Unknown

Dataset Information

0

Reverse engineering synthetic antiviral amyloids.


ABSTRACT: Human amyloids have been shown to interact with viruses and interfere with viral replication. Based on this observation, we employed a synthetic biology approach in which we engineered virus-specific amyloids against influenza A and Zika proteins. Each amyloid shares a homologous aggregation-prone fragment with a specific viral target protein. For influenza we demonstrate that a designer amyloid against PB2 accumulates in influenza A-infected tissue in vivo. Moreover, this amyloid acts specifically against influenza A and its common PB2 polymorphisms, but not influenza B, which lacks the homologous fragment. Our model amyloid demonstrates that the sequence specificity of amyloid interactions has the capacity to tune amyloid-virus interactions while allowing for the flexibility to maintain activity on evolutionary diverging variants.

SUBMITTER: Michiels E 

PROVIDER: S-EPMC7275043 | biostudies-literature | 2020 Jun

REPOSITORIES: biostudies-literature

altmetric image

Publications


Human amyloids have been shown to interact with viruses and interfere with viral replication. Based on this observation, we employed a synthetic biology approach in which we engineered virus-specific amyloids against influenza A and Zika proteins. Each amyloid shares a homologous aggregation-prone fragment with a specific viral target protein. For influenza we demonstrate that a designer amyloid against PB2 accumulates in influenza A-infected tissue in vivo. Moreover, this amyloid acts specifica  ...[more]

Similar Datasets

| S-EPMC8431744 | biostudies-literature
| S-EPMC3716858 | biostudies-literature
2006-03-08 | E-GEOD-4395 | biostudies-arrayexpress
| S-EPMC6340487 | biostudies-literature
| S-EPMC4051496 | biostudies-literature
| S-EPMC9477496 | biostudies-literature
| S-EPMC3497777 | biostudies-literature
2006-03-08 | GSE4395 | GEO
| S-EPMC6003312 | biostudies-literature
| S-EPMC5966606 | biostudies-literature