Cryo-EM structure of anchorless RML prion reveals variations in shared motifs between distinct strains

Forrest Hoyt; Heidi G. Standke; Efrosini Artikis; Cindi L. Schwartz; Bryan Hansen; Kunpeng Li; Andrew G. Hughson; Matteo Manca; Olivia R. Thomas; Gregory J. Raymond; Brent Race; Gerald S. Baron; Byron Caughey; Allison Kraus

doi:10.1038/s41467-022-30458-6

Nature Communications (Jul 2022)

Cryo-EM structure of anchorless RML prion reveals variations in shared motifs between distinct strains

Forrest Hoyt,
Heidi G. Standke,
Efrosini Artikis,
Cindi L. Schwartz,
Bryan Hansen,
Kunpeng Li,
Andrew G. Hughson,
Matteo Manca,
Olivia R. Thomas,
Gregory J. Raymond,
Brent Race,
Gerald S. Baron,
Byron Caughey,
Allison Kraus

Affiliations

Forrest Hoyt: Research Technologies Branch, Rocky Mountain Laboratories, National Institute of Allergy and Infectious Diseases, National Institutes of Health
Heidi G. Standke: Department of Pathology, Case Western Reserve University School of Medicine
Efrosini Artikis: Laboratory of Persistent Viral Diseases, Rocky Mountain Laboratories, National Institute of Allergy and Infectious Diseases, National Institutes of Health
Cindi L. Schwartz: Research Technologies Branch, Rocky Mountain Laboratories, National Institute of Allergy and Infectious Diseases, National Institutes of Health
Bryan Hansen: Research Technologies Branch, Rocky Mountain Laboratories, National Institute of Allergy and Infectious Diseases, National Institutes of Health
Kunpeng Li: Cleveland Center for Membrane and Structural Biology, Case Western Reserve University
Andrew G. Hughson: Laboratory of Persistent Viral Diseases, Rocky Mountain Laboratories, National Institute of Allergy and Infectious Diseases, National Institutes of Health
Matteo Manca: Department of Pathology, Case Western Reserve University School of Medicine
Olivia R. Thomas: Department of Pathology, Case Western Reserve University School of Medicine
Gregory J. Raymond: Laboratory of Persistent Viral Diseases, Rocky Mountain Laboratories, National Institute of Allergy and Infectious Diseases, National Institutes of Health
Brent Race: Laboratory of Persistent Viral Diseases, Rocky Mountain Laboratories, National Institute of Allergy and Infectious Diseases, National Institutes of Health
Gerald S. Baron: Laboratory of Persistent Viral Diseases, Rocky Mountain Laboratories, National Institute of Allergy and Infectious Diseases, National Institutes of Health
Byron Caughey: Laboratory of Persistent Viral Diseases, Rocky Mountain Laboratories, National Institute of Allergy and Infectious Diseases, National Institutes of Health
Allison Kraus: Department of Pathology, Case Western Reserve University School of Medicine

DOI: https://doi.org/10.1038/s41467-022-30458-6
Journal volume & issue: Vol. 13, no. 1
pp. 1 – 7

Abstract

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The authors report the near-atomic structure of the ex vivo aRML prion fibril. The comparison between this structure and the previously solved 263K prion fibril shows that both common and divergent features characterize these prion strains and their respective conformational replication templates.

Published in Nature Communications

ISSN: 2041-1723 (Online)
Publisher: Nature Portfolio
Country of publisher: United Kingdom
LCC subjects: Science
Website: https://www.nature.com/ncomms/

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