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Short consensus repeat domain 1 of decay-accelerating factor is required for enterovirus 70 binding
T M Karnauchow1, S Dawe, D M Lublin
1Department of Biochemistry, Microbiology and Immunology, University of Ottawa, Ottawa, Ontario, Canada K1H 8M5.
Journal of Virology
|October 10, 1998
Summary
Enterovirus 70 uses decay-accelerating factor (DAF) for cell entry. Specific sequences in the DAF
Area of Science:
- Virology
- Molecular Biology
- Immunology
Background:
- Human enteroviruses, including Enterovirus 70 (EV70), frequently utilize host cell surface proteins for viral entry.
- Decay-accelerating factor (DAF, also known as CD55) is a known attachment protein for several human enteroviruses.
- Membrane cofactor protein (CD46) is another complement regulatory protein that can serve as a receptor for some viruses.
Purpose of the Study:
- To identify the specific domains of Decay-accelerating factor (DAF) critical for Enterovirus 70 (EV70) binding.
- To compare the DAF binding requirements of EV70 with other DAF-binding enteroviruses.
Main Methods:
- Construction and utilization of chimeric molecules combining short consensus repeat (SCR) domains of DAF and CD46.
- Assessment of EV70 binding to these chimeric DAF/CD46 molecules.
- Comparative analysis of binding characteristics with other DAF-binding enteroviruses.
Main Results:
- Sequences within the SCR1 domain of DAF are essential for EV70 attachment to host cells.
- EV70 binding to DAF is critically dependent on the SCR1 domain.
- Only EV70 and Coxsackievirus A21 among DAF-binding enteroviruses specifically require DAF's SCR1 for interaction.
Conclusions:
- The SCR1 domain of DAF plays a crucial role in mediating EV70 attachment.
- EV70 and Coxsackievirus A21 exhibit a specific tropism for the SCR1 domain of DAF, distinguishing them from other DAF-binding enteroviruses.