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Structure of decay-accelerating factor bound to echovirus 7: a virus-receptor complex
Yongning He1, Feng Lin, Paul R Chipman
1Department of Biological Sciences, Purdue University, West Lafayette, IN 47907-1392, USA.
Summary
Echoviruses bind host cells using decay-accelerating factor (DAF) at a novel location, distinct from other enteroviruses. This unique attachment mechanism suggests a different viral entry pathway for DAF-binding echoviruses.
Area of Science:
- Virology
- Structural Biology
- Immunology
Background:
- Echoviruses, a type of enterovirus within the Picornaviridae family, frequently utilize decay-accelerating factor (DAF) as their cellular receptor.
- DAF is a complement regulatory protein anchored to cell surfaces, crucial for protecting cells against complement-mediated damage.
Purpose of the Study:
- To investigate the structural basis of echovirus-DAF interaction.
- To elucidate the implications of this interaction for viral cell entry mechanisms.
Main Methods:
- Cryo-electron microscopy was employed to reconstruct the structure of echovirus 7 complexed with DAF.
- Analysis of the binding site location on the viral particle.
Main Results:
- DAF-binding regions on echovirus 7 were identified near the icosahedral twofold axes.
- This binding site differs from the 'canyon' typically used by other enteroviruses for receptor interaction.
- The location suggests DAF's role in viral attachment but not necessarily in initiating uncoating.
Conclusions:
- Enteroviruses binding DAF employ a distinct receptor interaction site compared to other enteroviruses.
- This novel binding mode implies a unique cell entry mechanism for DAF-dependent echoviruses, differing from canyon-mediated entry.