived peptides and their complex with L-PGDS using cryo-EM and NMR. We show that L-PGDS specifically recognizes structurally frustrated regions in the amyloids and releases those frustrations. The released free energy increases the chaperone's binding affinity to amyloids, resulting in local restructuring and breakage of amyloids to protofibrils. Our mechanistic model provides insights into the alternative source of energy utilized by ATP-independent disaggregases and highlights the possibility of using these chaperones as treatment strategies for different types of amyloid-related diseases.
External linksCommun Biol / PubMed:36997596 / PubMed Central
MethodsEM (helical sym.) / NMR (solid-state)
Resolution4.9 Å
Structure data

34813

8hia

EMDB-34813, PDB-8hia:
Structure of transforming growth factor beta induced protein (TGFBIp) G623R fibril
Method: EM (helical sym.) / Resolution: 4.9 Å

PDB-8hga:
Monomer structure of transforming growth factor beta induced protein (TGFBIp) G623R fibril
Method: SOLID-STATE NMR

Source
  • homo sapiens (human)
KeywordsPROTEIN FIBRIL / Pathological fibrils / TGFBI related corneal dystrophy

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