Structure of anellovirus-like particles reveal a mechanism for immune evasion

Shu-hao Liou, Rajendra Boggavarapu, Noah R. Cohen, Yue Zhang, Ishwari Sharma, Lynn Zeheb, Nidhi Mukund Acharekar, Hillary D. Rodgers, Saadman Islam, Jared Pitts, Cesar Arze, Harish Swaminathan, Nathan Yozwiak, Tuyen Ong, Roger J. Hajjar, Yong Chang, Kurt A. Swanson () and Simon Delagrave
Additional contact information
Shu-hao Liou: Ring Therapeutics
Rajendra Boggavarapu: Ring Therapeutics
Noah R. Cohen: Ring Therapeutics
Yue Zhang: Ring Therapeutics
Ishwari Sharma: Ring Therapeutics
Lynn Zeheb: Ring Therapeutics
Nidhi Mukund Acharekar: Ring Therapeutics
Hillary D. Rodgers: Ring Therapeutics
Saadman Islam: Ring Therapeutics
Jared Pitts: Ring Therapeutics
Cesar Arze: Ring Therapeutics
Harish Swaminathan: Ring Therapeutics
Nathan Yozwiak: Ring Therapeutics
Tuyen Ong: Ring Therapeutics
Roger J. Hajjar: Ring Therapeutics
Yong Chang: Ring Therapeutics
Kurt A. Swanson: Ring Therapeutics
Simon Delagrave: Ring Therapeutics

Nature Communications, 2024, vol. 15, issue 1, 1-10

Abstract: Abstract Anelloviruses are nonpathogenic viruses that comprise a major portion of the human virome. Despite being ubiquitous in the human population, anelloviruses (ANVs) remain poorly understood. Basic features of the virus, such as the identity of its capsid protein and the structure of the viral particle, have been unclear until now. Here, we use cryogenic electron microscopy to describe the first structure of an ANV-like particle. The particle, formed by 60 jelly roll domain-containing ANV capsid proteins, forms an icosahedral particle core from which spike domains extend to form a salient part of the particle surface. The spike domains come together around the 5-fold symmetry axis to form crown-like features. The base of the spike domain, the P1 subdomain, shares some sequence conservation between ANV strains while a hypervariable region, forming the P2 subdomain, is at the spike domain apex. We propose that this structure renders the particle less susceptible to antibody neutralization by hiding vulnerable conserved domains while exposing highly diverse epitopes as immunological decoys, thereby contributing to the immune evasion properties of anelloviruses. These results shed light on the structure of anelloviruses and provide a framework to understand their interactions with the immune system.

Date: 2024
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DOI: 10.1038/s41467-024-51064-8

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