Structure of human Aichi virus and implications for receptor binding

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Ling Zhu1,2, Xiangxi Wang3, Jingshan Ren1

  • 1Division of Structural Biology, University of Oxford, The Henry Wellcome Building for Genomic Medicine, Headington, Oxford OX3 7BN, UK.

Nature Microbiology
|September 6, 2016
PubMed

Insights

Aichi virus (AiV), a kobuvirus causing severe gastroenteritis in children, has a novel structure. Understanding this structure may lead to new antiviral treatments for this significant pathogen.

Area of Science:

  • Virology
  • Structural Biology
  • Picornaviridae

Background:

  • Aichi virus (AiV) is an understudied kobuvirus linked to severe gastroenteritis in young children.
  • High seroprevalence of AiV underscores its public health importance, particularly in developing nations.
  • Currently, no vaccines or effective antiviral therapies exist for AiV infections.

Discussion:

  • The first high-resolution structure of a kobuvirus reveals unique features distinct from enteroviruses and cardioviruses.
  • AiV possesses a shallow surface depression instead of the typical viral canyon, potentially altering receptor interactions.
  • The VP0 capsid protein is not cleaved, resulting in an unusual internal structure within the VP2 barrel.

Key Insights:

  • A novel polyproline helix at the VP1 C terminus, previously unseen in picornaviruses, was identified.
  • This polyproline motif may play a role in host-cell attachment, as a corresponding peptide partially inhibited infectivity.
  • The findings provide a structural basis for understanding AiV pathogenesis and host interactions.

Outlook:

  • The determined AiV structure offers a foundation for identifying cellular receptors and developing targeted antiviral strategies.
  • Further research into the polyproline helix function could reveal new avenues for therapeutic intervention.
  • Structural insights may facilitate the design of novel vaccines against Aichi virus.

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