Fibril structures of diabetes-related amylin variants reveal a basis for surface-templated assembly

Aggregation of the peptide hormone amylin into amyloid deposits is a pathological hallmark of type-2 diabetes (T2D). While no causal link between T2D and amyloid has been established, the S20G mutation in amylin is associated with early-onset T2D. Here we report cryo-EM structures of amyloid fibrils...

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Published inNature structural & molecular biology Vol. 27; no. 11; pp. 1048 - 1056
Main Authors Gallardo, Rodrigo, Iadanza, Matthew G., Xu, Yong, Heath, George R., Foster, Richard, Radford, Sheena E., Ranson, Neil A.
Format Journal Article
LanguageEnglish
Published New York Nature Publishing Group US 01.11.2020
Nature Publishing Group
Subjects
101/28
14/3
631/45/470/2284
631/535/1258/1259
Age
Agglomeration
Amylin
Amyloid - chemistry
Amyloid - genetics
Amyloid - ultrastructure
Assembly
Biochemistry
Biological Microscopy
Biomedical and Life Sciences
Conformation
Cryoelectron Microscopy
Diabetes
Diabetes mellitus
Diabetes Mellitus, Type 2 - genetics
Diabetes Mellitus, Type 2 - pathology
Fibrils
Humans
Islet Amyloid Polypeptide - chemistry
Islet Amyloid Polypeptide - genetics
Islet Amyloid Polypeptide - ultrastructure
Life Sciences
Membrane Biology
Models, Molecular
Mutation
Point Mutation
Protein Conformation
Protein Structure
β-Amyloid
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Abstract Aggregation of the peptide hormone amylin into amyloid deposits is a pathological hallmark of type-2 diabetes (T2D). While no causal link between T2D and amyloid has been established, the S20G mutation in amylin is associated with early-onset T2D. Here we report cryo-EM structures of amyloid fibrils of wild-type human amylin and its S20G variant. The wild-type fibril structure, solved to 3.6-Å resolution, contains two protofilaments, each built from S-shaped subunits. S20G fibrils, by contrast, contain two major polymorphs. Their structures, solved at 3.9-Å and 4.0-Å resolution, respectively, share a common two-protofilament core that is distinct from the wild-type structure. Remarkably, one polymorph contains a third subunit with another, distinct, cross-β conformation. The presence of two different backbone conformations within the same fibril may explain the increased aggregation propensity of S20G, and illustrates a potential structural basis for surface-templated fibril assembly. Cryo-EM structures of diabetes-related amyloids formed by wild-type human amylin (IAPP) and its S20G variant reveal a mode for surface-templated fibril growth.
AbstractList Aggregation of the peptide hormone amylin into amyloid deposits is a pathological hallmark of type-2 diabetes (T2D). While no causal link between T2D and amyloid has been established, the S20G mutation in amylin is associated with early-onset T2D. Here we report cryo-EM structures of amyloid fibrils of wild-type human amylin and its S20G variant. The wild-type fibril structure, solved to 3.6-Å resolution, contains two protofilaments, each built from S-shaped subunits. S20G fibrils, by contrast, contain two major polymorphs. Their structures, solved at 3.9-Å and 4.0-Å resolution, respectively, share a common two-protofilament core that is distinct from the wild-type structure. Remarkably, one polymorph contains a third subunit with another, distinct, cross-β conformation. The presence of two different backbone conformations within the same fibril may explain the increased aggregation propensity of S20G, and illustrates a potential structural basis for surface-templated fibril assembly.
Aggregation of the peptide hormone amylin into amyloid deposits is a pathological hallmark of type-2 diabetes (T2D). While no causal link between T2D and amyloid has been established, the S20G mutation in amylin is associated with early-onset T2D. Here we report cryo-EM structures of amyloid fibrils of wild-type human amylin and its S20G variant. The wild-type fibril structure, solved to 3.6-Å resolution, contains two protofilaments, each built from S-shaped subunits. S20G fibrils, by contrast, contain two major polymorphs. Their structures, solved at 3.9-Å and 4.0-Å resolution, respectively, share a common two-protofilament core that is distinct from the wild-type structure. Remarkably, one polymorph contains a third subunit with another, distinct, cross-β conformation. The presence of two different backbone conformations within the same fibril may explain the increased aggregation propensity of S20G, and illustrates a potential structural basis for surface-templated fibril assembly.Cryo-EM structures of diabetes-related amyloids formed by wild-type human amylin (IAPP) and its S20G variant reveal a mode for surface-templated fibril growth.
Aggregation of the peptide hormone amylin into amyloid deposits is a pathological hallmark of type-2 diabetes (T2D). While no causal link between T2D and amyloid has been established, the S20G mutation in amylin is associated with early-onset T2D. Here we report cryo-EM structures of amyloid fibrils of wild-type human amylin and its S20G variant. The wild-type fibril structure, solved to 3.6-Å resolution, contains two protofilaments, each built from S-shaped subunits. S20G fibrils, by contrast, contain two major polymorphs. Their structures, solved at 3.9-Å and 4.0-Å resolution, respectively, share a common two-protofilament core that is distinct from the wild-type structure. Remarkably, one polymorph contains a third subunit with another, distinct, cross-β conformation. The presence of two different backbone conformations within the same fibril may explain the increased aggregation propensity of S20G, and illustrates a potential structural basis for surface-templated fibril assembly. Cryo-EM structures of diabetes-related amyloids formed by wild-type human amylin (IAPP) and its S20G variant reveal a mode for surface-templated fibril growth.
Author Xu, Yong
Gallardo, Rodrigo
Foster, Richard
Ranson, Neil A.
Radford, Sheena E.
Iadanza, Matthew G.
Heath, George R.
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Snippet Aggregation of the peptide hormone amylin into amyloid deposits is a pathological hallmark of type-2 diabetes (T2D). While no causal link between T2D and...
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SubjectTerms 101/28
14/3
631/45/470/2284
631/535/1258/1259
Age
Agglomeration
Amylin
Amyloid - chemistry
Amyloid - genetics
Amyloid - ultrastructure
Assembly
Biochemistry
Biological Microscopy
Biomedical and Life Sciences
Conformation
Cryoelectron Microscopy
Diabetes
Diabetes mellitus
Diabetes Mellitus, Type 2 - genetics
Diabetes Mellitus, Type 2 - pathology
Fibrils
Humans
Islet Amyloid Polypeptide - chemistry
Islet Amyloid Polypeptide - genetics
Islet Amyloid Polypeptide - ultrastructure
Life Sciences
Membrane Biology
Models, Molecular
Mutation
Point Mutation
Protein Conformation
Protein Structure
β-Amyloid
Title Fibril structures of diabetes-related amylin variants reveal a basis for surface-templated assembly
URI https://link.springer.com/article/10.1038/s41594-020-0496-3
https://www.ncbi.nlm.nih.gov/pubmed/32929282
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Volume 27
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